ITGA7: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
 
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Alpha-7 integrin''' is a [[protein]] that in humans is encoded by the ''ITGA7'' [[gene]].<ref name="pmid7607681">{{cite journal | vauthors = Wang W, Wu W, Desai T, Ward DC, Kaufman SJ | title = Localization of the alpha 7 integrin gene (ITGA7) on human chromosome 12q13: clustering of integrin and Hox genes implies parallel evolution of these gene families | journal = Genomics | volume = 26 | issue = 3 | pages = 568–70 | date = Aug 1995 | pmid = 7607681 | pmc =  | doi = 10.1016/0888-7543(95)80176-M }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ITGA7 integrin, alpha 7| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3679| accessdate = }}</ref> Alpha-7 integrin is critical for modulating cell-matrix interactions. Alpha-7 integrin is highly expressed in [[cardiac muscle]], [[skeletal muscle]] and [[smooth muscle]] cells, and localizes to [[sarcomere|Z-disc]] and [[costamere]] structures. Mutations in ''ITGA7'' have been associated with congenital myopathies and [[noncompaction cardiomyopathy]], and altered expression levels of alpha-7 integrin have been identified in various forms of [[muscular dystrophy]].
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
== Structure ==
{{GNF_Protein_box
''ITGA7'' encodes the [[protein]] alpha-7 integrin. Alpha-7 integrin is 128.9 kDa in molecular weight and 1181 [[amino acid]]s in length.<ref>{{cite web|title=Protein sequence of human ITGA7 (Uniprot ID: Q13683)|url=http://www.heartproteome.org/copa/ProteinInfo.aspx?QType=Protein%20ID&QValue=Q13683|website=Cardiac Organellar Protein Atlas Knowledgebase (COPaKB)|accessdate=20 July 2015}}</ref> [[Integrin]]s are heterodimeric [[integral membrane protein]]s composed of an alpha chain and a beta chain. Alpha-7 integrin undergoes [[post-translational modification|post-translational cleavage]] within the [[ectodomain|extracellular domain]] to yield [[disulfide bond|disulfide-linked]] light and heavy chains that join with beta 1 to form an [[integrin]] that binds to the [[extracellular matrix]] [[protein]] laminin-1. The primary binding partners of alpha-7 integrin are laminin-1 ([[LAMA1|alpha1]]-[[LAMB1|beta1]]-[[LAMC1|gamma1]]), laminin-2 ([[LAMA2|alpha2]]-[[LAMB1|beta1]]-[[LAMC1|gamma1]]) and laminin-4 ([[LAMA2|alpha2]]-[[LAMB2|beta2]]-[[LAMC1|gamma1]]).<ref name="ReferenceA">{{cite journal|last1=Cohn|first1=RD|last2=Mayer|first2=U|last3=Saher|first3=G|last4=Herrmann|first4=R|last5=van der Flier|first5=A|last6=Sonnenberg|first6=A|last7=Sorokin|first7=L|last8=Voit|first8=T|title=Secondary reduction of alpha7B integrin in laminin alpha2 deficient congenital muscular dystrophy supports an additional transmembrane link in skeletal muscle.|journal=Journal of the neurological sciences|date=1 March 1999|volume=163|issue=2|pages=140–52|pmid=10371075|doi=10.1016/s0022-510x(99)00012-x}}</ref> Alpha-7/[[ITGB1|beta-1]] is the major [[integrin]] complex expressed in differentiated muscle cells.
| image = 
| image_source = 
| PDB =
| Name = Integrin, alpha 7
| HGNCid = 6143
| Symbol = ITGA7
| AltSymbols =; FLJ25220
| OMIM = 600536
| ECnumber = 
| Homologene = 37592
| MGIid = 102700
| GeneAtlas_image1 = PBB_GE_ITGA7_216331_at_tn.png
| GeneAtlas_image2 = PBB_GE_ITGA7_209663_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0008305 |text = integrin complex}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007156 |text = homophilic cell adhesion}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0007517 |text = muscle development}} {{GNF_GO|id=GO:0008360 |text = regulation of cell shape}} {{GNF_GO|id=GO:0048514 |text = blood vessel morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3679
    | Hs_Ensembl = ENSG00000135424
    | Hs_RefseqProtein = NP_002197
    | Hs_RefseqmRNA = NM_002206
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 54364640
    | Hs_GenLoc_end = 54387949
    | Hs_Uniprot = Q13683
    | Mm_EntrezGene = 16404
    | Mm_Ensembl = ENSMUSG00000025348
    | Mm_RefseqmRNA = NM_008398
    | Mm_RefseqProtein = NP_032424
    | Mm_GenLoc_db =
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 128336767
    | Mm_GenLoc_end = 128361229
    | Mm_Uniprot = Q61738
  }}
}}
'''Integrin, alpha 7''', also known as '''ITGA7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ITGA7 integrin, alpha 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3679| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Splice variants of alpha-7 integrin that differ in both the [[ectodomain|extracellular]] and [[cytoplasm]]ic domains exist in the mouse<ref name="ReferenceB">{{cite journal|last1=Ziober|first1=BL|last2=Vu|first2=MP|last3=Waleh|first3=N|last4=Crawford|first4=J|last5=Lin|first5=CS|last6=Kramer|first6=RH|title=Alternative extracellular and cytoplasmic domains of the integrin alpha 7 subunit are differentially expressed during development.|journal=The Journal of Biological Chemistry|date=15 December 1993|volume=268|issue=35|pages=26773–83|pmid=8253814}}</ref> and are developmentally regulated in mouse and rat muscle tissue.<ref name="ReferenceB"/><ref name="ReferenceC">{{cite journal|last1=Maitra|first1=N|last2=Flink|first2=IL|last3=Bahl|first3=JJ|last4=Morkin|first4=E|title=Expression of alpha and beta integrins during terminal differentiation of cardiomyocytes.|journal=Cardiovascular research|date=September 2000|volume=47|issue=4|pages=715–25|pmid=10974220|doi=10.1016/s0008-6363(00)00140-1}}</ref><ref>{{cite journal|last1=Collo|first1=G|last2=Starr|first2=L|last3=Quaranta|first3=V|title=A new isoform of the laminin receptor integrin alpha 7 beta 1 is developmentally regulated in skeletal muscle.|journal=The Journal of Biological Chemistry|date=5 September 1993|volume=268|issue=25|pages=19019–24|pmid=8360188}}</ref><ref>{{cite journal|last1=Song|first1=WK|last2=Wang|first2=W|last3=Sato|first3=H|last4=Bielser|first4=DA|last5=Kaufman|first5=SJ|title=Expression of alpha 7 integrin cytoplasmic domains during skeletal muscle development: alternate forms, conformational change, and homologies with serine/threonine kinases and tyrosine phosphatases.|journal=Journal of Cell Science|date=December 1993|volume=106|pages=1139–52|pmid=8126096|issue=4}}</ref><ref>{{cite journal|last1=Ziober|first1=BL|last2=Kramer|first2=RH|title=Identification and characterization of the cell type-specific and developmentally regulated alpha7 integrin gene promoter.|journal=The Journal of Biological Chemistry|date=13 September 1996|volume=271|issue=37|pages=22915–22|pmid=8798472}}</ref> The X1/X2 [[alternative splicing]] region lies in the [[ectodomain|extracellular domain]] and alters the ligand binding site; specifically, the conserved homology repeat domains 3 and 4.<ref name="ReferenceB"/> The first identified human transcript contains [[ectodomain|extracellular]] and [[cytoplasm]]ic domains corresponding to the mouse X2 and B variants, respectively. A unique extracellular [[splice variant]] was also identified in human.<ref name="entrez" /><ref>{{cite journal|last1=Leung|first1=E|last2=Lim|first2=SP|last3=Berg|first3=R|last4=Yang|first4=Y|last5=Ni|first5=J|last6=Wang|first6=SX|last7=Krissansen|first7=GW|title=A novel extracellular domain variant of the human integrin alpha 7 subunit generated by alternative intron splicing.|journal=Biochemical and Biophysical Research Communications|date=4 February 1998|volume=243|issue=1|pages=317–25|pmid=9473524|doi=10.1006/bbrc.1998.8092}}</ref> The differentially spliced [[splice variant|variants]] detected in rodents have also been detected in humans. Major [[cytoplasm]]ic, developmentally regulated variants, alpha-7A and alpha-7B, as well as [[ectodomain|extracellular]] [[splice variant|variants]], X1 and X2 were identified in humans. Moreover, the D [[splice variant|variant]], but not the C [[splice variant|variant]] was detected in humans.<ref>{{cite journal|last1=Vignier|first1=N|last2=Moghadaszadeh|first2=B|last3=Gary|first3=F|last4=Beckmann|first4=J|last5=Mayer|first5=U|last6=Guicheney|first6=P|title=Structure, genetic localization, and identification of the cardiac and skeletal muscle transcripts of the human integrin alpha7 gene (ITGA7).|journal=Biochemical and Biophysical Research Communications|date=5 July 1999|volume=260|issue=2|pages=357–64|pmid=10403775|doi=10.1006/bbrc.1999.0916}}</ref>
{{PBB_Summary
| section_title =  
| summary_text = ITGA7 encodes integrin alpha chain 7. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. Alpha chain 7 undergoes post-translational cleavage within the extracellular domain to yield disulfide-linked light and heavy chains that join with beta 1 to form an integrin that binds to the extracellular matrix protein laminin-1. Alpha 7 beta 1 is the major integrin complex expressed in differentiated muscle cells. Splice variants of alpha 7 that differ in both the extracellular and cytoplasmic domains exist in the mouse; however, to date only a single human transcript type has been isolated: it contains extracellular and cytoplasmic domains corresponding to the mouse X2 and B variants, respectively. A unique extracellular splice variant has been identified in human, although it clearly represents a minor species and its biological significance is unclear.<ref name="entrez">{{cite web | title = Entrez Gene: ITGA7 integrin, alpha 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3679| accessdate = }}</ref>
}}


