Laminin, alpha 4: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Laminin subunit alpha-4''' is a [[protein]] that in humans is encoded by the ''LAMA4'' [[gene]].<ref name="pmid7959779">{{cite journal | vauthors = Richards AJ, al-Imara L, Carter NP, Lloyd JC, Leversha MA, Pope FM | title = Localization of the gene (LAMA4) to chromosome 6q21 and isolation of a partial cDNA encoding a variant laminin A chain | journal = Genomics | volume = 22 | issue = 1 | pages = 237–9 | date = Jul 1994 | pmid = 7959779 | pmc =  | doi = 10.1006/geno.1994.1372 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: LAMA4 laminin, alpha 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3910| accessdate = }}</ref>
| 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. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Laminin, alpha 4
| HGNCid = 6484
| Symbol = LAMA4
| AltSymbols =; LAMA3; DKFZp686D23145; LAMA4*-1
| OMIM = 600133
| ECnumber = 
| Homologene = 37604
| MGIid = 109321
| GeneAtlas_image1 = PBB_GE_LAMA4_202202_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_LAMA4_210089_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_LAMA4_210990_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}}
| Component = {{GNF_GO|id=GO:0005605 |text = basal lamina}} {{GNF_GO|id=GO:0005606 |text = laminin-1 complex}}
| Process = {{GNF_GO|id=GO:0001568 |text = blood vessel development}} {{GNF_GO|id=GO:0030155 |text = regulation of cell adhesion}} {{GNF_GO|id=GO:0030334 |text = regulation of cell migration}} {{GNF_GO|id=GO:0045995 |text = regulation of embryonic development}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3910
    | Hs_Ensembl = ENSG00000112769
    | Hs_RefseqProtein = NP_002281
    | Hs_RefseqmRNA = NM_002290
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 112536654
    | Hs_GenLoc_end = 112682605
    | Hs_Uniprot = Q16363
    | Mm_EntrezGene = 16775
    | Mm_Ensembl = ENSMUSG00000019846
    | Mm_RefseqmRNA = NM_010681
    | Mm_RefseqProtein = NP_034811
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 38654993
    | Mm_GenLoc_end = 38799597
    | Mm_Uniprot = Q14BF2
  }}
}}
'''Laminin, alpha 4''', also known as '''LAMA4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LAMA4 laminin, alpha 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3910| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Laminin]]s, a family of extracellular matrix [[glycoprotein]]s, are the major non[[collagenous]] constituent of [[basement membrane]]s.  They have been implicated in a wide variety of biological processes including [[cell adhesion]], differentiation, migration, signaling, neurite outgrowth and [[metastasis]].
{{PBB_Summary
| section_title =
| summary_text = Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes.  They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains.  Each laminin chain is a multidomain protein encoded by a distinct gene.  Several isoforms of each chain have been described.  Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1.  The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo.  This gene encodes the alpha chain isoform laminin, alpha 4.  The domain structure of alpha 4 is similar to that of alpha 3, both of which resemble truncated versions of alpha 1 and alpha 2, in that approximately 1,200 residues at the N-terminus (domains IV, V and VI) have been lost. Laminin, alpha 4 contains the C-terminal G domain which distinguishes all alpha chains from the beta and gamma chains.  The RNA analysis from adult and fetal tissues revealed developmental regulation of expression, however, the exact function of laminin, alpha 4 is not known.  Tissue-specific utilization of alternative polyA-signal has been described in literature.  Also, alternative splicing involving the first intron in the 5' UTR, and laminin alpha 4 like isoforms have been noted, however, the full-length nature of these products is not known.<ref name="entrez">{{cite web | title = Entrez Gene: LAMA4 laminin, alpha 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3910| accessdate = }}</ref>
}}


==References==
Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains.  Each laminin chain is a multidomain protein encoded by a distinct gene.  Several isoforms of each chain have been described.  Different alpha, beta and gamma chain [[isomer]]s combine to give rise to different hetero[[Protein trimer|trimeric]] laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1.  The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions [[in vivo]].
{{reflist|2}}
 
