Identification of a new collagen IV chain, α6(IV), by cDNA isolation and assignment of the gene to chromosome Xq22, which is the same locus for COL4A5

Toshitaka Oohashi, Manabu Sugimoto, Marie Genevieve Mattei, Yoshifumi Ninomiya

Research output: Contribution to journalArticle

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Abstract

To date, five distinct α chains have been identified in basement membrane collagen IV. We have cloned a gene encoding a new α chain belonging to basement membrane collagen IV by cDNA isolation under low stringency conditions. Isolation of overlapping clones and the technique of 5' rapid amplification of cDNA ends enabled us to derive the primary structure of the entire polypeptide. The deduced collagen polypeptide contained 1678 amino acid residues, including a 21-residue signal peptide, a 24-residue amino- terminal NC domain, a central 1405-residue collagenous (COL1) domain, and a 228-residue carboxyl-terminal NC1 domain. We have designated this newly found α chain as the α6(IV) chain. The gene was mapped to chromosome Xq22 by in situ hybridization of metaphase lymphocytes. This is the same region of chromosome X where the gene coding for the α5(IV) collagen chain (COL4A5) resides. Mutations in COL4A5 have been characterized in more than 50 patients with Alport syndrome. However, some of the X-linked cases of Alport syndrome are not apparently caused by COL4A5 mutations. The gene we describe in this paper therefore seems to be a candidate for mutations in this group of Alport syndrome patients.

Original languageEnglish
Pages (from-to)7520-7526
Number of pages7
JournalJournal of Biological Chemistry
Volume269
Issue number10
Publication statusPublished - Mar 11 1994

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Hereditary Nephritis
Chromosomes
Collagen
Complementary DNA
Genes
Basement Membrane
Mutation
X-Linked Genes
Peptides
Gene encoding
Lymphocytes
Metaphase
Protein Sorting Signals
In Situ Hybridization
Amplification
Clone Cells
Amino Acids

ASJC Scopus subject areas

  • Biochemistry

Cite this

Identification of a new collagen IV chain, α6(IV), by cDNA isolation and assignment of the gene to chromosome Xq22, which is the same locus for COL4A5. / Oohashi, Toshitaka; Sugimoto, Manabu; Mattei, Marie Genevieve; Ninomiya, Yoshifumi.

In: Journal of Biological Chemistry, Vol. 269, No. 10, 11.03.1994, p. 7520-7526.

Research output: Contribution to journalArticle

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abstract = "To date, five distinct α chains have been identified in basement membrane collagen IV. We have cloned a gene encoding a new α chain belonging to basement membrane collagen IV by cDNA isolation under low stringency conditions. Isolation of overlapping clones and the technique of 5' rapid amplification of cDNA ends enabled us to derive the primary structure of the entire polypeptide. The deduced collagen polypeptide contained 1678 amino acid residues, including a 21-residue signal peptide, a 24-residue amino- terminal NC domain, a central 1405-residue collagenous (COL1) domain, and a 228-residue carboxyl-terminal NC1 domain. We have designated this newly found α chain as the α6(IV) chain. The gene was mapped to chromosome Xq22 by in situ hybridization of metaphase lymphocytes. This is the same region of chromosome X where the gene coding for the α5(IV) collagen chain (COL4A5) resides. Mutations in COL4A5 have been characterized in more than 50 patients with Alport syndrome. However, some of the X-linked cases of Alport syndrome are not apparently caused by COL4A5 mutations. The gene we describe in this paper therefore seems to be a candidate for mutations in this group of Alport syndrome patients.",
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