Insulin-like growth factor 2: 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
{{Infobox protein family
| update_page = yes
| Symbol = IGF2_C
| require_manual_inspection = no
| Name = Insulin-like growth factor II E-peptide (somatomedians-A )
| update_protein_box = yes
| image =
| update_summary = no
| width =
| update_citations = yes
| caption =
| Pfam = PF08365
| Pfam_clan = 
| InterPro = IPR013576
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =  
| OPM family =  
| OPM protein =  
| CAZy =  
| CDD =  
}}
}}
'''Insulin-like growth factor 2''' ('''IGF-2''') is one of three protein [[hormone]]s that share structural similarity to [[insulin]].  The MeSH definition reads: "A well-characterized neutral [[peptide]] believed to be secreted by the liver and to circulate in the blood. It has growth-regulating, insulin-like and mitogenic activities. The growth factor has a major, but not absolute, dependence on [[somatotropin]]. It is believed to be a major fetal growth factor in contrast to [[IGF-1|Insulin-like growth factor 1]], which is a major growth factor in adults".<ref>{{cite web | url = https://www.ncbi.nlm.nih.gov/mesh/68007335 | title = Insulin-Like Growth Factor II | work = MeSH | publisher =  NCBI }}</ref>


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Gene structure ==
{{GNF_Protein_box
 
| image = PBB_Protein_IGF2_image.jpg
In humans, the IGF2 [[gene]] is located on [[chromosome 11]]p15.5, a region which contains numerous [[Genomic Imprinting|imprinted genes]]. In mice this [[Homology (biology)|homologous region]] is found at distal chromosome 7. In both organisms, ''Igf2'' is imprinted, with expression resulting favourably from the paternally inherited [[allele]]. However, in some human brain regions a loss of imprinting occurs resulting in both IGF2 and H19 being transcribed from both parental alleles.<ref>{{cite journal | vauthors = Pham NV, Nguyen MT, Hu JF, Vu TH, Hoffman AR | title = Dissociation of IGF2 and H19 imprinting in human brain | journal = Brain Research | volume = 810 | issue = 1–2 | pages = 1–8 | date = Nov 1998 | pmid = 9813220 | doi=10.1016/s0006-8993(98)00783-5}}</ref>
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1igl.
 
| Name = Insulin-like growth factor 2 (somatomedin A)
The protein [[CTCF]] is involved in repressing [[gene expression|expression]] of the gene, by binding to the [[H19 (gene)|H19]] imprinting control region (ICR) along with Differentially-methylated Region-1 (DMR1) and Matrix Attachment Region -3 (MAR3). These three [[DNA sequence]]s bind to [[CTCF]] in a way that limits downstream enhancer access to the Igf2 region. The mechanism in which CTCF binds to these regions is currently unknown, but could include either a direct DNA-CTCF interaction or it could possibly be mediated by other proteins.
| HGNCid = 5466
In mammals (mice, humans, pigs), only the allele for insulin-like growth factor-2 (IGF2) inherited from one's father is active; that inherited from the mother is not — a phenomenon called imprinting.The mechanism: the mother's allele has an insulator between the IGF2 promoter and enhancer. So does the father's allele, but in his case, the insulator has been methylated. CTCF can no longer bind to the insulator, and so the enhancer is now free to turn on the father's IGF2 promoter.{{citation needed|date=May 2014}}
| Symbol = IGF2
| AltSymbols =; C11orf43; FLJ22066; FLJ44734; INSIGF; pp9974
| OMIM = 147470
| ECnumber = 
| Homologene = 510
| MGIid = 96434
| GeneAtlas_image1 = PBB_GE_IGF2_202409_at_tn.png
| GeneAtlas_image2 = PBB_GE_IGF2_202410_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_IGF2_210881_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005159 |text = insulin-like growth factor receptor binding}} {{GNF_GO|id=GO:0005179 |text = hormone activity}} {{GNF_GO|id=GO:0005520 |text = insulin-like growth factor binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0018445 |text = prothoracicotrophic hormone activity}}  
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0006349 |text = imprinting}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008286 |text = insulin receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3481
    | Hs_Ensembl = ENSG00000167244
    | Hs_RefseqProtein = NP_000603
    | Hs_RefseqmRNA = NM_000612
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 2106918
    | Hs_GenLoc_end = 2125616
    | Hs_Uniprot = P01344
    | Mm_EntrezGene = 16002
    | Mm_Ensembl = ENSMUSG00000048583
    | Mm_RefseqmRNA = NM_010514
    | Mm_RefseqProtein = NP_034644
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 142460158
    | Mm_GenLoc_end = 142468879
    | Mm_Uniprot = P09535
  }}
}}
{{SI}}
__NOTOC__
{{GS}}