==References==
Alpha-7 integrin is highly expressed in [[striated muscle]], namely [[skeletal muscle|skeletal]] and [[cardiac muscle]], and functions as the major [[laminin]]-binding integrin.<ref>{{cite journal|last1=Kaufman|first1=SJ|last2=Foster|first2=RF|last3=Haye|first3=KR|last4=Faiman|first4=LE|title=Expression of a developmentally regulated antigen on the surface of skeletal and cardiac muscle cells.|journal=The Journal of Cell Biology|date=June 1985|volume=100|issue=6|pages=1977–87|pmid=3889014|doi=10.1083/jcb.100.6.1977|pmc=2113591}}</ref> It was later shown that alpha-7 integrin is also highly expressed in [[smooth muscle]].<ref>{{cite journal|last1=Yao|first1=CC|last2=Breuss|first2=J|last3=Pytela|first3=R|last4=Kramer|first4=RH|title=Functional expression of the alpha 7 integrin receptor in differentiated smooth muscle cells.|journal=Journal of Cell Science|date=July 1997|volume=110|pages=1477–87|pmid=9224765|issue=13}}</ref> The two major [[splice variant]]s of alpha-7 integrin appear to have developmentally regulated expression; alpha-7A integrin is expressed solely in [[skeletal muscle]], however alpha-7B integrin is expressed more loosely in [[striated muscle]] as well as the vasculature.<ref>{{cite journal|last1=Velling|first1=T|last2=Collo|first2=G|last3=Sorokin|first3=L|last4=Durbeej|first4=M|last5=Zhang|first5=H|last6=Gullberg|first6=D|title=Distinct alpha 7A beta 1 and alpha 7B beta 1 integrin expression patterns during mouse development: alpha 7A is restricted to skeletal muscle but alpha 7B is expressed in striated muscle, vasculature, and nervous system.|journal=Developmental Dynamics|date=December 1996|volume=207|issue=4|pages=355–71|pmid=8950511|doi=10.1002/(SICI)1097-0177(199612)207:4<355::AID-AJA1>3.0.CO;2-G}}</ref>
{{reflist|2}}
 
==Further reading==
== Function ==
 
The function of alpha-7 integrin, as is the case for most [[integrin]]s is to mediate cell membrane interactions with [[extracellular matrix]].<ref>{{cite journal|last1=Hynes|first1=RO|title=Integrins: versatility, modulation, and signaling in cell adhesion.|journal=Cell|date=3 April 1992|volume=69|issue=1|pages=11–25|pmid=1555235|doi=10.1016/0092-8674(92)90115-s}}</ref>
 
The alpha-7/beta-1 integrin complex clearly plays a role in the development of [[striated muscle]] and [[smooth muscle]]. Alpha-7/beta-1 integrin promotes the adhesion and motility of [[myoblast]]s, and is likely important in the recruitment of myogenic precursors during muscle differentiation.<ref>{{cite journal|last1=Yao|first1=CC|last2=Ziober|first2=BL|last3=Sutherland|first3=AE|last4=Mendrick|first4=DL|last5=Kramer|first5=RH|title=Laminins promote the locomotion of skeletal myoblasts via the alpha 7 integrin receptor.|journal=Journal of Cell Science|date=December 1996|volume=109|pages=3139–50|pmid=9004048|issue=13}}</ref> It was shown however that beta-1D integrin appears at embryonic day 11 and alpha-7 integrin does not appear until embryonic day 17; thus, beta-1D associates with alternate alpha subunits ([[ITGA5|alpha-5]], [[ITGA6|alpha-6A]]) prior to alpha-7.<ref>{{cite journal|last1=Brancaccio|first1=M|last2=Cabodi|first2=S|last3=Belkin|first3=AM|last4=Collo|first4=G|last5=Koteliansky|first5=VE|last6=Tomatis|first6=D|last7=Altruda|first7=F|last8=Silengo|first8=L|last9=Tarone|first9=G|title=Differential onset of expression of alpha 7 and beta 1D integrins during mouse heart and skeletal muscle development.|journal=Cell adhesion and communication|date=March 1998|volume=5|issue=3|pages=193–205|pmid=9686317|doi=10.3109/15419069809040291}}</ref> In human [[skeletal muscle]], alpha-7 integrin is also developmentally regulated, being first detected at age 2.<ref name="ReferenceA"/>
 
