Identification, characterization and expression analysis of a new fibrillar collagen gene, COL27A1

Matrix Biology

Volumn 22, Issue 1, 2003, Pages 3-14

  Pace, James M ^a   Corrado, Marcella ^b   Missero, Caterina ^b   Byers, Peter H ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

^b TELETHON INSTITUTE OF GENETICS AND MEDICINE TIGEM   (Italy)

Author keywords

Cartilage; COL27A1; Extracellular matrix (ECM); Fibrillar collagen; Type XXVII collagen

Indexed keywords

FIBRILLAR COLLAGEN; GLYCINE; MESSENGER RNA;

ALPHA CHAIN; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CARTILAGE; CHROMOSOME 4; CHROMOSOME 9Q; COL27A1 GENE; COLON; EAR; EXON; EXTRACELLULAR MATRIX; EYE; GENE; GENE EXPRESSION; GENE IDENTIFICATION; GENE LOCATION; GENE SEQUENCE; GENETIC CODE; LUNG; MOUSE; NEWBORN; NONHUMAN; NUCLEOTIDE REPEAT; NUCLEOTIDE SEQUENCE; PHYLOGENY; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; SPECIES DIFFERENCE; TISSUE DISTRIBUTION;

ALTERNATIVE SPLICING; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; EVOLUTION, MOLECULAR; FIBRILLAR COLLAGENS; GENE EXPRESSION PROFILING; HUMANS; MICE; MOLECULAR SEQUENCE DATA; PHYLOGENY; RNA, MESSENGER; SEQUENCE HOMOLOGY, NUCLEIC ACID;

EID: 0344088437     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(03)00007-6     Document Type: Article

References (30)