== Function ==


The major role of IGF-2 is as a growth promoting hormone during [[gestation]].


IGF-2 exerts its effects by binding to the [[Insulin-like growth factor 1 receptor|IGF-1 receptor]] and to the short isoform of the insulin receptor (IR-A or exon 11-).<ref name="pmid10207053">{{cite journal | vauthors = Frasca F, Pandini G, Scalia P, Sciacca L, Mineo R, Costantino A, Goldfine ID, Belfiore A, Vigneri R | title = Insulin receptor isoform A, a newly recognized, high-affinity insulin-like growth factor II receptor in fetal and cancer cells | journal = Molecular and Cellular Biology | volume = 19 | issue = 5 | pages = 3278–88 | year = 1999 | pmid = 10207053 | pmc = 84122 | doi =  10.1128/MCB.19.5.3278 }}</ref> IGF2 may also bind to the [[Insulin-like growth factor 2 receptor|IGF-2 receptor]] (also called the cation-independent [[mannose 6-phosphate receptor]]), which acts as a signalling antagonist; that is, to prevent IGF2 responses.


'''Insulin-like growth factor 2''' ('''IGF-2''') is one of three protein [[hormone]]s that share structural similarity to [[insulin]].  
In the process of folliculogenesis, IGF-2 is created by thecal cells to act in an autocrine manner on the theca cells themselves, and in a paracrine manner on granulosa cells in the ovary.{{citation needed|date=February 2014}} IGF2 promotes granulosa cell proliferation during the follicular phase of the menstrual cycle, acting alongside follicle stimulating hormone (FSH).<ref>{{cite book |vauthors= Neidhart, M |date= 2016 |title= DNA Methylation and Complex Human Disease |edition= 1st |place= San Diego |publisher= Academic Press |page= 222}} {{ISBN|9780124201941}}.</ref> After ovulation has occurred, IGF-2 promotes [[progesterone]] secretion during the luteal phase of the menstrual cycle, together with luteinizing hormone (LH). Thus, IGF2 acts as a co-hormone together with both FSH and LH.<ref>{{cite book |vauthors= Neidhart, M |date= 2016 |title= DNA Methylation and Complex Human Disease |edition= 1st |place= San Diego |publisher= Academic Press |page= 22}} {{ISBN|978-0124201941}}.</ref>


==Gene structure==
A study at the Mount Sinai School of Medicine found that IGF-2 may be linked to memory and reproduction.<ref>{{cite journal |vauthors= Chen DY, Stern SA, Garcia-Osta A, Saunier-Rebori B, Pollonini G, Bambah-Mukku D, Blitzer RD, Alberini CM |title= A critical role for IGF-II in memory consolidation and enhancement |journal= Nature |volume = 469 |issue = 7331 |pages = 491–7 |date= Jan 2011 |pmid= 21270887 |doi= 10.1038/nature09667 |pmc=3908455}}</ref> A study at the European Neuroscience Institute-Goettingen (Germany) found that fear extinction-induced [[IGF2]]/[[IGFBP7]] signalling promotes the survival of 17- to 19-day-old newborn hippocampal neurons. This suggests that therapeutic strategies that enhance IGF2 signalling and adult [[neurogenesis]] might be suitable to treat diseases linked to excessive [[fear]] memory such as [[PTSD]].<ref name="pmid21873981">{{cite journal |vauthors= Agis-Balboa RC, Arcos-Diaz D, Wittnam J, Govindarajan N, Blom K, Burkhardt S, Haladyniak U, Agbemenyah HY, Zovoilis A, Salinas-Riester G, Opitz L, Sananbenesi F, Fischer A |title= A hippocampal insulin-growth factor 2 pathway regulates the extinction of fear memories |journal= The EMBO Journal |volume= 30 |issue= 19 |pages= 4071–83 |date= Oct 2011 |pmid= 21873981 |pmc= 3209781 |doi= 10.1038/emboj.2011.293 }}</ref>
In humans, the IGF2 [[gene]] is located on [[chromosome]] 11p15.5, a region which contains numerous [[Genomic Imprinting|imprinted genes]]. In mice this homologous region is found at distal chromosome 7. In both organisms, ''Igf2'' is imprinted, with expression resulting favourably from the paternally inherited [[allele]].