In adult [[striated muscle]] cells, alpha-7 integrin (complexed to [[ITGB1|beta-1 integrin]]) is localized to [[sarcomere|Z-disc]]s and [[costamere]] structures, bound to the four and one half [[LIM domain]] proteins, [[FHL1]] and [[FHL2]].<ref name="ReferenceC"/><ref>{{cite journal|last1=Samson|first1=T|last2=Smyth|first2=N|last3=Janetzky|first3=S|last4=Wendler|first4=O|last5=Müller|first5=JM|last6=Schüle|first6=R|last7=von der Mark|first7=H|last8=von der Mark|first8=K|last9=Wixler|first9=V|title=The LIM-only proteins FHL2 and FHL3 interact with alpha- and beta-subunits of the muscle alpha7beta1 integrin receptor.|journal=The Journal of Biological Chemistry|date=2 July 2004|volume=279|issue=27|pages=28641–52|pmid=15117962|doi=10.1074/jbc.m312894200}}</ref><ref>{{cite journal|last1=Galie|first1=PA|last2=Khalid|first2=N|last3=Carnahan|first3=KE|last4=Westfall|first4=MV|last5=Stegemann|first5=JP|title=Substrate stiffness affects sarcomere and costamere structure and electrophysiological function of isolated adult cardiomyocytes.|journal=Cardiovascular Pathology|date=NaN|volume=22|issue=3|pages=219–27|pmid=23266222|doi=10.1016/j.carpath.2012.10.003|pmc=3610795}}</ref> It has been demonstrated that alpha-7 integrin can be mono-ADP-ribosylated on the cell surface in [[skeletal muscle]] cells;<ref>{{cite journal|last1=Zolkiewska|first1=A|last2=Moss|first2=J|title=The alpha 7 integrin as a target protein for cell surface mono-ADP-ribosylation in muscle cells.|journal=Advances in experimental medicine and biology|date=1997|volume=419|pages=297–303|pmid=9193669}}</ref> however, the functional significance of this modification has not been investigated.
 
Insights into the function of alpha-7 integrin have come from studies employing mouse transgenesis. A mouse expressing a null allele of the ''ITGA7'' [[gene]] are viable, suggesting that alpha-7 integrin is not essential for normal [[myogenesis]]; however, these mice develop a phenotype that resembles [[muscular dystrophy]]. In soleus muscle, there was a significant disruption of myotendinous junctions, variation in the size of fibers, centrally located [[Cell nucleus|nuclei]], [[necrosis]], [[phagocytosis]], and elevated [[serum (blood)|serum]] levels of [[creatine kinase]].<ref>{{cite journal|last1=Mayer|first1=U|last2=Saher|first2=G|last3=Fässler|first3=R|last4=Bornemann|first4=A|last5=Echtermeyer|first5=F|last6=von der Mark|first6=H|last7=Miosge|first7=N|last8=Pöschl|first8=E|last9=von der Mark|first9=K|title=Absence of integrin alpha 7 causes a novel form of muscular dystrophy.|journal=Nature Genetics|date=November 1997|volume=17|issue=3|pages=318–23|pmid=9354797|doi=10.1038/ng1197-318}}</ref> It has also been proposed that alpha-7 integrin and [[SGCG|gamma-sarcoglycan]] have overlapping functions in [[skeletal muscle]]. In support of this, a double knockout of [[SGCG|gamma-sarcoglycan]] and alpha-7 integrin produced a phenotype that was far worse than either knockout alone. Mice died within 1 month of birth and had severe muscle degeneration, suggesting that the roles of these proteins may overlap to maintain the stability of the [[sarcolemma]].<ref>{{cite journal|last1=Allikian|first1=MJ|last2=Hack|first2=AA|last3=Mewborn|first3=S|last4=Mayer|first4=U|last5=McNally|first5=EM|title=Genetic compensation for sarcoglycan loss by integrin alpha7beta1 in muscle.|journal=Journal of Cell Science|date=1 August 2004|volume=117|issue=Pt 17|pages=3821–30|pmid=15252120|doi=10.1242/jcs.01234}}</ref> Moreover, the double knockout of [[dystrophin]] and alpha-7 integrin produced a [[Duchenne muscular dystrophy]]-like phenotype, and demonstrated that alterations in alpha-7 integrin affect the pathological changes observed in [[dystrophin]] deficiencies.<ref>{{cite journal|last1=Guo|first1=C|last2=Willem|first2=M|last3=Werner|first3=A|last4=Raivich|first4=G|last5=Emerson|first5=M|last6=Neyses|first6=L|last7=Mayer|first7=U|title=Absence of alpha 7 integrin in dystrophin-deficient mice causes a myopathy similar to Duchenne muscular dystrophy.|journal=Human Molecular Genetics|date=15 March 2006|volume=15|issue=6|pages=989–98|pmid=16476707|doi=10.1093/hmg/ddl018}}</ref> In support of this notion, [[adeno-associated virus|AAV]] overexpression of ''ITGA7'' in [[skeletal muscle]] of [[Duchenne muscular dystrophy|Duchenne muscular dystrophy (DMD)]] mice showed a significant protective effect against adverse functional parameters associated with DMD, combined with a reversal of these negative features, suggesting that alpha-7 integrin may be a potential therapeutic candidate to treat [[Duchenne muscular dystrophy]].<ref>{{cite journal|last1=Heller|first1=KN|last2=Montgomery|first2=CL|last3=Janssen|first3=PM|last4=Clark|first4=KR|last5=Mendell|first5=JR|last6=Rodino-Klapac|first6=LR|title=AAV-mediated overexpression of human α7 integrin leads to histological and functional improvement in dystrophic mice.|journal=Molecular Therapy|date=March 2013|volume=21|issue=3|pages=520–5|pmid=23319059|doi=10.1038/mt.2012.281|pmc=3589167}}</ref>
 
Studies employing mutant alpha-7 integrin constructs have shown that the [[cytoplasm]]ic tail of alpha-7B integrin is essential for regulation of [[lamellipodia]] formation and regulation of cell mobility regulation via laminin-1/E8 and [[BCAR1|p130(CAS)]]/[[Adapter molecule crk|Crk]] complex formation.<ref>{{cite journal|last1=Mielenz|first1=D|last2=Hapke|first2=S|last3=Pöschl|first3=E|last4=von Der Mark|first4=H|last5=von Der Mark|first5=K|title=The integrin alpha 7 cytoplasmic domain regulates cell migration, lamellipodia formation, and p130CAS/Crk coupling.|journal=The Journal of Biological Chemistry|date=20 April 2001|volume=276|issue=16|pages=13417–26|pmid=11278916|doi=10.1074/jbc.m011481200}}</ref>
 