1. Altschul S.F., Madden T.L., Schäffer A.A., et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:1997;3389-3402.
2. Bernard M., Yoshioka H., Rodriguez E., et al. Cloning and sequencing of pro-α 1 (XI) collagen cDNA demonstrates that type XI belongs to the fibrillar class of collagens and reveals that the expression of the gene is not restricted to cartilagenous tissue. J. Biol. Chem. 263:1988;17159-17166.
3. Bulleid N.J., Wilson R., Lees J.F. Type-III procollagen assembly in semi-intact cells: chain association, nucleation and triple-helix folding do not require formation of inter-chain disulfide bonds but triple-helix nucleation does require hydroxylation. Biochem J. 317:(Pt. 1):1996;195-202.
4. Byers P.H. Disorders of collagen biosynthesis and structure. Scriver C.R., Beaudet A.L., Sly W.S., et al. The Metabolic and Molecular Bases of Inherited Disease. 2001;5241-5286 McGraw-Hill, New York.
5. Byers P.H. Folding defects in fibrillar collagens. Philos. Trans. R. Soc. Lond. B: Biol. Sci. 356:2001;151-157 discussion 157-158.
6. Cluzel C., Lethias C., Garrone R., Exposito J. Production in mammalian cells of chimeric human/sea urchin procollagen molecules displaying distinct versions of the minor triple helix. J. Biochem. 128:2000;957-963.
7. Farrell J., Siegel-Bartelt J., Teshima I. Patients with deletions of 9q22q34 do not define a syndrome: three case reports and a literature review. Clin. Genet. 40:1991;207-214.
8. Fitzgerald J., Bateman J.F. A new FACIT of the collagen family: COL21A1. FEBS Lett. 505:2001;275-280.
9. Hashimoto T., Wakabayashi T., Watanabe A., et al. CLAC: a novel Alzheimer amyloid plaque component derived from a transmembrane precursor, CLAC-P/collagen type XXV. EMBO J. 21:2002;1524-1534.
10. Horton W.A., Hecht J.T. Chondrodysplasias: disorders of cartilage matrix proteins. Royce P., Steinmann B. Connective Tissue and its Heritable Disorders: Molecular, Genetic and Medical Aspects. 2002;909-937 Wiley-Liss, Inc, New York.
11. Imamura Y., Scott I.C., Greenspan D.S. The pro-α 3(V) collagen chain. Complete primary structure, expression domains in adult and developing tissues, and comparison to the structures and expression domains of the other types V and XI procollagen chains. J. Biol. Chem. 275:2000;8749-8759.
12. Kent W.J. BLAT - the BLAST-like alignment tool. Genome Res. 12:2002;656-664.
13. Kent W.J., Sugnet C.W., Furey T.S., et al. The human genome browser at UCSC. Genome Res. 12:2002;996-1006.
14. Kielty C.M., Grant M.E. The collagen family: structure, assembly, and organization in the extracellular matrix. Royce P., Steinmann B. Connective Tissue and its Heritable Disorders: Molecular, Genetic and Medical Aspects. 2002;159-221 Wiley-Liss, Inc, New York.
15. Kimura T., Cheah K.S., Chan S.D., et al. The human α 2(XI) collagen (COL11A2) chain. Molecular cloning of cDNA and genomic DNA reveals characteristics of a fibrillar collagen with differences in genomic organization. J. Biol. Chem. 264:1989;13910-13916.
16. Koch M., Foley J.E., Hahn R., et al. α1(XX) collagen, a new member of the collagen subfamily, fibril-associated collagens with interrupted triple helices. J. Biol. Chem. 276:2001;23120-23126.
17. Lefebvre V., Garofalo S., Zhou G., Metsaranta M., Vuorio E., De Crombrugghe B. Characterization of primary cultures of chondrocytes from type II collagen/beta-galactosidase transgenic mice. Matrix Biol. 14:1994;329-335.
18. Mendell J.T., Dietz H.C. When the message goes awry: disease-producing mutations that influence mRNA content and performance. Cell. 107:2001;411-414.
19. Mustapha M., Chouery E., Chardenoux S., et al. DFNB31, a recessive form of sensorineural hearing loss, maps to chromosome 9q32-34. Eur. J. Hum. Genet. 10:2002;210-212.
20. Myllyharju J., Kivirikko K.I. Collagens and collagen-related diseases. Ann. Med. 33:2001;7-21.
21. Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O. Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 8:2001;85-95.
22. Pace J.M., Atkinson M., Willing M.C., Wallis G., Byers P.H. Deletions and duplications of Gly-Xaa-Yaa triplet repeats in the triple helical domains of type I collagen chains disrupt helix formation and result in several types of osteogenesis imperfecta. Hum. Mutat. 18:2001;319-326.
23. Paige A.J., Kiernan B.W., Varela A., et al. A deletion on chromosome 4 cosegregates with the whirler deafness mutation: exclusion of Orm1 as a candidate. Mamm. Genome. 11:2000;51-57.
24. Pearson W.R., Wood T., Zhang Z., Miller W. Comparison of DNA sequences with protein sequences. Genomics. 46:1997;24-36.
25. Riddle R.D., Johnson R.L., Laufer E., Tabin C. Sonic hedgehog mediates the polarizing activity of the ZPA. Cell. 75:1993;1401-1416.
26. Sato K., Yomogida K., Wada T., et al. Type XXVI collagen, a new member of the collagen family, is specifically expressed in the testis and ovary. J. Biol. Chem. 277:2002;37678-37684.
27. Shah N.K., Sharma M., Kirkpatrick A., Ramshaw A.M., Brodsky B. Gly-Gly-containing triplets of low stability adjacent to a type III collagen epitope. Biochemistry. 36:1997;5878-5883.
28. Takahara K., Hoffman G.G., Greenspan D.S. Complete structural organization of the human α 1 (V) collagen gene (COL5A1): divergence from the conserved organization of other characterized fibrillar collagen genes. Genomics. 29:1995;588-597.
29. Valkkila M., Melkoniemi M., Kvist L., Kuivaniemi H., Tromp G., Ala-Kokko L. Genomic organization of the human COL3A1 and COL5A2 genes: COL5A2 has evolved differently than the other minor fibrillar collagen genes. Matrix Biol. 20:2001;357-366.
30. Wilkin D.J., Mortier G.R., Johnson C.L., et al. Correlation of linkage data with phenotype in eight families with Stickler syndrome. Am. J. Med. Genet. 80:1998;121-127.