COL11A2

COL11A2
Identificadores
Nomes alternativosCOL11A2
IDs externosOMIM: 120290 HomoloGene: 22547 GeneCards: COL11A2
Doenças Geneticamente Relacionadas
Displasia oto-espondilo-megaepifisária, autosomal dominant nonsyndromic deafness 13, autosomal recessive nonsyndromic deafness 53, Stickler syndrome type 3
Wikidata
Ver/Editar Humano

A cadeia alfa-2, tipo XI, do colagénio é uma proteína que em humanos é codificada pelo gene COL11A2. O gene COL11A2 produz um componente desse tipo de colágeno, chamado de cadeia pró-alfa2 (XI). O colágeno tipo XI adiciona estrutura e força aos tecidos que sustentam os músculos, articulações, órgãos e pele do corpo (o tecido conjuntivo). O colágeno tipo XI é normalmente encontrado na cartilagem, bem como no fluido que preenche o globo ocular, o ouvido interno e a porção central dos discos entre as vértebras da coluna (núcleo pulposo).

O gene COL11A2 está localizado no braço curto (p) do cromossomo 6 na posição 21.3, do par de bases 33.238.446 até o par de bases 33.268.222.

Leitura adicional

  • Kuivaniemi H, Tromp G, Prockop DJ (1997). «Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels». Human Mutation. 9 (4): 300–15. PMID 9101290. doi:10.1002/(SICI)1098-1004(1997)9:4<300::AID-HUMU2>3.0.CO;2-9 
  • Van Camp G, Willems PJ, Smith RJ (abril de 1997). «Nonsyndromic hearing impairment: unparalleled heterogeneity». American Journal of Human Genetics. 60 (4): 758–64. PMC 1712474Acessível livremente. PMID 9106521 
  • Hanson IM, Gorman P, Lui VC, Cheah KS, Solomon E, Trowsdale J (novembro de 1989). «The human alpha 2(XI) collagen gene (COL11A2) maps to the centromeric border of the major histocompatibility complex on chromosome 6». Genomics. 5 (4): 925–31. PMID 2591970. doi:10.1016/0888-7543(89)90135-3 
  • Kimura T, Cheah KS, Chan SD, Lui VC, Mattei MG, van der Rest M, Ono K, Solomon E, Ninomiya Y, Olsen BR (agosto de 1989). «The human alpha 2(XI) collagen (COL11A2) chain. Molecular cloning of cDNA and genomic DNA reveals characteristics of a fibrillar collagen with differences in genomic organization». The Journal of Biological Chemistry. 264 (23): 13910–6. PMID 2760050 
  • Keene DR, Oxford JT, Morris NP (outubro de 1995). «Ultrastructural localization of collagen types II, IX, and XI in the growth plate of human rib and fetal bovine epiphyseal cartilage: type XI collagen is restricted to thin fibrils». The Journal of Histochemistry and Cytochemistry. 43 (10): 967–79. PMID 7560887. doi:10.1177/43.10.7560887 
  • Zhidkova NI, Justice SK, Mayne R (abril de 1995). «Alternative mRNA processing occurs in the variable region of the pro-alpha 1(XI) and pro-alpha 2(XI) collagen chains». The Journal of Biological Chemistry. 270 (16): 9486–93. PMID 7721876. doi:10.1074/jbc.270.16.9486 
  • Tsumaki N, Kimura T (fevereiro de 1995). «Differential expression of an acidic domain in the amino-terminal propeptide of mouse pro-alpha 2(XI) collagen by complex alternative splicing». The Journal of Biological Chemistry. 270 (5): 2372–8. PMID 7836472. doi:10.1074/jbc.270.5.2372 
  • Vikkula M, Mariman EC, Lui VC, Zhidkova NI, Tiller GE, Goldring MB, van Beersum SE, de Waal Malefijt MC, van den Hoogen FH, Ropers HH (fevereiro de 1995). «Autosomal dominant and recessive osteochondrodysplasias associated with the COL11A2 locus». Cell. 80 (3): 431–7. PMID 7859284. doi:10.1016/0092-8674(95)90493-X 
  • Zhidkova NI, Brewton RG, Mayne R (julho de 1993). «Molecular cloning of PARP (proline/arginine-rich protein) from human cartilage and subsequent demonstration that PARP is a fragment of the NH2-terminal domain of the collagen alpha 2(XI) chain». FEBS Letters. 326 (1-3): 25–8. PMID 8325374. doi:10.1016/0014-5793(93)81753-M 