==Further reading==
This gene encodes the alpha chain isoform laminin, alpha 4.  The [[Protein domain|domain]] structure of alpha 4 is similar to that of alpha 3, both of which resemble truncated versions of alpha 1 and alpha 2, in that approximately 1,200 residues at the [[N-terminus]] (domains IV, V and VI) have been lost. Laminin, alpha 4 contains the [[C-terminal]] G domain which distinguishes all alpha chains from the beta and gamma chains.  The [[RNA]] analysis from adult and fetal tissues revealed developmental regulation of expression, however, the exact function of laminin, alpha 4 is not known.<ref name="entrez" />
 
== Gene ==
 
Tissue-specific utilization of alternative polyA-signal has been described in literature.  Also, alternative splicing involving the first [[intron]] in the 5' UTR, and laminin alpha 4 like isoforms have been noted, however, the full-length nature of these products is not known.<ref name="entrez" />
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Ljubimova JY, Fujita M, Khazenzon NM, Ljubimov AV, Black KL | title = Changes in laminin isoforms associated with brain tumor invasion and angiogenesis | journal = Frontiers in Bioscience | volume = 11 | issue = 1 | pages = 81–8 | year = 2006 | pmid = 16146715 | pmc = 3506377 | doi = 10.2741/1781 }}
| citations =
* {{cite journal | vauthors = Iivanainen A, Sainio K, Sariola H, Tryggvason K | title = Primary structure and expression of a novel human laminin alpha 4 chain | journal = FEBS Letters | volume = 365 | issue = 2-3 | pages = 183–8 | date = May 1995 | pmid = 7781776 | doi = 10.1016/0014-5793(95)00462-I }}
*{{cite journal | author=Ljubimova JY, Fujita M, Khazenzon NM, ''et al.'' |title=Changes in laminin isoforms associated with brain tumor invasion and angiogenesis. |journal=Front. Biosci. |volume=11 |issue= |pages= 81-8 |year= 2006 |pmid= 16146715 |doi= }}
* {{cite journal | vauthors = Burgeson RE, Chiquet M, Deutzmann R, Ekblom P, Engel J, Kleinman H, Martin GR, Meneguzzi G, Paulsson M, Sanes J | title = A new nomenclature for the laminins | journal = Matrix Biology | volume = 14 | issue = 3 | pages = 209–11 | date = Apr 1994 | pmid = 7921537 | doi = 10.1016/0945-053X(94)90184-8 }}
*{{cite journal | author=Iivanainen A, Sainio K, Sariola H, Tryggvason K |title=Primary structure and expression of a novel human laminin alpha 4 chain. |journal=FEBS Lett. |volume=365 |issue= 2-3 |pages= 183-8 |year= 1995 |pmid= 7781776 |doi= }}
* {{cite journal | vauthors = Ryan MC, Tizard R, VanDevanter DR, Carter WG | title = Cloning of the LamA3 gene encoding the alpha 3 chain of the adhesive ligand epiligrin. Expression in wound repair | journal = The Journal of Biological Chemistry | volume = 269 | issue = 36 | pages = 22779–87 | date = Sep 1994 | pmid = 8077230 | doi =  }}
*{{cite journal | author=Burgeson RE, Chiquet M, Deutzmann R, ''et al.'' |title=A new nomenclature for the laminins. |journal=Matrix Biol. |volume=14 |issue= 3 |pages= 209-11 |year= 1994 |pmid= 7921537 |doi= }}
* {{cite journal | vauthors = Richards A, Al-Imara L, Pope FM | title = The complete cDNA sequence of laminin alpha 4 and its relationship to the other human laminin alpha chains | journal = European Journal of Biochemistry / FEBS | volume = 238 | issue = 3 | pages = 813–21 | date = Jun 1996 | pmid = 8706685 | doi = 10.1111/j.1432-1033.1996.0813w.x }}
*{{cite journal  | author=Richards AJ, al-Imara L, Carter NP, ''et al.'' |title=Localization of the gene (LAMA4) to chromosome 6q21 and isolation of a partial cDNA encoding a variant laminin A chain. |journal=Genomics |volume=22 |issue= 1 |pages= 237-9 |year= 1994 |pmid= 7959779 |doi= 10.1006/geno.1994.1372 }}
* {{cite journal | vauthors = Xiao S, Lux ML, Reeves R, Hudson TJ, Fletcher JA | title = HMGI(Y) activation by chromosome 6p21 rearrangements in multilineage mesenchymal cells from pulmonary hamartoma | journal = The American Journal of Pathology | volume = 150 | issue = 3 | pages = 901–10 | date = Mar 1997 | pmid = 9060828 | pmc = 1857887 | doi =  }}
*{{cite journal | author=Ryan MC, Tizard R, VanDevanter DR, Carter WG |title=Cloning of the LamA3 gene encoding the alpha 3 chain of the adhesive ligand epiligrin. Expression in wound repair. |journal=J. Biol. Chem. |volume=269 |issue= 36 |pages= 22779-87 |year= 1994 |pmid= 8077230 |doi=  }}