== Clinical Significance ==
Mutations in ''ITGA7'' have been found in patients with unclassified [[congenital myopathy]].<ref>{{cite journal|last1=Hayashi|first1=YK|last2=Chou|first2=FL|last3=Engvall|first3=E|last4=Ogawa|first4=M|last5=Matsuda|first5=C|last6=Hirabayashi|first6=S|last7=Yokochi|first7=K|last8=Ziober|first8=BL|last9=Kramer|first9=RH|last10=Kaufman|first10=SJ|last11=Ozawa|first11=E|last12=Goto|first12=Y|last13=Nonaka|first13=I|last14=Tsukahara|first14=T|last15=Wang|first15=JZ|last16=Hoffman|first16=EP|last17=Arahata|first17=K|title=Mutations in the integrin alpha7 gene cause congenital myopathy.|journal=Nature Genetics|date=May 1998|volume=19|issue=1|pages=94–7|pmid=9590299|doi=10.1038/ng0598-94}}</ref> Additionally, in patients with severe [[congenital fiber type disproportion]] and [[Noncompaction cardiomyopathy|left ventricular non-compaction cardiomyopathy]], a missense mutation, [[glutamate|Glu]]882[[lysine|Lys]], was identified in ''ITGA7'' along with a missense mutation in ''MYH7B'', both novel disease genes having a synergistic effect on disease severity.<ref>{{cite journal|last1=Esposito|first1=T|last2=Sampaolo|first2=S|last3=Limongelli|first3=G|last4=Varone|first4=A|last5=Formicola|first5=D|last6=Diodato|first6=D|last7=Farina|first7=O|last8=Napolitano|first8=F|last9=Pacileo|first9=G|last10=Gianfrancesco|first10=F|last11=Di Iorio|first11=G|title=Digenic mutational inheritance of the integrin alpha 7 and the myosin heavy chain 7B genes causes congenital myopathy with left ventricular non-compact cardiomyopathy.|journal=Orphanet journal of rare diseases|date=21 June 2013|volume=8|pages=91|pmid=23800289|doi=10.1186/1750-1172-8-91|pmc=3695851}}</ref>
 
Alpha-7B integrin expression has been shown to be significantly decreased at [[sarcolemma|sarcolemmal membranes]] in patients with [[Congenital muscular dystrophy#classification|laminin alpha2 chain-deficient congenital muscular dystrophy]]. Additionally, in [[Duchenne muscular dystrophy]] and [[Becker muscular dystrophy]], the expression of alpha-7B integrin was enhanced.<ref name="ReferenceA"/>
 
== Interactions ==
 
ITGA7 has been shown to [[Protein-protein interaction|interact]] with:
* [[LAMA2|Merosin]]<ref>{{cite journal|last1=Vachon|first1=PH|last2=Xu|first2=H|last3=Liu|first3=L|last4=Loechel|first4=F|last5=Hayashi|first5=Y|last6=Arahata|first6=K|last7=Reed|first7=JC|last8=Wewer|first8=UM|last9=Engvall|first9=E|title=Integrins (alpha7beta1) in muscle function and survival. Disrupted expression in merosin-deficient congenital muscular dystrophy.|journal=The Journal of Clinical Investigation|date=1 October 1997|volume=100|issue=7|pages=1870–81|pmid=9312189|doi=10.1172/jci119716|pmc=508374}}</ref>
* [[ITGB1]]<ref>{{cite journal|last1=Hodges|first1=BL|last2=Hayashi|first2=YK|last3=Nonaka|first3=I|last4=Wang|first4=W|last5=Arahata|first5=K|last6=Kaufman|first6=SJ|title=Altered expression of the alpha7beta1 integrin in human and murine muscular dystrophies.|journal=Journal of Cell Science|date=November 1997|volume=110|pages=2873–81|pmid=9427295|issue=22}}</ref><ref>{{cite journal|last1=Vachon|first1=PH|last2=Xu|first2=H|last3=Liu|first3=L|last4=Loechel|first4=F|last5=Hayashi|first5=Y|last6=Arahata|first6=K|last7=Reed|first7=JC|last8=Wewer|first8=UM|last9=Engvall|first9=E|title=Integrins (alpha7beta1) in muscle function and survival. Disrupted expression in merosin-deficient congenital muscular dystrophy.|journal=The Journal of Clinical Investigation|date=1 October 1997|volume=100|issue=7|pages=1870–81|pmid=9312189|doi=10.1172/jci119716|pmc=508374}}</ref>
* [[FHL2]]<ref name=pmid15117962>{{cite journal | vauthors = Samson T, Smyth N, Janetzky S, Wendler O, Müller JM, Schüle R, von der Mark H, von der Mark K, Wixler V | title = The LIM-only proteins FHL2 and FHL3 interact with alpha- and beta-subunits of the muscle alpha7beta1 integrin receptor | language =  | journal = J. Biol. Chem. | volume = 279 | issue = 27 | pages = 28641–52 | date = Jul 2004 | pmid = 15117962 | doi = 10.1074/jbc.M312894200 }}</ref> and
* [[FHL3]].<ref name=pmid15117962/>
 
