Collagen, type XXV, alpha 1
| COL25A1 | |||||||||||||||||
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| Identifiers | |||||||||||||||||
| Aliases | COL25A1, AMY, CLAC, CLAC-P, CLACP, CFEOM5, Collagen, type XXV, alpha 1, collagen type XXV alpha 1, collagen type XXV alpha 1 chain | ||||||||||||||||
| External IDs | MGI: 1924268 HomoloGene: 57111 GeneCards: COL25A1 | ||||||||||||||||
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| Orthologs | |||||||||||||||||
| Species | Human | Mouse | |||||||||||||||
| Entrez | |||||||||||||||||
| Ensembl | |||||||||||||||||
| UniProt | |||||||||||||||||
| RefSeq (mRNA) | |||||||||||||||||
| RefSeq (protein) | |||||||||||||||||
| Location (UCSC) | Chr 4: 108.81 – 109.3 Mb | Chr 3: 130.13 – 130.6 Mb | |||||||||||||||
| PubMed search | [1] | [2] | |||||||||||||||
| Wikidata | |||||||||||||||||
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Collagen alpha-1(XXV) chain is a protein that in humans is encoded by the COL25A1 gene.[3][4]
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][4]
Interactions
Collagen, type XXV, alpha 1 has been shown to interact with Amyloid precursor protein.[3]
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- 1 2 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. PMC 125364
. PMID 11927537. doi:10.1093/emboj/21.7.1524. - 1 2 "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. PMID 16300410. doi:10.1021/bi051263e.
- 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. PMID 15853808. doi:10.1111/j.1742-4658.2005.04647.x.
- 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. PMID 15615705. doi:10.1074/jbc.M413340200.
- 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. PMID 15522881. doi:10.1074/jbc.M403628200.
- 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. PMC 1618534 . PMID 15215182. doi:10.1016/s0002-9440(10)63295-6.
- 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. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
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