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Laminin is a basement membrane glycoprotein composed of three nonidentical chains, A, B1, and B2. Variant chains such as merosin and S-laminin have been found in different tissues. We have isolated a cDNA encoding a novel laminin A variant that hybridizes to a 6.45-kb mRNA. Using amplification of genomic DNA and flow-sorted chromosomes we have assigned the(More)
We have studied a patient with Ehlers-Danlos syndrome type IV. Protein mapping studies of her type III collagen had indicated that cyanogen bromide fragment 9 contained the site of the mutation. Here we describe the mapping of this region for a single base mutation using a chemical modification and cleavage technique. Sequence analysis of cDNA showed a G to(More)
The human carbonic anhydrase isozymes represent a family of homologous proteins which are important in respiratory function, fluid secretion, and maintenance of cellular acid-base homeostasis. Using somatic cell genetic techniques we have mapped two of the CA genes (CA1 and CA3) to human chromosome 8. In situ hybridization data demonstrates that both CA1(More)
cDNA encoding the C-terminal domain (nt2283 to 3714) of type III collagen was amplified by PCR in five overlapping products and examined for mutations in 13 patients with Ehlers-Danlos syndrome type IV (EDS IV) with uncharacterised lesions and in five control patients with known single base mutations. Six different point mutations were detected by(More)
A cDNA clone complementary to the mRNA encoding the human muscle specific carbonic anhydrase CAIII has been used as probe in the analysis of DNA from panels of rodent/human somatic cell hybrids. The presence of the CA III gene in all hybrids correlates with the presence of chromosome 8. This is the first assignment of the CAIII gene in any species and,(More)
Ehlers-Danlos syndrome type IV is usually caused by mutations in COL3A1, the gene coding for type III collagen. In a woman with a milder form of this disease, analysis of type III collagen synthesised by her cultured skin fibroblasts showed an apparently shorter form of the protein. Amplification of overlapping cDNAs, encoding the triple helical region of(More)
We report the nucleotide (nt) sequence of a full length cDNA clone, pCA15, which encodes the human muscle-specific carbonic anhydrase, CAIII. pCA15 identifies a 1.7-kb mRNA, which is present at high levels in skeletal muscle, at much lower levels in cardiac and smooth muscle and which appears to be developmentally regulated. The CAIII mRNA is distinguished(More)
We report the isolation and analysis of genomic clones comprising the entire gene coding for the human muscle carbonic anhydrase, CAIII. The gene spans 10.3 kb and has a seven-exon/six-intron structure. A noncanonical TATA box, a CCAAT motif, and two CCGCCC elements are present in the sequences upstream of exon 1. Although the expression of CAIII shows(More)
Analysis of human glyceraldehyde-3-phosphate dehydrogenase mRNA revealed that levels in adult skeletal muscle are 12-fold greater per microgram of polyadenylated RNA than in fetal skeletal muscle, whereas in cardiac muscle RNA levels were about equal in fetal and adult tissue. The mRNA levels correlate well with glyceraldehyde 3-phosphate dehydrogenase(More)
The molecular cloning of cDNA for the human muscle specific carbonic anhydrase CAIII is described. The recombinant was isolated from a human muscle cDNA library prepared in the expression vector lambda gt11, and was characterized by hybridization selection and immunoprecipitation. A comparison of insert cDNA and mRNA sizes suggests that the cDNA is full(More)