== See also ==
* [[Congenital muscular dystrophy]]
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal | vauthors = Fornaro M, Languino LR | title = Alternatively spliced variants: a new view of the integrin cytoplasmic domain | journal = Matrix Biol. | volume = 16 | issue = 4 | pages = 185–93 | year = 1998 | pmid = 9402008 | doi = 10.1016/S0945-053X(97)90007-X }}
| citations =
*{{cite journal | vauthors = Song WK, Wang W, Foster RF, Bielser DA, Kaufman SJ | title = H36-alpha 7 is a novel integrin alpha chain that is developmentally regulated during skeletal myogenesis | journal = J. Cell Biol. | volume = 117 | issue = 3 | pages = 643–57 | year = 1992 | pmid = 1315319 | pmc = 2289453 | doi = 10.1083/jcb.117.3.643 }}
*{{cite journal | author=Fornaro M, Languino LR |title=Alternatively spliced variants: a new view of the integrin cytoplasmic domain. |journal=Matrix Biol. |volume=16 |issue= 4 |pages= 185-93 |year= 1998 |pmid= 9402008 |doi= }}
*{{cite journal | vauthors = Kramer RH, Vu MP, Cheng YF, Ramos DM, Timpl R, Waleh N | title = Laminin-binding integrin alpha 7 beta 1: functional characterization and expression in normal and malignant melanocytes | journal = Cell Regul. | volume = 2 | issue = 10 | pages = 805–17 | year = 1992 | pmid = 1839357 | pmc = 361876 | doi = 10.1091/mbc.2.10.805 }}
*{{cite journal | author=Song WK, Wang W, Foster RF, ''et al.'' |title=H36-alpha 7 is a novel integrin alpha chain that is developmentally regulated during skeletal myogenesis. |journal=J. Cell Biol. |volume=117 |issue= 3 |pages= 643-57 |year= 1992 |pmid= 1315319 |doi= }}
*{{cite journal | vauthors = Song WK, Wang W, Sato H, Bielser DA, Kaufman SJ | title = Expression of alpha 7 integrin cytoplasmic domains during skeletal muscle development: alternate forms, conformational change, and homologies with serine/threonine kinases and tyrosine phosphatases | journal = J. Cell Sci. | volume = 106 | issue = 4 | pages = 1139–52 | year = 1994 | pmid = 8126096 | doi =  }}
*{{cite journal | author=Kramer RH, Vu MP, Cheng YF, ''et al.'' |title=Laminin-binding integrin alpha 7 beta 1: functional characterization and expression in normal and malignant melanocytes. |journal=Cell Regul. |volume=2 |issue= 10 |pages= 805-17 |year= 1992 |pmid= 1839357 |doi= }}
*{{cite journal | vauthors = Ziober BL, Vu MP, Waleh N, Crawford J, Lin CS, Kramer RH | title = Alternative extracellular and cytoplasmic domains of the integrin alpha 7 subunit are differentially expressed during development | journal = J. Biol. Chem. | volume = 268 | issue = 35 | pages = 26773–83 | year = 1994 | pmid = 8253814 | doi =  }}
*{{cite journal | author=Wang W, Wu W, Desai T, ''et al.'' |title=Localization of the alpha 7 integrin gene (ITGA7) on human chromosome 12q13: clustering of integrin and Hox genes implies parallel evolution of these gene families. |journal=Genomics |volume=26 |issue= 3 |pages= 568-70 |year= 1995 |pmid= 7607681 |doi=  }}
*{{cite journal | vauthors = Martin PT, Kaufman SJ, Kramer RH, Sanes JR | title = Synaptic integrins in developing, adult, and mutant muscle: selective association of alpha1, alpha7A, and alpha7B integrins with the neuromuscular junction | journal = Dev. Biol. | volume = 174 | issue = 1 | pages = 125–39 | year = 1996 | pmid = 8626012 | doi = 10.1006/dbio.1996.0057 }}
*{{cite journal | author=Song WK, Wang W, Sato H, ''et al.'' |title=Expression of alpha 7 integrin cytoplasmic domains during skeletal muscle development: alternate forms, conformational change, and homologies with serine/threonine kinases and tyrosine phosphatases. |journal=J. Cell. Sci. |volume=106 ( Pt 4) |issue= |pages= 1139-52 |year= 1994 |pmid= 8126096 |doi=  }}
*{{cite journal | vauthors = Ziober BL, Chen Y, Kramer RH | title = The laminin-binding activity of the alpha 7 integrin receptor is defined by developmentally regulated splicing in the extracellular domain | journal = Mol. Biol. Cell | volume = 8 | issue = 9 | pages = 1723–34 | year = 1997 | pmid = 9307969 | pmc = 305732 | doi = 10.1091/mbc.8.9.1723 }}
*{{cite journal | author=Ziober BL, Vu MP, Waleh N, ''et al.'' |title=Alternative extracellular and cytoplasmic domains of the integrin alpha 7 subunit are differentially expressed during development. |journal=J. Biol. Chem. |volume=268 |issue= 35 |pages= 26773-83 |year= 1994 |pmid= 8253814 |doi= }}
*{{cite journal | vauthors = Basora N, Vachon PH, Herring-Gillam FE, Perreault N, Beaulieu JF | title = Relation between integrin alpha7Bbeta1 expression in human intestinal cells and enterocytic differentiation | journal = Gastroenterology | volume = 113 | issue = 5 | pages = 1510–21 | year = 1997 | pmid = 9352853 | doi = 10.1053/gast.1997.v113.pm9352853 }}
*{{cite journal | author=Martin PT, Kaufman SJ, Kramer RH, Sanes JR |title=Synaptic integrins in developing, adult, and mutant muscle: selective association of alpha1, alpha7A, and alpha7B integrins with the neuromuscular junction. |journal=Dev. Biol. |volume=174 |issue= 1 |pages= 125-39 |year= 1996 |pmid= 8626012 |doi= 10.1006/dbio.1996.0057 }}
*{{cite journal | vauthors = Mayer U, Saher G, Fässler R, Bornemann A, Echtermeyer F, von der Mark H, Miosge N, Pöschl E, von der Mark K | title = Absence of integrin alpha 7 causes a novel form of muscular dystrophy | journal = Nat. Genet. | volume = 17 | issue = 3 | pages = 318–23 | year = 1997 | pmid = 9354797 | doi = 10.1038/ng1197-318 }}
*{{cite journal | author=Ziober BL, Chen Y, Kramer RH |title=The laminin-binding activity of the alpha 7 integrin receptor is defined by developmentally regulated splicing in the extracellular domain. |journal=Mol. Biol. Cell |volume=8 |issue= 9 |pages= 1723-34 |year= 1997 |pmid= 9307969 |doi= }}
*{{cite journal | vauthors = Leung E, Lim SP, Berg R, Yang Y, Ni J, Wang SX, Krissansen GW | title = A novel extracellular domain variant of the human integrin alpha 7 subunit generated by alternative intron splicing | journal = Biochem. Biophys. Res. Commun. | volume = 243 | issue = 1 | pages = 317–25 | year = 1998 | pmid = 9473524 | doi = 10.1006/bbrc.1998.8092 }}
*{{cite journal | author=Basora N, Vachon PH, Herring-Gillam FE, ''et al.'' |title=Relation between integrin alpha7Bbeta1 expression in human intestinal cells and enterocytic differentiation. |journal=Gastroenterology |volume=113 |issue= 5 |pages= 1510-21 |year= 1997 |pmid= 9352853 |doi= }}
*{{cite journal | vauthors = Zolkiewska A, Thompson WC, Moss J | title = Interaction of integrin alpha 7 beta 1 in C2C12 myotubes and in solution with laminin | journal = Exp. Cell Res. | volume = 240 | issue = 1 | pages = 86–94 | year = 1998 | pmid = 9570924 | doi = 10.1006/excr.1998.4002 }}
*{{cite journal | author=Mayer U, Saher G, Fässler R, ''et al.'' |title=Absence of integrin alpha 7 causes a novel form of muscular dystrophy. |journal=Nat. Genet. |volume=17 |issue= 3 |pages= 318-23 |year= 1997 |pmid= 9354797 |doi= 10.1038/ng1197-318 }}
*{{cite journal | vauthors = Hayashi YK, Chou FL, Engvall E, Ogawa M, Matsuda C, Hirabayashi S, Yokochi K, Ziober BL, Kramer RH, Kaufman SJ, Ozawa E, Goto Y, Nonaka I, Tsukahara T, Wang JZ, Hoffman EP, Arahata K | title = Mutations in the integrin alpha7 gene cause congenital myopathy | journal = Nat. Genet. | volume = 19 | issue = 1 | pages = 94–7 | year = 1998 | pmid = 9590299 | doi = 10.1038/ng0598-94 }}
*{{cite journal | author=Leung E, Lim SP, Berg R, ''et al.'' |title=A novel extracellular domain variant of the human integrin alpha 7 subunit generated by alternative intron splicing. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 1 |pages= 317-25 |year= 1998 |pmid= 9473524 |doi= 10.1006/bbrc.1998.8092 }}
*{{cite journal | vauthors = Vignier N, Moghadaszadeh B, Gary F, Beckmann J, Mayer U, Guicheney P | title = Structure, genetic localization, and identification of the cardiac and skeletal muscle transcripts of the human integrin alpha7 gene (ITGA7) | journal = Biochem. Biophys. Res. Commun. | volume = 260 | issue = 2 | pages = 357–64 | year = 1999 | pmid = 10403775 | doi = 10.1006/bbrc.1999.0916 }}
*{{cite journal | author=Zolkiewska A, Thompson WC, Moss J |title=Interaction of integrin alpha 7 beta 1 in C2C12 myotubes and in solution with laminin. |journal=Exp. Cell Res. |volume=240 |issue= 1 |pages= 86-94 |year= 1998 |pmid= 9570924 |doi= 10.1006/excr.1998.4002 }}
*{{cite journal | vauthors = Tachibana I, Hemler ME | title = Role of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance | journal = J. Cell Biol. | volume = 146 | issue = 4 | pages = 893–904 | year = 1999 | pmid = 10459022 | pmc = 2156130 | doi = 10.1083/jcb.146.4.893 }}
*{{cite journal | author=Hayashi YK, Chou FL, Engvall E, ''et al.'' |title=Mutations in the integrin alpha7 gene cause congenital myopathy. |journal=Nat. Genet. |volume=19 |issue= 1 |pages= 94-7 |year= 1998 |pmid= 9590299 |doi= 10.1038/ng0598-94 }}
*{{cite journal | vauthors = Schöber S, Mielenz D, Echtermeyer F, Hapke S, Pöschl E, von der Mark H, Moch H, von der Mark K | title = The role of extracellular and cytoplasmic splice domains of alpha7-integrin in cell adhesion and migration on laminins | journal = Exp. Cell Res. | volume = 255 | issue = 2 | pages = 303–13 | year = 2000 | pmid = 10694445 | doi = 10.1006/excr.2000.4806 }}
*{{cite journal | author=Vignier N, Moghadaszadeh B, Gary F, ''et al.'' |title=Structure, genetic localization, and identification of the cardiac and skeletal muscle transcripts of the human integrin alpha7 gene (ITGA7). |journal=Biochem. Biophys. Res. Commun. |volume=260 |issue= 2 |pages= 357-64 |year= 1999 |pmid= 10403775 |doi= 10.1006/bbrc.1999.0916 }}
*{{cite journal | vauthors = Wixler V, Geerts D, Laplantine E, Westhoff D, Smyth N, Aumailley M, Sonnenberg A, Paulsson M | title = The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes | journal = J. Biol. Chem. | volume = 275 | issue = 43 | pages = 33669–78 | year = 2000 | pmid = 10906324 | doi = 10.1074/jbc.M002519200 }}
*{{cite journal | author=Tachibana I, Hemler ME |title=Role of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance. |journal=J. Cell Biol. |volume=146 |issue= 4 |pages= 893-904 |year= 1999 |pmid= 10459022 |doi= }}
*{{cite journal | vauthors = Burkin DJ, Kim JE, Gu M, Kaufman SJ | title = Laminin and alpha7beta1 integrin regulate agrin-induced clustering of acetylcholine receptors | journal = J. Cell Sci. | volume = 113 | issue = 16 | pages = 2877–86 | year = 2000 | pmid = 10910772 | doi = }}
*{{cite journal | author=Schöber S, Mielenz D, Echtermeyer F, ''et al.'' |title=The role of extracellular and cytoplasmic splice domains of alpha7-integrin in cell adhesion and migration on laminins. |journal=Exp. Cell Res. |volume=255 |issue= 2 |pages= 303-13 |year= 2000 |pmid= 10694445 |doi= 10.1006/excr.2000.4806 }}
*{{cite journal | vauthors = Vizirianakis IS, Yao CC, Chen Y, Ziober BL, Tsiftsoglou AS, Kramer RH | title = Transfection of MCF-7 carcinoma cells with human integrin alpha7 cDNA promotes adhesion to laminin | journal = Arch. Biochem. Biophys. | volume = 385 | issue = 1 | pages = 108–16 | year = 2001 | pmid = 11361006 | doi = 10.1006/abbi.2000.2134 }}
*{{cite journal | author=Wixler V, Geerts D, Laplantine E, ''et al.'' |title=The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes. |journal=J. Biol. Chem. |volume=275 |issue= 43 |pages= 33669-78 |year= 2000 |pmid= 10906324 |doi= 10.1074/jbc.M002519200 }}
*{{cite journal | author=Burkin DJ, Kim JE, Gu M, Kaufman SJ |title=Laminin and alpha7beta1 integrin regulate agrin-induced clustering of acetylcholine receptors. |journal=J. Cell. Sci. |volume=113 ( Pt 16) |issue=  |pages= 2877-86 |year= 2000 |pmid= 10910772 |doi=  }}
*{{cite journal  | author=Vizirianakis IS, Yao CC, Chen Y, ''et al.'' |title=Transfection of MCF-7 carcinoma cells with human integrin alpha7 cDNA promotes adhesion to laminin. |journal=Arch. Biochem. Biophys. |volume=385 |issue= 1 |pages= 108-16 |year= 2001 |pmid= 11361006 |doi= 10.1006/abbi.2000.2134 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
== External links ==
{{WikiDoc Sources}}
*[http://cmkb.cellmigration.org/report.cgi?report=orth_overview&gene_id=3679 ITGA7] Info with links in the [http://www.cellmigration.org/index.shtml Cell Migration Gateway]
 
