Protein found in humans
COL25A1 Identifiers Aliases COL25A1 External IDs OMIM : 610004 MGI : 1924268 HomoloGene : 57111 GeneCards : COL25A1 Wikidata
Collagen alpha-1(XXV) chain is a protein that in humans is encoded by the COL25A1 gene .[5] [6]
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][6]
Interactions Collagen, type XXV, alpha 1 has been shown to interact with Amyloid precursor protein .[5]
References
^ a b c GRCh38: Ensembl release 89: ENSG00000188517 – Ensembl , May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000058897 – Ensembl , May 2017^ "Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .^ "Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .^ a b Hashimoto T, Wakabayashi T, Watanabe A, Kowa H, Hosoda R, Nakamura A, Kanazawa I, Arai T, Takio K, Mann DM, Iwatsubo T (Apr 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 . PMC 125364 PMID 11927537 . ^ a b "Entrez Gene: COL25A1 collagen, type XXV, alpha 1" .
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 . hdl :10616/39314 PMID 15853808 . S2CID 26505595 . 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. doi :10.1016/s0002-9440(10)63295-6 . PMC 1618534 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. doi :10.1093/jnen/62.11.1108 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. Bibcode :2002PNAS...9916899M . doi :10.1073/pnas.242603899 PMC 139241 PMID 12477932 .