The protein [[CTCF]] is involved in repressing [[gene expression|expression]] of the gene, by binding to the [[H19 (gene)|H19]] imprinting control region (ICR) along with Differentially-methylated Region-1 (DMR1) and Matrix Attachment Region -3 (MAR3). These three [[DNA sequence]]s bind to [[CTCF]] in a way that limits downstream enhancer access to the Igf2 region. The mechanism in which CTCF binds to these regions is currently unknown, but could include either a direct DNA-CTCF interaction or it could possibly be mediated by other proteins
== Clinical relevance ==


==Protein structure==
It is sometimes produced in excess in [[Islets of Langerhans|islet]] cell [[tumor]]s and [[Non islet hypoglycemic cell tumor|non-islet hypoglycemic cell tumors]], causing [[hypoglycemia]]. [[Doege-Potter syndrome]] is a [[paraneoplastic syndrome]]<ref name = pmid17409923>{{cite journal |vauthors= Balduyck B, Lauwers P, Govaert K, Hendriks J, De Maeseneer M, Van Schil P |title= Solitary fibrous tumor of the pleura with associated hypoglycemia: Doege-Potter syndrome: a case report |journal= Journal of Thoracic Oncology |volume= 1 |issue= 6 |pages= 588–90 |date= Jul 2006 |pmid= 17409923 |doi= 10.1097/01243894-200607000-00016 }}</ref> in which hypoglycemia is associated with the presence of one or more non-islet fibrous [[tumor]]s in the [[pleural cavity]]. Loss of imprinting of IGF2 is a common feature in tumors seen in [[Beckwith-Wiedemann syndrome]]. As IGF2 promotes development of fetal pancreatic beta cells, it is believed to be related to some forms of diabetes mellitus. Preeclampsia induces a decrease in methylation level at IGF2 demethylated region, and this might be among the mechanisms behind the association between intrauterine exposure to preeclampsia and high risk for metabolic diseases in the later life of the infants.<ref name="pmid573">{{cite journal |vauthors= He J, Zhang A, Fang M, Fang R, Ge J, Jiang Y, Zhang H, Han C, Ye X, Yu D, Huang H, Liu Y, Dong M |title= Methylation levels at IGF2 and GNAS DMRs in infants born to preeclamptic pregnancies |journal= BMC Genomics |volume= 14 |pages= 472 |date= 12 July 2013 |pmid= 23844573 |pmc= 3723441 |doi= 10.1186/1471-2164-14-472 }}</ref>
IGF-2 exerts its effects by binding to the [[Insulin-like growth factor 1 receptor|IGF-1 receptor]]. IGF2 may also bind to the [[Insulin-like growth factor 2 receptor|IGF-2 receptor]] (also called the cation-independent [[mannose 6-phosphate receptor]]), which acts as a signalling antagonist; that is, to prevent IGF2 responses.


==Function==
== Interactions ==
The major role of IGF2 is as a growth promoting hormone during [[gestation]].   