* {{cite journal | vauthors = Durkin ME, Loechel F, Mattei MG, Gilpin BJ, Albrechtsen R, Wewer UM | title = Tissue-specific expression of the human laminin alpha5-chain, and mapping of the gene to human chromosome 20q13.2-13.3 and to distal mouse chromosome 2 near the locus for the ragged (Ra) mutation | journal = FEBS Letters | volume = 411 | issue = 2-3 | pages = 296–300 | date = Jul 1997 | pmid = 9271224 | doi = 10.1016/S0014-5793(97)00686-8 }}
*{{cite journal | author=Richards A, Al-Imara L, Pope FM |title=The complete cDNA sequence of laminin alpha 4 and its relationship to the other human laminin alpha chains. |journal=Eur. J. Biochem. |volume=238 |issue= 3 |pages= 813-21 |year= 1996 |pmid= 8706685 |doi= }}
* {{cite journal | vauthors = Richards A, Luccarini C, Pope FM | title = The structural organisation of LAMA4, the gene encoding laminin alpha4 | journal = European Journal of Biochemistry / FEBS | volume = 248 | issue = 1 | pages = 15–23 | date = Aug 1997 | pmid = 9310354 | doi = 10.1111/j.1432-1033.1997.t01-1-00015.x }}
*{{cite journal | author=Xiao S, Lux ML, Reeves R, ''et al.'' |title=HMGI(Y) activation by chromosome 6p21 rearrangements in multilineage mesenchymal cells from pulmonary hamartoma. |journal=Am. J. Pathol. |volume=150 |issue= 3 |pages= 901-10 |year= 1997 |pmid= 9060828 |doi=  }}
* {{cite journal | vauthors = Mrowiec T, Melchar C, Górski A | title = HIV-protein-mediated alterations in T cell interactions with the extracellular matrix proteins and endothelium | journal = Archivum Immunologiae et Therapiae Experimentalis | volume = 45 | issue = 2-3 | pages = 255–9 | year = 1998 | pmid = 9597096 | doi =  }}
*{{cite journal | author=Durkin ME, Loechel F, Mattei MG, ''et al.'' |title=Tissue-specific expression of the human laminin alpha5-chain, and mapping of the gene to human chromosome 20q13.2-13.3 and to distal mouse chromosome 2 near the locus for the ragged (Ra) mutation. |journal=FEBS Lett. |volume=411 |issue= 2-3 |pages= 296-300 |year= 1997 |pmid= 9271224 |doi= }}
* {{cite journal | vauthors = Talts JF, Sasaki T, Miosge N, Göhring W, Mann K, Mayne R, Timpl R | title = Structural and functional analysis of the recombinant G domain of the laminin alpha4 chain and its proteolytic processing in tissues | journal = The Journal of Biological Chemistry | volume = 275 | issue = 45 | pages = 35192–9 | date = Nov 2000 | pmid = 10934193 | doi = 10.1074/jbc.M003261200 }}
*{{cite journal | author=Richards A, Luccarini C, Pope FM |title=The structural organisation of LAMA4, the gene encoding laminin alpha4. |journal=Eur. J. Biochem. |volume=248 |issue= 1 |pages= 15-23 |year= 1997 |pmid= 9310354 |doi= }}
* {{cite journal | vauthors = Fleischmajer R, Kuroda K, Utani A, Douglas MacDonald E, Perlish JS, Arikawa-Hirasawa E, Sekiguchi K, Sanzen N, Timpl R, Yamada Y | title = Differential expression of laminin alpha chains during proliferative and differentiation stages in a model for skin morphogenesis | journal = Matrix Biology | volume = 19 | issue = 7 | pages = 637–47 | date = Dec 2000 | pmid = 11102753 | doi = 10.1016/S0945-053X(00)00092-5 }}
*{{cite journal | author=Mrowiec T, Melchar C, Górski A |title=HIV-protein-mediated alterations in T cell interactions with the extracellular matrix proteins and endothelium. |journal=Arch. Immunol. Ther. Exp. (Warsz.) |volume=45 |issue= 2-3 |pages= 255-9 |year= 1998 |pmid= 9597096 |doi=  }}
* {{cite journal | vauthors = McArthur CP, Wang Y, Heruth D, Gustafson S | title = Amplification of extracellular matrix and oncogenes in tat-transfected human salivary gland cell lines with expression of laminin, fibronectin, collagens I, III, IV, c-myc and p53 | journal = Archives of Oral Biology | volume = 46 | issue = 6 | pages = 545–55 | date = Jun 2001 | pmid = 11311202 | doi = 10.1016/S0003-9969(01)00014-0 }}
*{{cite journal | author=Talts JF, Sasaki T, Miosge N, ''et al.'' |title=Structural and functional analysis of the recombinant G domain of the laminin alpha4 chain and its proteolytic processing in tissues. |journal=J. Biol. Chem. |volume=275 |issue= 45 |pages= 35192-9 |year= 2001 |pmid= 10934193 |doi= 10.1074/jbc.M003261200 }}
