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Insulin-like growth factor 2: Wikis


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Insulin-like growth factor 2 (somatomedin A)

PDB rendering based on 1igl.
Available structures
Symbols IGF2; C11orf43; FLJ22066; FLJ44734; INSIGF; pp9974
External IDs OMIM147470 MGI96434 HomoloGene510 GeneCards: IGF2 Gene
RNA expression pattern
PBB GE IGF2 202409 at tn.png
PBB GE IGF2 202410 x at tn.png
PBB GE IGF2 210881 s at tn.png
More reference expression data
Species Human Mouse
Entrez 3481 16002
Ensembl ENSG00000167244 ENSMUSG00000048583
UniProt P01344 P09535
RefSeq (mRNA) NM_000612 NM_010514
RefSeq (protein) NP_000603 NP_034644
Location (UCSC) Chr 11:
2.11 - 2.13 Mb
Chr 7:
142.46 - 142.47 Mb
PubMed search [1] [2]

Insulin-like growth factor 2 (IGF-2) is one of three protein hormones that share structural similarity to insulin.


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.

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

Protein structure

IGF-2 exerts its effects by binding to the IGF-1 receptor. 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.


The major role of IGF2 is as a growth promoting hormone during gestation.


It is sometimes produced in non-islet cell tumours, causing hypoglycemia (Doege-Potter syndrome).

See also


Insulin-like growth factor 2 has been shown to interact with IGFBP3[1][2][3][4] and Transferrin.[1]


  1. ^ a b 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 Lett. (Netherlands) 509 (3): 395–8. ISSN 0014-5793. PMID 11749962.  
  2. ^ Buckway, C K; Wilson E M, Ahlsén M, Bang P, Oh Y, Rosenfeld R G (Oct. 2001). "Mutation of three critical amino acids of the N-terminal domain of IGF-binding protein-3 essential for high affinity IGF binding". J. Clin. Endocrinol. Metab. (United States) 86 (10): 4943–50. ISSN 0021-972X. PMID 11600567.  
  3. ^ Twigg, S M; Baxter R C (Mar. 1998). "Insulin-like growth factor (IGF)-binding protein 5 forms an alternative ternary complex with IGFs and the acid-labile subunit". J. Biol. Chem. (UNITED STATES) 273 (11): 6074–9. ISSN 0021-9258. PMID 9497324.  
  4. ^ Firth, S M; Ganeshprasad U, Baxter R C (Jan. 1998). "Structural determinants of ligand and cell surface binding of insulin-like growth factor-binding protein-3". J. Biol. Chem. (UNITED STATES) 273 (5): 2631–8. ISSN 0021-9258. PMID 9446566.  

External links

Further reading

  • O'Dell SD, Day IN (1998). "Insulin-like growth factor II (IGF-II).". Int. J. Biochem. Cell Biol. 30 (7): 767–71. doi:10.1016/S1357-2725(98)00048-X. PMID 9722981.  
  • Butler AA, Yakar S, Gewolb IH, et al. (1999). "Insulin-like growth factor-I receptor signal transduction: at the interface between physiology and cell biology.". Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 121 (1): 19–26. doi:10.1016/S0305-0491(98)10106-2. PMID 9972281.  
  • Kalli KR, Conover CA (2004). "The insulin-like growth factor/insulin system in epithelial ovarian cancer.". Front. Biosci. 8: d714–22. doi:10.2741/1034. PMID 12700030.  
  • Wood AW, Duan C, Bern HA (2005). "Insulin-like growth factor signaling in fish.". Int. Rev. Cytol. 243: 215–85. doi:10.1016/S0074-7696(05)43004-1. PMID 15797461.  
  • Fowden AL, Sibley C, Reik W, Constancia M (2006). "Imprinted genes, placental development and fetal growth.". Horm. Res. 65 Suppl 3: 50–8. doi:10.1159/000091506. PMID 16612114.  


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