==Diseases==
Insulin-like growth factor 2 has been shown to [[Protein-protein interaction|interact]] with [[IGFBP3]]<ref name=pmid11749962>{{cite journal |vauthors = Storch S, Kübler B, Höning S, Ackmann M, Zapf J, Blum W, Braulke T | title = Transferrin binds insulin-like growth factors and affects binding properties of insulin-like growth factor binding protein-3 | journal = FEBS Letters | volume = 509 | issue = 3 | pages = 395–8 | date = Dec 2001 | pmid = 11749962 | doi = 10.1016/S0014-5793(01)03204-5 }}</ref><ref name=pmid11600567>{{cite journal |vauthors= Buckway CK, Wilson EM, Ahlsén M, Bang P, Oh Y, Rosenfeld RG |title= Mutation of three critical amino acids of the N-terminal domain of IGF-binding protein-3 essential for high affinity IGF binding |journal= The Journal of Clinical Endocrinology and Metabolism |volume= 86 |issue= 10 |pages= 4943–50 |date= Oct 2001 |pmid= 11600567 |doi= 10.1210/jcem.86.10.7936 }}</ref><ref name=pmid9497324>{{cite journal |vauthors = Twigg SM, Baxter RC |title= Insulin-like growth factor (IGF)-binding protein 5 forms an alternative ternary complex with IGFs and the acid-labile subunit |journal= The Journal of Biological Chemistry |volume= 273 |issue= 11 |pages= 6074–9 |date= Mar 1998 | pmid= 9497324 |doi= 10.1074/jbc.273.11.6074 }}</ref><ref name=pmid9446566>{{cite journal | vauthors = Firth SM, Ganeshprasad U, Baxter RC |title= Structural determinants of ligand and cell surface binding of insulin-like growth factor-binding protein-3 |journal= The Journal of Biological Chemistry |volume= 273 |issue=5 |pages= 2631–8 |date= Jan 1998 |pmid= 9446566 |doi= 10.1074/jbc.273.5.2631 }}</ref> and [[transferrin]].<ref name=pmid11749962/>
It is sometimes produced in non-islet cell [[tumour]]s, causing [[hypoglycemia]] (Doege-Potter syndrome).


==See also==
== See also ==
* [[Insulin-like growth factor 2 receptor]]
* [[Insulin-like growth factor 2 receptor]]
* [[Insulin-like growth factor II IRES]]
{{Clear}}
== References ==
{{reflist|33em}}
== Further reading ==
{{refbegin|33em}}
* {{cite journal | vauthors = O'Dell SD, Day IN | title = Insulin-like growth factor II (IGF-II) | journal = The International Journal of Biochemistry & Cell Biology | volume = 30 | issue = 7 | pages = 767–71 | date = Jul 1998 | pmid = 9722981 | doi = 10.1016/S1357-2725(98)00048-X }}
* {{cite journal | vauthors = Butler AA, Yakar S, Gewolb IH, Karas M, Okubo Y, LeRoith D | title = Insulin-like growth factor-I receptor signal transduction: at the interface between physiology and cell biology | journal = Comparative Biochemistry and Physiology B | volume = 121 | issue = 1 | pages = 19–26 | date = Sep 1998 | pmid = 9972281 | doi = 10.1016/S0305-0491(98)10106-2 }}
* {{cite journal | vauthors = Kalli KR, Conover CA | title = The insulin-like growth factor/insulin system in epithelial ovarian cancer | journal = Frontiers in Bioscience | volume = 8 | issue =  | pages = d714-22 | date = May 2003 | pmid = 12700030 | doi = 10.2741/1034 }}
* {{cite journal | vauthors = Wood AW, Duan C, Bern HA | title = Insulin-like growth factor signaling in fish | journal = International Review of Cytology | volume = 243 | issue =  | pages = 215–85 | year = 2005 | pmid = 15797461 | doi = 10.1016/S0074-7696(05)43004-1 }}
* {{cite journal | vauthors = Fowden AL, Sibley C, Reik W, Constancia M | title = Imprinted genes, placental development and fetal growth | journal = Hormone Research | volume = 65 Suppl 3 | issue = 3 | pages = 50–8 | year = 2006 | pmid = 16612114 | doi = 10.1159/000091506 }}
{{refend}}