* {{cite journal | vauthors = Petäjäniemi N, Korhonen M, Kortesmaa J, Tryggvason K, Sekiguchi K, Fujiwara H, Sorokin L, Thornell LE, Wondimu Z, Assefa D, Patarroyo M, Virtanen I | title = Localization of laminin alpha4-chain in developing and adult human tissues | journal = The Journal of Histochemistry and Cytochemistry | volume = 50 | issue = 8 | pages = 1113–30 | date = Aug 2002 | pmid = 12133914 | doi = 10.1177/002215540205000813 }}
*{{cite journal | author=Fleischmajer R, Kuroda K, Utani A, ''et al.'' |title=Differential expression of laminin alpha chains during proliferative and differentiation stages in a model for skin morphogenesis. |journal=Matrix Biol. |volume=19 |issue= 7 |pages= 637-47 |year= 2001 |pmid= 11102753 |doi= }}
* {{cite journal | vauthors = Gu YC, Kortesmaa J, Tryggvason K, Persson J, Ekblom P, Jacobsen SE, Ekblom M | title = Laminin isoform-specific promotion of adhesion and migration of human bone marrow progenitor cells | journal = Blood | volume = 101 | issue = 3 | pages = 877–85 | date = Feb 2003 | pmid = 12393739 | doi = 10.1182/blood-2002-03-0796 }}
*{{cite journal | author=McArthur CP, Wang Y, Heruth D, Gustafson S |title=Amplification of extracellular matrix and oncogenes in tat-transfected human salivary gland cell lines with expression of laminin, fibronectin, collagens I, III, IV, c-myc and p53. |journal=Arch. Oral Biol. |volume=46 |issue= 6 |pages= 545-55 |year= 2001 |pmid= 11311202 |doi= }}
* {{cite journal | vauthors = Hayashi Y, Kim KH, Fujiwara H, Shimono C, Yamashita M, Sanzen N, Futaki S, Sekiguchi K | title = Identification and recombinant production of human laminin alpha4 subunit splice variants | journal = Biochemical and Biophysical Research Communications | volume = 299 | issue = 3 | pages = 498–504 | date = Dec 2002 | pmid = 12445830 | doi = 10.1016/S0006-291X(02)02642-6 }}
*{{cite journal | author=Petäjäniemi N, Korhonen M, Kortesmaa J, ''et al.'' |title=Localization of laminin alpha4-chain in developing and adult human tissues. |journal=J. Histochem. Cytochem. |volume=50 |issue= 8 |pages= 1113-30 |year= 2002 |pmid= 12133914 |doi= }}
* {{cite journal | vauthors = Gonzalez AM, Gonzales M, Herron GS, Nagavarapu U, Hopkinson SB, Tsuruta D, Jones JC | title = Complex interactions between the laminin alpha 4 subunit and integrins regulate endothelial cell behavior in vitro and angiogenesis in vivo | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 25 | pages = 16075–80 | date = Dec 2002 | pmid = 12454288 | pmc = 138567 | doi = 10.1073/pnas.252649399 }}
*{{cite journal | author=Gu YC, Kortesmaa J, Tryggvason K, ''et al.'' |title=Laminin isoform-specific promotion of adhesion and migration of human bone marrow progenitor cells. |journal=Blood |volume=101 |issue= 3 |pages= 877-85 |year= 2003 |pmid= 12393739 |doi= 10.1182/blood-2002-03-0796 }}
* {{cite journal | vauthors = DeHahn KC, Gonzales M, Gonzalez AM, Hopkinson SB, Chandel NS, Brunelle JK, Jones JC | title = The alpha4 laminin subunit regulates endothelial cell survival | journal = Experimental Cell Research | volume = 294 | issue = 1 | pages = 281–9 | date = Mar 2004 | pmid = 14980521 | doi = 10.1016/j.yexcr.2003.11.006 }}
*{{cite journal | author=Hayashi Y, Kim KH, Fujiwara H, ''et al.'' |title=Identification and recombinant production of human laminin alpha4 subunit splice variants. |journal=Biochem. Biophys. Res. Commun. |volume=299 |issue= 3 |pages= 498-504 |year= 2003 |pmid= 12445830 |doi= }}
*{{cite journal | author=Gonzalez AM, Gonzales M, Herron GS, ''et al.'' |title=Complex interactions between the laminin alpha 4 subunit and integrins regulate endothelial cell behavior in vitro and angiogenesis in vivo. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 25 |pages= 16075-80 |year= 2003 |pmid= 12454288 |doi= 10.1073/pnas.252649399 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Mungall AJ, Palmer SA, Sims SK, ''et al.'' |title=The DNA sequence and analysis of human chromosome 6. |journal=Nature |volume=425 |issue= 6960 |pages= 805-11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055 }}
*{{cite journal | author=DeHahn KC, Gonzales M, Gonzalez AM, ''et al.'' |title=The alpha4 laminin subunit regulates endothelial cell survival. |journal=Exp. Cell Res. |volume=294 |issue= 1 |pages= 281-9 |year= 2004 |pmid= 14980521 |doi= 10.1016/j.yexcr.2003.11.006 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{Fibrous proteins}}
{{WikiDoc Sources}}
 
