Molecular complementation of mutant phenotypes by transgenic technology is a potentially
important tool for gene identification. A technology was developed that allows the transfer of …

The identification and functional analysis of DNA‐protein interactions in the intronic and 5′
flanking regions of the type I collagen genes has begun to define a series of cis‐elements …

Degradation of type I collagen, the most abundant collagen, is initiated by collagenase
cleavage at a highly conserved site between Gly775 and Ile776 of the alpha 1 (I) chain …

The hepatic stellate cell (HSC) is the primary cell responsible for the dramatic increase in the
synthesis of type I collagen in the cirrhotic liver. Quiescent HSCs contain a low level of …

A heterozygous single base change in exon 49 of COL1A1, which converted the codon for
proα1 (I) carboxyl-terminal propeptide residue 94 from tryptophan (TGG) to cysteine (TGT) …

Collagenase (matrix metalloproteinase 1) cleaves type I, II, and III collagen helices at a
specific site between Gly-Ile or Gly-Leu bonds (residues 775 and 776, P1-P1'). To …

A third member of the thrombospondin gene family (Thbs3) has been partially characterized
in the mouse. In both the mouse and humans, the Thbs3/THBS3 gene is located …

The collagen α1 (I) promoter, which is efficiently transcribed in NIH 3T3 fibroblasts, contains
four binding sites for trans-acting factors, as demonstrated by DNase I protection assays (DA …

Increasing numbers of transgenic mouse lines have resulted in several dozens of mutants
created by insertional mutagenesis. The advantages of different vector systems and the …

Collagen in the skin undergoes dramatic reorganization during wound repair. Matrix
metalloproteinases degrade and remodel the collagen in a tightly controlled process. The …