== External links ==
== External links ==
* {{MeshName|Insulin-Like+Growth+Factor+II}}
* {{MeshName|Insulin-Like+Growth+Factor+II}}


==References==
{{PDB Gallery|geneid=3481}}
{{reflist}}
{{Growth factors}}
 
{{Hormones}}
==Further reading==
{{Growth factor receptor modulators}}
{{refbegin | 2}}
{{Signaling peptide/protein receptor modulators}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=O'Dell SD, Day IN |title=Insulin-like growth factor II (IGF-II). |journal=Int. J. Biochem. Cell Biol. |volume=30 |issue= 7 |pages= 767-71 |year= 1998 |pmid= 9722981 |doi=  }}
*{{cite journal  | author=Butler AA, Yakar S, Gewolb IH, ''et al.'' |title=Insulin-like growth factor-I receptor signal transduction: at the interface between physiology and cell biology. |journal=Comp. Biochem. Physiol. B, Biochem. Mol. Biol. |volume=121 |issue= 1 |pages= 19-26 |year= 1999 |pmid= 9972281 |doi=  }}
*{{cite journal  | author=Kalli KR, Conover CA |title=The insulin-like growth factor/insulin system in epithelial ovarian cancer. |journal=Front. Biosci. |volume=8 |issue=  |pages= d714-22 |year= 2004 |pmid= 12700030 |doi=  }}
*{{cite journal  | author=Wood AW, Duan C, Bern HA |title=Insulin-like growth factor signaling in fish. |journal=Int. Rev. Cytol. |volume=243 |issue=  |pages= 215-85 |year= 2005 |pmid= 15797461 |doi= 10.1016/S0074-7696(05)43004-1 }}
*{{cite journal  | author=Fowden AL, Sibley C, Reik W, Constancia M |title=Imprinted genes, placental development and fetal growth. |journal=Horm. Res. |volume=65 Suppl 3 |issue=  |pages= 50-8 |year= 2006 |pmid= 16612114 |doi= 10.1159/000091506 }}
}}
{{refend}}


{{Hormones}}
{{DEFAULTSORT:Insulin-Like Growth Factor 2}}


[[Category:Peptide hormones]]
[[Category:Peptide hormones]]
[[Category:Growth factors]]
[[Category:Growth factors]]
[[Category:Endocrinology]]
[[Category:Hormones of the somatotropic axis]]
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[[Category:Insulin receptor agonists]]
 
[[he:IGF-2]]

Latest revision as of 05:08, 21 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
Insulin-like growth factor II E-peptide (somatomedians-A )
Identifiers
SymbolIGF2_C
PfamPF08365
InterProIPR013576

Insulin-like growth factor 2 (IGF-2) is one of three protein hormones that share structural similarity to insulin. The MeSH definition reads: "A well-characterized neutral peptide believed to be secreted by the liver and to circulate in the blood. It has growth-regulating, insulin-like and mitogenic activities. The growth factor has a major, but not absolute, dependence on somatotropin. It is believed to be a major fetal growth factor in contrast to Insulin-like growth factor 1, which is a major growth factor in adults".[1]

Gene structure

In humans, the IGF2 gene is located on chromosome 11p15.5, a region which contains numerous imprinted genes. In mice this homologous region is found at distal chromosome 7. In both organisms, Igf2 is imprinted, with expression resulting favourably from the paternally inherited allele. However, in some human brain regions a loss of imprinting occurs resulting in both IGF2 and H19 being transcribed from both parental alleles.[2]

The protein CTCF is involved in repressing expression of the gene, by binding to the H19 imprinting control region (ICR) along with Differentially-methylated Region-1 (DMR1) and Matrix Attachment Region -3 (MAR3). These three DNA sequences bind to CTCF in a way that limits downstream enhancer access to the Igf2 region. The mechanism in which CTCF binds to these regions is currently unknown, but could include either a direct DNA-CTCF interaction or it could possibly be mediated by other proteins. In mammals (mice, humans, pigs), only the allele for insulin-like growth factor-2 (IGF2) inherited from one's father is active; that inherited from the mother is not — a phenomenon called imprinting.The mechanism: the mother's allele has an insulator between the IGF2 promoter and enhancer. So does the father's allele, but in his case, the insulator has been methylated. CTCF can no longer bind to the insulator, and so the enhancer is now free to turn on the father's IGF2 promoter.[citation needed]

Function

The major role of IGF-2 is as a growth promoting hormone during gestation.