{{Integrins}}
 
[[Category:Integrins]]

Latest revision as of 20:07, 8 November 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Alpha-7 integrin is a protein that in humans is encoded by the ITGA7 gene.[1][2] Alpha-7 integrin is critical for modulating cell-matrix interactions. Alpha-7 integrin is highly expressed in cardiac muscle, skeletal muscle and smooth muscle cells, and localizes to Z-disc and costamere structures. Mutations in ITGA7 have been associated with congenital myopathies and noncompaction cardiomyopathy, and altered expression levels of alpha-7 integrin have been identified in various forms of muscular dystrophy.

Structure

ITGA7 encodes the protein alpha-7 integrin. Alpha-7 integrin is 128.9 kDa in molecular weight and 1181 amino acids in length.[3] Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. Alpha-7 integrin undergoes post-translational cleavage within the extracellular domain to yield disulfide-linked light and heavy chains that join with beta 1 to form an integrin that binds to the extracellular matrix protein laminin-1. The primary binding partners of alpha-7 integrin are laminin-1 (alpha1-beta1-gamma1), laminin-2 (alpha2-beta1-gamma1) and laminin-4 (alpha2-beta2-gamma1).[4] Alpha-7/beta-1 is the major integrin complex expressed in differentiated muscle cells.

Splice variants of alpha-7 integrin that differ in both the extracellular and cytoplasmic domains exist in the mouse[5] and are developmentally regulated in mouse and rat muscle tissue.[5][6][7][8][9] The X1/X2 alternative splicing region lies in the extracellular domain and alters the ligand binding site; specifically, the conserved homology repeat domains 3 and 4.[5] The first identified human transcript contains extracellular and cytoplasmic domains corresponding to the mouse X2 and B variants, respectively. A unique extracellular splice variant was also identified in human.[2][10] The differentially spliced variants detected in rodents have also been detected in humans. Major cytoplasmic, developmentally regulated variants, alpha-7A and alpha-7B, as well as extracellular variants, X1 and X2 were identified in humans. Moreover, the D variant, but not the C variant was detected in humans.[11]

Alpha-7 integrin is highly expressed in striated muscle, namely skeletal and cardiac muscle, and functions as the major laminin-binding integrin.[12] It was later shown that alpha-7 integrin is also highly expressed in smooth muscle.[13] The two major splice variants of alpha-7 integrin appear to have developmentally regulated expression; alpha-7A integrin is expressed solely in skeletal muscle, however alpha-7B integrin is expressed more loosely in striated muscle as well as the vasculature.[14]

Function

The function of alpha-7 integrin, as is the case for most integrins is to mediate cell membrane interactions with extracellular matrix.[15]

The alpha-7/beta-1 integrin complex clearly plays a role in the development of striated muscle and smooth muscle. Alpha-7/beta-1 integrin promotes the adhesion and motility of myoblasts, and is likely important in the recruitment of myogenic precursors during muscle differentiation.[16] It was shown however that beta-1D integrin appears at embryonic day 11 and alpha-7 integrin does not appear until embryonic day 17; thus, beta-1D associates with alternate alpha subunits (alpha-5, alpha-6A) prior to alpha-7.[17] In human skeletal muscle, alpha-7 integrin is also developmentally regulated, being first detected at age 2.[4]

In adult striated muscle cells, alpha-7 integrin (complexed to beta-1 integrin) is localized to Z-discs and costamere structures, bound to the four and one half LIM domain proteins, FHL1 and FHL2.[6][18][19] It has been demonstrated that alpha-7 integrin can be mono-ADP-ribosylated on the cell surface in skeletal muscle cells;[20] however, the functional significance of this modification has not been investigated.