  • Lui VC, Ng LJ, Sat EW, Nicholls J, Cheah KS (julho de 1996). «Extensive alternative splicing within the amino-propeptide coding domain of alpha2(XI) procollagen mRNAs. Expression of transcripts encoding truncated pro-alpha chains». The Journal of Biological Chemistry. 271 (28): 16945–51. PMID 8663204. doi:10.1074/jbc.271.28.16945 
  • Lui VC, Ng LJ, Sat EW, Cheah KS (março de 1996). «The human alpha 2(XI) collagen gene (COL11A2): completion of coding information, identification of the promoter sequence, and precise localization within the major histocompatibility complex reveal overlap with the KE5 gene». Genomics. 32 (3): 401–12. PMID 8838804. doi:10.1006/geno.1996.0135 
  • van Steensel MA, Buma P, de Waal Malefijt MC, van den Hoogen FH, Brunner HG (junho de 1997). «Oto- spondylo-megaepiphyseal dysplasia (OSMED): clinical description of three patients homozygous for a missense mutation in the COL11A2 gene». American Journal of Medical Genetics. 70 (3): 315–23. PMID 9188673. doi:10.1002/(SICI)1096-8628(19970613)70:3<315::AID-AJMG19>3.0.CO;2-O 
  • Sirko-Osadsa DA, Murray MA, Scott JA, Lavery MA, Warman ML, Robin NH (fevereiro de 1998). «Stickler syndrome without eye involvement is caused by mutations in COL11A2, the gene encoding the alpha2(XI) chain of type XI collagen». The Journal of Pediatrics. 132 (2): 368–71. PMID 9506662. doi:10.1016/S0022-3476(98)70466-4 
  • Koga H, Sakou T, Taketomi E, Hayashi K, Numasawa T, Harata S, Yone K, Matsunaga S, Otterud B, Inoue I, Leppert M (junho de 1998). «Genetic mapping of ossification of the posterior longitudinal ligament of the spine». American Journal of Human Genetics. 62 (6): 1460–7. PMC 1377147Acessível livremente. PMID 9585596. doi:10.1086/301868 
  • Pihlajamaa T, Prockop DJ, Faber J, Winterpacht A, Zabel B, Giedion A, Wiesbauer P, Spranger J, Ala-Kokko L (novembro de 1998). «Heterozygous glycine substitution in the COL11A2 gene in the original patient with the Weissenbacher-Zweymüller syndrome demonstrates its identity with heterozygous OSMED (nonocular Stickler syndrome)». American Journal of Medical Genetics. 80 (2): 115–20. PMID 9805126. doi:10.1002/(SICI)1096-8628(19981102)80:2<115::AID-AJMG5>3.0.CO;2-O 
  • Melkoniemi M, Brunner HG, Manouvrier S, Hennekam R, Superti-Furga A, Kääriäinen H, Pauli RM, van Essen T, Warman ML, Bonaventure J, Miny P, Ala-Kokko L (fevereiro de 2000). «Autosomal recessive disorder otospondylomegaepiphyseal dysplasia is associated with loss-of-function mutations in the COL11A2 gene». American Journal of Human Genetics. 66 (2): 368–77. PMC 1288089Acessível livremente. PMID 10677296. doi:10.1086/302750 
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  1. ↑ «Doenças geneticamente associadas a COL11A2 ver/editar referências no wikidata»
  2. ↑ «Human PubMed Reference:»
  3. ↑ Vuristo MM, Pihlajamaa T, Vandenberg P, Prockop DJ, Ala-Kokko L (setembro de 1995). «The human COL11A2 gene structure indicates that the gene has not evolved with the genes for the major fibrillar collagens». The Journal of Biological Chemistry. 270 (39): 22873–81. PMID 7559422. doi:10.1074/jbc.270.39.22873
  4. ↑ McGuirt WT, Prasad SD, Griffith AJ, Kunst HP, Green GE, Shpargel KB, Runge C, Huybrechts C, Mueller RF, Lynch E, King MC, Brunner HG, Cremers CW, Takanosu M, Li SW, Arita M, Mayne R, Prockop DJ, Van Camp G, Smith RJ (dezembro de 1999). «Mutations in COL11A2 cause non-syndromic hearing loss (DFNA13)». Nature Genetics. 23 (4): 413–9. PMID 10581026. doi:10.1038/70516
  5. ↑ «Entrez Gene: COL11A2 collagen, type XI, alpha 2»