COL25A1

From Wikipedia, the free encyclopedia

Collagen, type XXV, alpha 1

Identifiers

External IDs

OMIM: 610004 MGI: 1924268 HomoloGene: 57111

Gene ontology
Molecular Function:	• beta-amyloid binding • heparin binding
Cellular Component:	• extracellular region • extracellular space • cytoplasm • integral to plasma membrane • membrane
Biological Process:	• phosphate transport

Orthologs

Human

Mouse

Refseq

NM_032518 (mRNA)
NP_115907 (protein)

NM_029838 (mRNA)
NP_084114 (protein)

Location

Chr 4: 109.96 - 110.44 Mb

Chr 3: 130.17 - 130.58 Mb

Pubmed search

[1]

[2]

Collagen, type XXV, alpha 1, also known as COL25A1, is a human gene.^[1]

COL25A1 is a brain-specific membrane-bound collagen. Proteolytic processing releases CLAC, a soluble form of COL25A1 containing the extracellular collagen domains that associates with senile plaques in Alzheimer disease (AD; MIM 104300) brains (Osada et al., 2005).[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: COL25A1 collagen, type XXV, alpha 1.

[edit] Further reading

Kakuyama H, Söderberg L, Horigome K, et al. (2006). "CLAC binds to aggregated Abeta and Abeta fragments, and attenuates fibril elongation.". Biochemistry 44 (47): 15602-9. doi:10.1021/bi051263e. PMID 16300410.
Söderberg L, Dahlqvist C, Kakuyama H, et al. (2005). "Collagenous Alzheimer amyloid plaque component assembles amyloid fibrils into protease resistant aggregates.". FEBS J. 272 (9): 2231-6. doi:10.1111/j.1742-4658.2005.04647.x. PMID 15853808.
Osada Y, Hashimoto T, Nishimura A, et al. (2005). "CLAC binds to amyloid beta peptides through the positively charged amino acid cluster within the collagenous domain 1 and inhibits formation of amyloid fibrils.". J. Biol. Chem. 280 (9): 8596-605. doi:10.1074/jbc.M413340200. PMID 15615705.
Söderberg L, Kakuyama H, Möller A, et al. (2005). "Characterization of the Alzheimer's disease-associated CLAC protein and identification of an amyloid beta-peptide-binding site.". J. Biol. Chem. 280 (2): 1007-15. doi:10.1074/jbc.M403628200. PMID 15522881.
Kowa H, Sakakura T, Matsuura Y, et al. (2004). "Mostly separate distributions of CLAC- versus Abeta40- or thioflavin S-reactivities in senile plaques reveal two distinct subpopulations of beta-amyloid deposits.". Am. J. Pathol. 165 (1): 273-81. PMID 15215182.
Söderberg L, Zhukareva V, Bogdanovic N, et al. (2004). "Molecular identification of AMY, an Alzheimer disease amyloid-associated protein.". J. Neuropathol. Exp. Neurol. 62 (11): 1108-17. PMID 14656069.
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:10.1073/pnas.242603899. PMID 12477932.
Hashimoto T, Wakabayashi T, Watanabe A, et al. (2002). "CLAC: a novel Alzheimer amyloid plaque component derived from a transmembrane precursor, CLAC-P/collagen type XXV.". EMBO J. 21 (7): 1524-34. doi:10.1093/emboj/21.7.1524. PMID 11927537.