Insights into the function of alpha-7 integrin have come from studies employing mouse transgenesis. A mouse expressing a null allele of the ITGA7 gene are viable, suggesting that alpha-7 integrin is not essential for normal myogenesis; however, these mice develop a phenotype that resembles muscular dystrophy. In soleus muscle, there was a significant disruption of myotendinous junctions, variation in the size of fibers, centrally located nuclei, necrosis, phagocytosis, and elevated serum levels of creatine kinase.[21] It has also been proposed that alpha-7 integrin and gamma-sarcoglycan have overlapping functions in skeletal muscle. In support of this, a double knockout of gamma-sarcoglycan and alpha-7 integrin produced a phenotype that was far worse than either knockout alone. Mice died within 1 month of birth and had severe muscle degeneration, suggesting that the roles of these proteins may overlap to maintain the stability of the sarcolemma.[22] Moreover, the double knockout of dystrophin and alpha-7 integrin produced a Duchenne muscular dystrophy-like phenotype, and demonstrated that alterations in alpha-7 integrin affect the pathological changes observed in dystrophin deficiencies.[23] In support of this notion, AAV overexpression of ITGA7 in skeletal muscle of Duchenne muscular dystrophy (DMD) mice showed a significant protective effect against adverse functional parameters associated with DMD, combined with a reversal of these negative features, suggesting that alpha-7 integrin may be a potential therapeutic candidate to treat Duchenne muscular dystrophy.[24]

Studies employing mutant alpha-7 integrin constructs have shown that the cytoplasmic tail of alpha-7B integrin is essential for regulation of lamellipodia formation and regulation of cell mobility regulation via laminin-1/E8 and p130(CAS)/Crk complex formation.[25]

Clinical Significance

Mutations in ITGA7 have been found in patients with unclassified congenital myopathy.[26] Additionally, in patients with severe congenital fiber type disproportion and left ventricular non-compaction cardiomyopathy, a missense mutation, Glu882Lys, was identified in ITGA7 along with a missense mutation in MYH7B, both novel disease genes having a synergistic effect on disease severity.[27]

Alpha-7B integrin expression has been shown to be significantly decreased at sarcolemmal membranes in patients with laminin alpha2 chain-deficient congenital muscular dystrophy. Additionally, in Duchenne muscular dystrophy and Becker muscular dystrophy, the expression of alpha-7B integrin was enhanced.[4]

Interactions

ITGA7 has been shown to interact with:

