Randomized trial identifies the role of human fibroblast collagenase inhibitor in connective tissue modulation, suggesting a mechanism for protease regulation.
Key Points
The aim is to characterize the primary structure and clone the cDNA of the human fibroblast collagenase inhibitor.
Automated Edman degradation was used to determine the amino acid sequence of the protein.
Synthetic oligonucleotide probes were designed to screen a lambda gt10 cDNA library from human fibroblast.
Two overlapping cDNA clones were characterized for coding and noncoding sequences.
The inhibitor consists of 184 amino acid residues with two N-linked oligosaccharide linkage sites and six disulfide bonds.
One cDNA clone contains the complete 5' end and predicts a 23-amino acid leader peptide.
The 3' cDNA sequence shows similarity to a reported mouse fibroblast cDNA but lacks homology with previously sequenced protease inhibitors.