COL18A1

From Wikipedia, the free encyclopedia

Collagen, type XVIII, alpha 1

PDB rendering based on 1bnl.

Available structures: 1bnl

Identifiers

Symbol(s)

COL18A1; FLJ27325; KNO; MGC74745

External IDs

OMIM: 120328 MGI: 88451 HomoloGene: 7673

Gene ontology
Molecular Function:	• extracellular matrix structural constituent • protein binding • zinc ion binding • metal ion binding
Cellular Component:	• collagen • cytoplasm
Biological Process:	• phosphate transport • cell adhesion • visual perception • negative regulation of cell proliferation • organ morphogenesis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_030582 (mRNA)
NP_085059 (protein)

NM_009929 (mRNA)
NP_034059 (protein)

Location

Chr 21: 45.65 - 45.76 Mb

Chr 10: 76.5 - 76.61 Mb

Pubmed search

[1]

[2]

Collagen, type XVIII, alpha 1, also known as COL18A1, is a human gene.

This gene encodes the alpha chain of type XVIII collagen. This collagen is one of the multiplexins, extracellular matrix proteins that contain multiple triple-helix domains (collagenous domains) interrupted by non-collagenous domains. The proteolytically produced C-terminal fragment of type XVIII collagen is endostatin, a potent antiangiogenic protein. Mutations in this gene are associated with Knobloch syndrome. The main features of this syndrome involve retinal abnormalities so type XVIII collagen may play an important role in retinal structure and in neural tube closure. Two transcript variants encoding different isoforms have been found for this gene.^[1]

[edit] See also

Collagen

[edit] References

^ Entrez Gene: COL18A1 collagen, type XVIII, alpha 1.

[edit] Further reading

Pufe T, Kurz B, Petersen W, et al. (2006). "The influence of biomechanical parameters on the expression of VEGF and endostatin in the bone and joint system.". Ann. Anat. 187 (5-6): 461–72. PMID 16320826.
Oh SP, Kamagata Y, Muragaki Y, et al. (1994). "Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteins.". Proc. Natl. Acad. Sci. U.S.A. 91 (10): 4229–33. PMID 8183893.
Oh SP, Warman ML, Seldin MF, et al. (1994). "Cloning of cDNA and genomic DNA encoding human type XVIII collagen and localization of the alpha 1(XVIII) collagen gene to mouse chromosome 10 and human chromosome 21.". Genomics 19 (3): 494–9. doi:10.1006/geno.1994.1098. PMID 8188291.
Sertié AL, Quimby M, Moreira ES, et al. (1996). "A gene which causes severe ocular alterations and occipital encephalocele (Knobloch syndrome) is mapped to 21q22.3.". Hum. Mol. Genet. 5 (6): 843–7. PMID 8776601.
O'Reilly MS, Boehm T, Shing Y, et al. (1997). "Endostatin: an endogenous inhibitor of angiogenesis and tumor growth.". Cell 88 (2): 277–85. PMID 9008168.
Saarela J, Ylikärppä R, Rehn M, et al. (1998). "Complete primary structure of two variant forms of human type XVIII collagen and tissue-specific differences in the expression of the corresponding transcripts.". Matrix Biol. 16 (6): 319–28. PMID 9503365.
Ding YH, Javaherian K, Lo KM, et al. (1998). "Zinc-dependent dimers observed in crystals of human endostatin.". Proc. Natl. Acad. Sci. U.S.A. 95 (18): 10443–8. PMID 9724722.
Sasaki T, Göhring W, Miosge N, et al. (1999). "Tropoelastin binding to fibulins, nidogen-2 and other extracellular matrix proteins.". FEBS Lett. 460 (2): 280–4. PMID 10544250.
Felbor U, Dreier L, Bryant RA, et al. (2000). "Secreted cathepsin L generates endostatin from collagen XVIII.". EMBO J. 19 (6): 1187–94. doi:10.1093/emboj/19.6.1187. PMID 10716919.
Hattori M, Fujiyama A, Taylor TD, et al. (2000). "The DNA sequence of human chromosome 21.". Nature 405 (6784): 311–9. doi:10.1038/35012518. PMID 10830953.
Sertié AL, Sossi V, Camargo AA, et al. (2000). "Collagen XVIII, containing an endogenous inhibitor of angiogenesis and tumor growth, plays a critical role in the maintenance of retinal structure and in neural tube closure (Knobloch syndrome).". Hum. Mol. Genet. 9 (13): 2051–8. PMID 10942434.
Rehn M, Veikkola T, Kukk-Valdre E, et al. (2001). "Interaction of endostatin with integrins implicated in angiogenesis.". Proc. Natl. Acad. Sci. U.S.A. 98 (3): 1024–9. doi:10.1073/pnas.031564998. PMID 11158588.
Karumanchi SA, Jha V, Ramchandran R, et al. (2001). "Cell surface glypicans are low-affinity endostatin receptors.". Mol. Cell 7 (4): 811–22. PMID 11336704.
Feng Y, Cui LB, Liu CX, Ma QJ (2001). "[Inhibition effect in vitro of purified endostatin expressed in Pichia pastoris]". Sheng Wu Gong Cheng Xue Bao 17 (3): 278–82. PMID 11517600.
Iughetti P, Suzuki O, Godoi PH, et al. (2001). "A polymorphism in endostatin, an angiogenesis inhibitor, predisposes for the development of prostatic adenocarcinoma.". Cancer Res. 61 (20): 7375–8. PMID 11606364.
Wu P, Yonekura H, Li H, et al. (2001). "Hypoxia down-regulates endostatin production by human microvascular endothelial cells and pericytes.". Biochem. Biophys. Res. Commun. 288 (5): 1149–54. doi:10.1006/bbrc.2001.5903. PMID 11700031.
Zorick TS, Mustacchi Z, Bando SY, et al. (2002). "High serum endostatin levels in Down syndrome: implications for improved treatment and prevention of solid tumours.". Eur. J. Hum. Genet. 9 (11): 811–4. doi:10.1038/sj.ejhg.5200721. PMID 11781696.
Hanai J, Dhanabal M, Karumanchi SA, et al. (2002). "Endostatin causes G1 arrest of endothelial cells through inhibition of cyclin D1.". J. Biol. Chem. 277 (19): 16464–9. doi:10.1074/jbc.M112274200. PMID 11815623.
Ergün S, Kilic N, Wurmbach JH, et al. (2002). "Endostatin inhibits angiogenesis by stabilization of newly formed endothelial tubes.". Angiogenesis 4 (3): 193–206. PMID 11911017.
Tomono Y, Naito I, Ando K, et al. (2002). "Epitope-defined monoclonal antibodies against multiplexin collagens demonstrate that type XV and XVIII collagens are expressed in specialized basement membranes.". Cell Struct. Funct. 27 (1): 9–20. PMID 11937714.