ITGA9
From Wikipedia, the free encyclopedia
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Integrin, alpha 9
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| Identifiers | ||||||||||||||
| Symbol(s) | ITGA9; ALPHA-RLC; ITGA4L; RLC | |||||||||||||
| External IDs | OMIM: 603963 MGI: 104756 HomoloGene: 1664 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 3680 | 104099 | ||||||||||||
| Ensembl | ENSG00000144668 | ENSMUSG00000039115 | ||||||||||||
| Uniprot | Q13797 | n/a | ||||||||||||
| Refseq | NM_002207 (mRNA) NP_002198 (protein) |
XM_985968 (mRNA) XP_991062 (protein) |
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| Location | Chr 3: 37.47 - 37.84 Mb | Chr 9: 118.46 - 118.75 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
Integrin, alpha 9, also known as ITGA9, is a human gene.[1]
This gene encodes an alpha integrin. Integrins are heterodimeric integral membrane glycoproteins composed of an alpha chain and a beta chain that mediate cell-cell and cell-matrix adhesion. The protein encoded by this gene, when bound to the beta 1 chain, forms an integrin that is a receptor for VCAM1, cytotactin and osteopontin. Expression of this gene has been found to be upregulated in small cell lung cancers.[1]
[edit] References
[edit] Further reading
- Evans JP (2001). "Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization.". Bioessays 23 (7): 628–39. doi:. PMID 11462216.
- Palmer EL, Rüegg C, Ferrando R, et al. (1994). "Sequence and tissue distribution of the integrin alpha 9 subunit, a novel partner of beta 1 that is widely distributed in epithelia and muscle.". J. Cell Biol. 123 (5): 1289–97. PMID 8245132.
- Hibi K, Yamakawa K, Ueda R, et al. (1994). "Aberrant upregulation of a novel integrin alpha subunit gene at 3p21.3 in small cell lung cancer.". Oncogene 9 (2): 611–9. PMID 8290272.
- Yamakawa K, Takahashi T, Horio Y, et al. (1993). "Frequent homozygous deletions in lung cancer cell lines detected by a DNA marker located at 3p21.3-p22.". Oncogene 8 (2): 327–30. PMID 8381220.
- Yokosaki Y, Monis H, Chen J, Sheppard D (1996). "Differential effects of the integrins alpha9beta1, alphavbeta3, and alphavbeta6 on cell proliferative responses to tenascin. Roles of the beta subunit extracellular and cytoplasmic domains.". J. Biol. Chem. 271 (39): 24144–50. PMID 8798654.
- Yokosaki Y, Matsuura N, Sasaki T, et al. (2000). "The integrin alpha(9)beta(1) binds to a novel recognition sequence (SVVYGLR) in the thrombin-cleaved amino-terminal fragment of osteopontin.". J. Biol. Chem. 274 (51): 36328–34. PMID 10593924.
- Young BA, Taooka Y, Liu S, et al. (2002). "The cytoplasmic domain of the integrin alpha9 subunit requires the adaptor protein paxillin to inhibit cell spreading but promotes cell migration in a paxillin-independent manner.". Mol. Biol. Cell 12 (10): 3214–25. PMID 11598204.
- Eto K, Huet C, Tarui T, et al. (2002). "Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta 1: implications for sperm-egg binding and other cell interactions.". J. Biol. Chem. 277 (20): 17804–10. doi:. PMID 11882657.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:. PMID 12477932.
- Majumdar M, Tarui T, Shi B, et al. (2004). "Plasmin-induced migration requires signaling through protease-activated receptor 1 and integrin alpha(9)beta(1).". J. Biol. Chem. 279 (36): 37528–34. doi:. PMID 15247268.
- Chen C, Young BA, Coleman CS, et al. (2004). "Spermidine/spermine N1-acetyltransferase specifically binds to the integrin alpha9 subunit cytoplasmic domain and enhances cell migration.". J. Cell Biol. 167 (1): 161–70. doi:. PMID 15479742.
- Vlahakis NE, Young BA, Atakilit A, Sheppard D (2005). "The lymphangiogenic vascular endothelial growth factors VEGF-C and -D are ligands for the integrin alpha9beta1.". J. Biol. Chem. 280 (6): 4544–52. doi:. PMID 15590642.
- Yokosaki Y, Tanaka K, Higashikawa F, et al. (2005). "Distinct structural requirements for binding of the integrins alphavbeta6, alphavbeta3, alphavbeta5, alpha5beta1 and alpha9beta1 to osteopontin.". Matrix Biol. 24 (6): 418–27. doi:. PMID 16005200.
- Gulubova M, Vlaykova T (2006). "Immunohistochemical assessment of fibronectin and tenascin and their integrin receptors alpha5beta1 and alpha9beta1 in gastric and colorectal cancers with lymph node and liver metastases.". Acta Histochem. 108 (1): 25–35. doi:. PMID 16430945.

