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J. Biol. Chem., Vol. 265, Issue 36, 22342-22347, 12, 1990
CO Quinn, DK Scott, CE Brinckerhoff, LM Matrisian, JJ Jeffrey and NC Partridge
We have isolated clones for rat collagenase from a rat osteoblastic cell
cDNA library. These clones have been sequenced and the amino acids deduced.
The calculated molecular weight is 51,352 for the proenzyme and 42,229 for
the active enzyme. The deduced amino acid sequence was compared to those
previously reported for: 1) human collagenase, 2) rat transin 1
(stromelysin), 3) human stromelysin, and 4) rabbit collagenase. The number
of amino acids conserved was 47, 47, 50, and 47%, respectively. We also
compared the collagenase mRNA and protein in different rat cells
(osteoblast, uterine smooth muscle, synovial fibroblast) and determined
that in rat uterine cells the message is slightly larger, although
collagenase protein in all three cell types was identical in size.
Parathyroid hormone dramatically induces the 2.9- kilobase collagenase mRNA
in the rat osteoblastic cells, UMR 106-01. Nuclear run-on studies in UMR
106-01 cells demonstrated a 4-8-fold induction in the rate of synthesis of
collagenase mRNA at 2 and 4 after parathyroid hormone treatment, with
steady state levels of mRNA increased 100-fold at 4 h. Thus, parathyroid
hormone regulation of the collagenase gene in UMR 106-01 cells is in part
transcriptional.
Rat collagenase. Cloning, amino acid sequence comparison, and parathyroid hormone regulation in osteoblastic cells
Pediatric Research Institute, Cardinal Glennon Children's Hospital, St. Louis, Missouri.
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