See also

References

  1. ↑ Wang W, Wu W, Desai T, Ward DC, Kaufman SJ (Aug 1995). "Localization of the alpha 7 integrin gene (ITGA7) on human chromosome 12q13: clustering of integrin and Hox genes implies parallel evolution of these gene families". Genomics. 26 (3): 568–70. doi:10.1016/0888-7543(95)80176-M. PMID 7607681.
  2. ↑ 2.0 2.1 "Entrez Gene: ITGA7 integrin, alpha 7".
  3. ↑ "Protein sequence of human ITGA7 (Uniprot ID: Q13683)". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Retrieved 20 July 2015.
  4. ↑ 4.0 4.1 4.2 Cohn, RD; Mayer, U; Saher, G; Herrmann, R; van der Flier, A; Sonnenberg, A; Sorokin, L; Voit, T (1 March 1999). "Secondary reduction of alpha7B integrin in laminin alpha2 deficient congenital muscular dystrophy supports an additional transmembrane link in skeletal muscle". Journal of the neurological sciences. 163 (2): 140–52. doi:10.1016/s0022-510x(99)00012-x. PMID 10371075.
  5. ↑ 5.0 5.1 5.2 Ziober, BL; Vu, MP; Waleh, N; Crawford, J; Lin, CS; Kramer, RH (15 December 1993). "Alternative extracellular and cytoplasmic domains of the integrin alpha 7 subunit are differentially expressed during development". The Journal of Biological Chemistry. 268 (35): 26773–83. PMID 8253814.
  6. ↑ 6.0 6.1 Maitra, N; Flink, IL; Bahl, JJ; Morkin, E (September 2000). "Expression of alpha and beta integrins during terminal differentiation of cardiomyocytes". Cardiovascular research. 47 (4): 715–25. doi:10.1016/s0008-6363(00)00140-1. PMID 10974220.
  7. ↑ Collo, G; Starr, L; Quaranta, V (5 September 1993). "A new isoform of the laminin receptor integrin alpha 7 beta 1 is developmentally regulated in skeletal muscle". The Journal of Biological Chemistry. 268 (25): 19019–24. PMID 8360188.
  8. ↑ Song, WK; Wang, W; Sato, H; Bielser, DA; Kaufman, SJ (December 1993). "Expression of alpha 7 integrin cytoplasmic domains during skeletal muscle development: alternate forms, conformational change, and homologies with serine/threonine kinases and tyrosine phosphatases". Journal of Cell Science. 106 (4): 1139–52. PMID 8126096.
  9. ↑ Ziober, BL; Kramer, RH (13 September 1996). "Identification and characterization of the cell type-specific and developmentally regulated alpha7 integrin gene promoter". The Journal of Biological Chemistry. 271 (37): 22915–22. PMID 8798472.
  10. ↑ Leung, E; Lim, SP; Berg, R; Yang, Y; Ni, J; Wang, SX; Krissansen, GW (4 February 1998). "A novel extracellular domain variant of the human integrin alpha 7 subunit generated by alternative intron splicing". Biochemical and Biophysical Research Communications. 243 (1): 317–25. doi:10.1006/bbrc.1998.8092. PMID 9473524.
  11. ↑ Vignier, N; Moghadaszadeh, B; Gary, F; Beckmann, J; Mayer, U; Guicheney, P (5 July 1999). "Structure, genetic localization, and identification of the cardiac and skeletal muscle transcripts of the human integrin alpha7 gene (ITGA7)". Biochemical and Biophysical Research Communications. 260 (2): 357–64. doi:10.1006/bbrc.1999.0916. PMID 10403775.
  12. ↑ Kaufman, SJ; Foster, RF; Haye, KR; Faiman, LE (June 1985). "Expression of a developmentally regulated antigen on the surface of skeletal and cardiac muscle cells". The Journal of Cell Biology. 100 (6): 1977–87. doi:10.1083/jcb.100.6.1977. PMC 2113591. PMID 3889014.
  13. ↑ Yao, CC; Breuss, J; Pytela, R; Kramer, RH (July 1997). "Functional expression of the alpha 7 integrin receptor in differentiated smooth muscle cells". Journal of Cell Science. 110 (13): 1477–87. PMID 9224765.
  14. ↑ Velling, T; Collo, G; Sorokin, L; Durbeej, M; Zhang, H; Gullberg, D (December 1996). "Distinct alpha 7A beta 1 and alpha 7B beta 1 integrin expression patterns during mouse development: alpha 7A is restricted to skeletal muscle but alpha 7B is expressed in striated muscle, vasculature, and nervous system". Developmental Dynamics. 207 (4): 355–71. doi:10.1002/(SICI)1097-0177(199612)207:4<355::AID-AJA1>3.0.CO;2-G. PMID 8950511.
  15. ↑ Hynes, RO (3 April 1992). "Integrins: versatility, modulation, and signaling in cell adhesion". Cell. 69 (1): 11–25. doi:10.1016/0092-8674(92)90115-s. PMID 1555235.
  16. ↑ Yao, CC; Ziober, BL; Sutherland, AE; Mendrick, DL; Kramer, RH (December 1996). "Laminins promote the locomotion of skeletal myoblasts via the alpha 7 integrin receptor". Journal of Cell Science. 109 (13): 3139–50. PMID 9004048.
  17. ↑ Brancaccio, M; Cabodi, S; Belkin, AM; Collo, G; Koteliansky, VE; Tomatis, D; Altruda, F; Silengo, L; Tarone, G (March 1998). "Differential onset of expression of alpha 7 and beta 1D integrins during mouse heart and skeletal muscle development". Cell adhesion and communication. 5 (3): 193–205. doi:10.3109/15419069809040291. PMID 9686317.
  18. ↑ Samson, T; Smyth, N; Janetzky, S; Wendler, O; Müller, JM; Schüle, R; von der Mark, H; von der Mark, K; Wixler, V (2 July 2004). "The LIM-only proteins FHL2 and FHL3 interact with alpha- and beta-subunits of the muscle alpha7beta1 integrin receptor". The Journal of Biological Chemistry. 279 (27): 28641–52. doi:10.1074/jbc.m312894200. PMID 15117962.
  19. ↑ Galie, PA; Khalid, N; Carnahan, KE; Westfall, MV; Stegemann, JP (NaN). "Substrate stiffness affects sarcomere and costamere structure and electrophysiological function of isolated adult cardiomyocytes". Cardiovascular Pathology. 22 (3): 219–27. doi:10.1016/j.carpath.2012.10.003. PMC 3610795. PMID 23266222. Check date values in: |date= (help)
  20. ↑ Zolkiewska, A; Moss, J (1997). "The alpha 7 integrin as a target protein for cell surface mono-ADP-ribosylation in muscle cells". Advances in experimental medicine and biology. 419: 297–303. PMID 9193669.
  21. ↑ Mayer, U; Saher, G; Fässler, R; Bornemann, A; Echtermeyer, F; von der Mark, H; Miosge, N; Pöschl, E; von der Mark, K (November 1997). "Absence of integrin alpha 7 causes a novel form of muscular dystrophy". Nature Genetics. 17 (3): 318–23. doi:10.1038/ng1197-318. PMID 9354797.
  22. ↑ Allikian, MJ; Hack, AA; Mewborn, S; Mayer, U; McNally, EM (1 August 2004). "Genetic compensation for sarcoglycan loss by integrin alpha7beta1 in muscle". Journal of Cell Science. 117 (Pt 17): 3821–30. doi:10.1242/jcs.01234. PMID 15252120.
  23. ↑ Guo, C; Willem, M; Werner, A; Raivich, G; Emerson, M; Neyses, L; Mayer, U (15 March 2006). "Absence of alpha 7 integrin in dystrophin-deficient mice causes a myopathy similar to Duchenne muscular dystrophy". Human Molecular Genetics. 15 (6): 989–98. doi:10.1093/hmg/ddl018. PMID 16476707.
  24. ↑ Heller, KN; Montgomery, CL; Janssen, PM; Clark, KR; Mendell, JR; Rodino-Klapac, LR (March 2013). "AAV-mediated overexpression of human α7 integrin leads to histological and functional improvement in dystrophic mice". Molecular Therapy. 21 (3): 520–5. doi:10.1038/mt.2012.281. PMC 3589167. PMID 23319059.
  25. ↑ Mielenz, D; Hapke, S; Pöschl, E; von Der Mark, H; von Der Mark, K (20 April 2001). "The integrin alpha 7 cytoplasmic domain regulates cell migration, lamellipodia formation, and p130CAS/Crk coupling". The Journal of Biological Chemistry. 276 (16): 13417–26. doi:10.1074/jbc.m011481200. PMID 11278916.
  26. ↑ Hayashi, YK; Chou, FL; Engvall, E; Ogawa, M; Matsuda, C; Hirabayashi, S; Yokochi, K; Ziober, BL; Kramer, RH; Kaufman, SJ; Ozawa, E; Goto, Y; Nonaka, I; Tsukahara, T; Wang, JZ; Hoffman, EP; Arahata, K (May 1998). "Mutations in the integrin alpha7 gene cause congenital myopathy". Nature Genetics. 19 (1): 94–7. doi:10.1038/ng0598-94. PMID 9590299.
  27. ↑ Esposito, T; Sampaolo, S; Limongelli, G; Varone, A; Formicola, D; Diodato, D; Farina, O; Napolitano, F; Pacileo, G; Gianfrancesco, F; Di Iorio, G (21 June 2013). "Digenic mutational inheritance of the integrin alpha 7 and the myosin heavy chain 7B genes causes congenital myopathy with left ventricular non-compact cardiomyopathy". Orphanet journal of rare diseases. 8: 91. doi:10.1186/1750-1172-8-91. PMC 3695851. PMID 23800289.
  28. ↑ Vachon, PH; Xu, H; Liu, L; Loechel, F; Hayashi, Y; Arahata, K; Reed, JC; Wewer, UM; Engvall, E (1 October 1997). "Integrins (alpha7beta1) in muscle function and survival. Disrupted expression in merosin-deficient congenital muscular dystrophy". The Journal of Clinical Investigation. 100 (7): 1870–81. doi:10.1172/jci119716. PMC 508374. PMID 9312189.
  29. ↑ Hodges, BL; Hayashi, YK; Nonaka, I; Wang, W; Arahata, K; Kaufman, SJ (November 1997). "Altered expression of the alpha7beta1 integrin in human and murine muscular dystrophies". Journal of Cell Science. 110 (22): 2873–81. PMID 9427295.
  30. ↑ Vachon, PH; Xu, H; Liu, L; Loechel, F; Hayashi, Y; Arahata, K; Reed, JC; Wewer, UM; Engvall, E (1 October 1997). "Integrins (alpha7beta1) in muscle function and survival. Disrupted expression in merosin-deficient congenital muscular dystrophy". The Journal of Clinical Investigation. 100 (7): 1870–81. doi:10.1172/jci119716. PMC 508374. PMID 9312189.
  31. ↑ 31.0 31.1 Samson T, Smyth N, Janetzky S, Wendler O, Müller JM, Schüle R, von der Mark H, von der Mark K, Wixler V (Jul 2004). "The LIM-only proteins FHL2 and FHL3 interact with alpha- and beta-subunits of the muscle alpha7beta1 integrin receptor". J. Biol. Chem. 279 (27): 28641–52. doi:10.1074/jbc.M312894200. PMID 15117962.

Further reading

External links

Retrieved from "https://www.wikidoc.org/index.php?title=ITGA7&oldid=1415705"