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Human lysyl oxidase and type IV collagen alpha-5 chain. cDNA and genomic cloning, chromosomal localization and quantification of mRNAs for lysyl oxidase, and cDNA cloning of type IV collagen alpha-5 chain and identification of a mutation in the COL4A5 gene in a patient with Alport syndrome



Human lysyl oxidase and type IV collagen alpha-5 chain. cDNA and genomic cloning, chromosomal localization and quantification of mRNAs for lysyl oxidase, and cDNA cloning of type IV collagen alpha-5 chain and identification of a mutation in the COL4A5 gene in a patient with Alport syndrome



Acta Universitatis Ouluensis Series A Scientiae Rerum Naturalium 0(267): 1-60



Lysyl oxidase (EC 1.4.3.13), an extracellular copper enzyme, initiates the crosslinking of collagens and elastin by catalyzing oxidative deamination of the E-amino group in certain lysine and hydroxylysine residues. Based on the cDNA sequence, the lysyl oxidase polypeptide had 417 amino acid residues, including a 21 amino acid signal peptide. Northern blot analysis indicated that the human lysyl oxidase cDNA hybridized to at least four mRNA species of 5.5, 4.3, 2.4, and 2.0 kb in size. Variation in mRNA size was due to different lengths of 3' untranslated sequences. The structure of the human lysyl oxidase gene the transcription initiation site was also determined. The transcribed part of the gene is about 11-15 kb and consists of seven exons and six introns. There were one major and four minor transcription initiation sites and the size of the first exon was 923-900 bp, exons 2-6 varied in size from 96 to 157 bp, and exon 7 varied from 220 bp to about 4 kb. The 5' flanking region contained a TATA-like sequence, a CCAAT motif and several other potential binding sites for different transcription factors. Analysis of human-hamster cell hybrids by Southern blotting mapped the human lysyl oxidase gene to chromosome 5, and in situ hybridization sub-localized it to 5q23.3-31.2. PCR-based method was developed to quantify the amount of human lysyl oxidase mRNA in malignantly transformed cell lines. The results indicated that the number of lysyl oxidase mRNA molecules in the transformed cell lines was about 5% of that of the controls. Type IV collagen is the major structural component of basement membranes. The type IV collagen molecule is a heterotrimer composed of three alpha-chains. The primary structure of the human type IV collagen pro alpha-5 chain was determined by sequencing several overlapping cDNA clones. The cDNA clones encoded an open reading frame of 1602 amino acids. The predicted amino acid sequence consisted of a 1373-residue collagenous domain with 22 interruptions and a 229-residue C-terminal noncollagenous domain. Small mutations in exon 47 of the COL4A5 gene in 37 Italian patients with Alport syndrome were identified using the SSCP technique. Sequence analysis revealed a duplication of 36 bp in exon 47.

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