Collagen, type XXV, alpha 1
| Collagen, type XXV, alpha 1 | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||||
| Symbols | COL25A1 ; AMY; CFEOM5; CLAC; CLAC-P; CLACP | ||||||||||||
| External IDs | OMIM: 610004 MGI: 1924268 HomoloGene: 57111 GeneCards: COL25A1 Gene | ||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 84570 | 77018 | |||||||||||
| Ensembl | ENSG00000188517 | ENSMUSG00000058897 | |||||||||||
| UniProt | Q9BXS0 | Q99MQ5 | |||||||||||
| RefSeq (mRNA) | NM_001256074 | NM_001244952 | |||||||||||
| RefSeq (protein) | NP_001243003 | NP_001231881 | |||||||||||
| Location (UCSC) |
Chr 4: 108.81 – 109.3 Mb |
Chr 3: 130.13 – 130.6 Mb | |||||||||||
| PubMed search | |||||||||||||
Collagen alpha-1(XXV) chain is a protein that in humans is encoded by the COL25A1 gene.[1][2]
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][2]
Interactions
Collagen, type XXV, alpha 1 has been shown to interact with Amyloid precursor protein.[1]
References
- 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. doi:10.1093/emboj/21.7.1524. PMC 125364. PMID 11927537.
- 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. 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. 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. 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. PMC 139241. PMID 12477932.
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