IGF-2 exerts its effects by binding to the IGF-1 receptor and to the short isoform of the insulin receptor (IR-A or exon 11-).[3] IGF2 may also bind to the IGF-2 receptor (also called the cation-independent mannose 6-phosphate receptor), which acts as a signalling antagonist; that is, to prevent IGF2 responses.

In the process of folliculogenesis, IGF-2 is created by thecal cells to act in an autocrine manner on the theca cells themselves, and in a paracrine manner on granulosa cells in the ovary.[citation needed] IGF2 promotes granulosa cell proliferation during the follicular phase of the menstrual cycle, acting alongside follicle stimulating hormone (FSH).[4] After ovulation has occurred, IGF-2 promotes progesterone secretion during the luteal phase of the menstrual cycle, together with luteinizing hormone (LH). Thus, IGF2 acts as a co-hormone together with both FSH and LH.[5]

A study at the Mount Sinai School of Medicine found that IGF-2 may be linked to memory and reproduction.[6] A study at the European Neuroscience Institute-Goettingen (Germany) found that fear extinction-induced IGF2/IGFBP7 signalling promotes the survival of 17- to 19-day-old newborn hippocampal neurons. This suggests that therapeutic strategies that enhance IGF2 signalling and adult neurogenesis might be suitable to treat diseases linked to excessive fear memory such as PTSD.[7]

Clinical relevance

It is sometimes produced in excess in islet cell tumors and non-islet hypoglycemic cell tumors, causing hypoglycemia. Doege-Potter syndrome is a paraneoplastic syndrome[8] in which hypoglycemia is associated with the presence of one or more non-islet fibrous tumors in the pleural cavity. Loss of imprinting of IGF2 is a common feature in tumors seen in Beckwith-Wiedemann syndrome. As IGF2 promotes development of fetal pancreatic beta cells, it is believed to be related to some forms of diabetes mellitus. Preeclampsia induces a decrease in methylation level at IGF2 demethylated region, and this might be among the mechanisms behind the association between intrauterine exposure to preeclampsia and high risk for metabolic diseases in the later life of the infants.[9]

Interactions

Insulin-like growth factor 2 has been shown to interact with IGFBP3[10][11][12][13] and transferrin.[10]