[[Category:Laminins]]

Latest revision as of 19:27, 2 September 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

Laminin subunit alpha-4 is a protein that in humans is encoded by the LAMA4 gene.[1][2]

Function

Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis.

Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo.

This gene encodes the alpha chain isoform laminin, alpha 4. The domain structure of alpha 4 is similar to that of alpha 3, both of which resemble truncated versions of alpha 1 and alpha 2, in that approximately 1,200 residues at the N-terminus (domains IV, V and VI) have been lost. Laminin, alpha 4 contains the C-terminal G domain which distinguishes all alpha chains from the beta and gamma chains. The RNA analysis from adult and fetal tissues revealed developmental regulation of expression, however, the exact function of laminin, alpha 4 is not known.[2]

Gene

Tissue-specific utilization of alternative polyA-signal has been described in literature. Also, alternative splicing involving the first intron in the 5' UTR, and laminin alpha 4 like isoforms have been noted, however, the full-length nature of these products is not known.[2]

References

  1. ↑ Richards AJ, al-Imara L, Carter NP, Lloyd JC, Leversha MA, Pope FM (Jul 1994). "Localization of the gene (LAMA4) to chromosome 6q21 and isolation of a partial cDNA encoding a variant laminin A chain". Genomics. 22 (1): 237–9. doi:10.1006/geno.1994.1372. PMID 7959779.
  2. ↑ 2.0 2.1 2.2 "Entrez Gene: LAMA4 laminin, alpha 4".

Further reading

  • Ljubimova JY, Fujita M, Khazenzon NM, Ljubimov AV, Black KL (2006). "Changes in laminin isoforms associated with brain tumor invasion and angiogenesis". Frontiers in Bioscience. 11 (1): 81–8. doi:10.2741/1781. PMC 3506377. PMID 16146715.
  • Iivanainen A, Sainio K, Sariola H, Tryggvason K (May 1995). "Primary structure and expression of a novel human laminin alpha 4 chain". FEBS Letters. 365 (2–3): 183–8. doi:10.1016/0014-5793(95)00462-I. PMID 7781776.
  • Burgeson RE, Chiquet M, Deutzmann R, Ekblom P, Engel J, Kleinman H, Martin GR, Meneguzzi G, Paulsson M, Sanes J (Apr 1994). "A new nomenclature for the laminins". Matrix Biology. 14 (3): 209–11. doi:10.1016/0945-053X(94)90184-8. PMID 7921537.
  • Ryan MC, Tizard R, VanDevanter DR, Carter WG (Sep 1994). "Cloning of the LamA3 gene encoding the alpha 3 chain of the adhesive ligand epiligrin. Expression in wound repair". The Journal of Biological Chemistry. 269 (36): 22779–87. PMID 8077230.
  • Richards A, Al-Imara L, Pope FM (Jun 1996). "The complete cDNA sequence of laminin alpha 4 and its relationship to the other human laminin alpha chains". European Journal of Biochemistry / FEBS. 238 (3): 813–21. doi:10.1111/j.1432-1033.1996.0813w.x. PMID 8706685.
  • Xiao S, Lux ML, Reeves R, Hudson TJ, Fletcher JA (Mar 1997). "HMGI(Y) activation by chromosome 6p21 rearrangements in multilineage mesenchymal cells from pulmonary hamartoma". The American Journal of Pathology. 150 (3): 901–10. PMC 1857887. PMID 9060828.
  • Durkin ME, Loechel F, Mattei MG, Gilpin BJ, Albrechtsen R, Wewer UM (Jul 1997). "Tissue-specific expression of the human laminin alpha5-chain, and mapping of the gene to human chromosome 20q13.2-13.3 and to distal mouse chromosome 2 near the locus for the ragged (Ra) mutation". FEBS Letters. 411 (2–3): 296–300. doi:10.1016/S0014-5793(97)00686-8. PMID 9271224.
  • Richards A, Luccarini C, Pope FM (Aug 1997). "The structural organisation of LAMA4, the gene encoding laminin alpha4". European Journal of Biochemistry / FEBS. 248 (1): 15–23. doi:10.1111/j.1432-1033.1997.t01-1-00015.x. PMID 9310354.
  • Mrowiec T, Melchar C, Górski A (1998). "HIV-protein-mediated alterations in T cell interactions with the extracellular matrix proteins and endothelium". Archivum Immunologiae et Therapiae Experimentalis. 45 (2–3): 255–9. PMID 9597096.
  • Talts JF, Sasaki T, Miosge N, Göhring W, Mann K, Mayne R, Timpl R (Nov 2000). "Structural and functional analysis of the recombinant G domain of the laminin alpha4 chain and its proteolytic processing in tissues". The Journal of Biological Chemistry. 275 (45): 35192–9. doi:10.1074/jbc.M003261200. PMID 10934193.
  • Fleischmajer R, Kuroda K, Utani A, Douglas MacDonald E, Perlish JS, Arikawa-Hirasawa E, Sekiguchi K, Sanzen N, Timpl R, Yamada Y (Dec 2000). "Differential expression of laminin alpha chains during proliferative and differentiation stages in a model for skin morphogenesis". Matrix Biology. 19 (7): 637–47. doi:10.1016/S0945-053X(00)00092-5. PMID 11102753.
  • McArthur CP, Wang Y, Heruth D, Gustafson S (Jun 2001). "Amplification of extracellular matrix and oncogenes in tat-transfected human salivary gland cell lines with expression of laminin, fibronectin, collagens I, III, IV, c-myc and p53". Archives of Oral Biology. 46 (6): 545–55. doi:10.1016/S0003-9969(01)00014-0. PMID 11311202.
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