See also

References

  1. ↑ "Insulin-Like Growth Factor II". MeSH. NCBI.
  2. ↑ Pham NV, Nguyen MT, Hu JF, Vu TH, Hoffman AR (Nov 1998). "Dissociation of IGF2 and H19 imprinting in human brain". Brain Research. 810 (1–2): 1–8. doi:10.1016/s0006-8993(98)00783-5. PMID 9813220.
  3. ↑ Frasca F, Pandini G, Scalia P, Sciacca L, Mineo R, Costantino A, Goldfine ID, Belfiore A, Vigneri R (1999). "Insulin receptor isoform A, a newly recognized, high-affinity insulin-like growth factor II receptor in fetal and cancer cells". Molecular and Cellular Biology. 19 (5): 3278–88. doi:10.1128/MCB.19.5.3278. PMC 84122. PMID 10207053.
  4. ↑ Neidhart, M (2016). DNA Methylation and Complex Human Disease (1st ed.). San Diego: Academic Press. p. 222. ISBN 9780124201941.
  5. ↑ Neidhart, M (2016). DNA Methylation and Complex Human Disease (1st ed.). San Diego: Academic Press. p. 22. ISBN 978-0124201941.
  6. ↑ Chen DY, Stern SA, Garcia-Osta A, Saunier-Rebori B, Pollonini G, Bambah-Mukku D, Blitzer RD, Alberini CM (Jan 2011). "A critical role for IGF-II in memory consolidation and enhancement". Nature. 469 (7331): 491–7. doi:10.1038/nature09667. PMC 3908455. PMID 21270887.
  7. ↑ Agis-Balboa RC, Arcos-Diaz D, Wittnam J, Govindarajan N, Blom K, Burkhardt S, Haladyniak U, Agbemenyah HY, Zovoilis A, Salinas-Riester G, Opitz L, Sananbenesi F, Fischer A (Oct 2011). "A hippocampal insulin-growth factor 2 pathway regulates the extinction of fear memories". The EMBO Journal. 30 (19): 4071–83. doi:10.1038/emboj.2011.293. PMC 3209781. PMID 21873981.
  8. ↑ Balduyck B, Lauwers P, Govaert K, Hendriks J, De Maeseneer M, Van Schil P (Jul 2006). "Solitary fibrous tumor of the pleura with associated hypoglycemia: Doege-Potter syndrome: a case report". Journal of Thoracic Oncology. 1 (6): 588–90. doi:10.1097/01243894-200607000-00016. PMID 17409923.
  9. ↑ He J, Zhang A, Fang M, Fang R, Ge J, Jiang Y, Zhang H, Han C, Ye X, Yu D, Huang H, Liu Y, Dong M (12 July 2013). "Methylation levels at IGF2 and GNAS DMRs in infants born to preeclamptic pregnancies". BMC Genomics. 14: 472. doi:10.1186/1471-2164-14-472. PMC 3723441. PMID 23844573.
  10. ↑ 10.0 10.1 Storch S, Kübler B, Höning S, Ackmann M, Zapf J, Blum W, Braulke T (Dec 2001). "Transferrin binds insulin-like growth factors and affects binding properties of insulin-like growth factor binding protein-3". FEBS Letters. 509 (3): 395–8. doi:10.1016/S0014-5793(01)03204-5. PMID 11749962.
  11. ↑ Buckway CK, Wilson EM, Ahlsén M, Bang P, Oh Y, Rosenfeld RG (Oct 2001). "Mutation of three critical amino acids of the N-terminal domain of IGF-binding protein-3 essential for high affinity IGF binding". The Journal of Clinical Endocrinology and Metabolism. 86 (10): 4943–50. doi:10.1210/jcem.86.10.7936. PMID 11600567.
  12. ↑ Twigg SM, Baxter RC (Mar 1998). "Insulin-like growth factor (IGF)-binding protein 5 forms an alternative ternary complex with IGFs and the acid-labile subunit". The Journal of Biological Chemistry. 273 (11): 6074–9. doi:10.1074/jbc.273.11.6074. PMID 9497324.
  13. ↑ Firth SM, Ganeshprasad U, Baxter RC (Jan 1998). "Structural determinants of ligand and cell surface binding of insulin-like growth factor-binding protein-3". The Journal of Biological Chemistry. 273 (5): 2631–8. doi:10.1074/jbc.273.5.2631. PMID 9446566.

Further reading

  • O'Dell SD, Day IN (Jul 1998). "Insulin-like growth factor II (IGF-II)". The International Journal of Biochemistry & Cell Biology. 30 (7): 767–71. doi:10.1016/S1357-2725(98)00048-X. PMID 9722981.
  • Butler AA, Yakar S, Gewolb IH, Karas M, Okubo Y, LeRoith D (Sep 1998). "Insulin-like growth factor-I receptor signal transduction: at the interface between physiology and cell biology". Comparative Biochemistry and Physiology B. 121 (1): 19–26. doi:10.1016/S0305-0491(98)10106-2. PMID 9972281.
  • Kalli KR, Conover CA (May 2003). "The insulin-like growth factor/insulin system in epithelial ovarian cancer". Frontiers in Bioscience. 8: d714–22. doi:10.2741/1034. PMID 12700030.
  • Wood AW, Duan C, Bern HA (2005). "Insulin-like growth factor signaling in fish". International Review of Cytology. 243: 215–85. doi:10.1016/S0074-7696(05)43004-1. PMID 15797461.
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External links

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