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J. Biol. Chem., Vol. 258, Issue 20, 12259-12264, Oct, 1983
HG Welgus and GP Stricklin
In order to gain insight into the biological significance of a collagenase
inhibitor secreted by human skin fibroblasts, we examined various human
connective tissues and body fluids for such a protein. The inhibitors found
in these tissues were compared immunologically to skin fibroblast inhibitor
by Ouchterlony analysis and by the development of a highly specific
enzyme-linked immunosorbent assay (ELISA). Using this ELISA, cell cultures
of human skin fibroblasts, corneal fibroblasts, gingival fibroblasts, and
adult and fetal lung fibroblasts secreted similar amounts of immunoreactive
inhibitor protein. Each culture medium displayed a reaction of immunologic
identity with skin fibroblast inhibitor when examined in Ouchterlony gel
diffusion. In testing for functional inhibitory activity, the same 1:1
stoichiometry of collagenase inhibition was observed in each culture medium
that characterizes the human skin inhibitor. Other mesodermally derived
human cell types, including human fetal osteoblasts, uterine smooth muscle
cells, fibrosarcoma cells, and explants of tendon and articular cartilage
behaved in the same manner as the fibroblast cultures. Because collagenase
inhibitors with biochemical similarities to skin fibroblast inhibitor have
been described in serum and in amniotic fluid, we also examined these
sources of inhibitory proteins. The data indicate that both serum and
amniotic fluid contain collagenase inhibitors which are immunologically and
functionally identical with the skin fibroblast inhibitor. The
concentration of inhibitor in serum, as measured by ELISA assay, is 1.03
+/- 0.27 micrograms/ml. The results suggest that collagenase inhibitors
which are functionally equivalent and immunologically identical with human
skin fibroblast collagenase inhibitor are synthesized by many, if not all,
fetal and adult mesodermal tissues in the human organism. The inhibitor
apparently gains access to certain body fluids such as serum and amniotic
fluid. This inhibitor protein may, therefore, function in the regulation of
collagen degradation in most human connective tissues.
Human skin fibroblast collagenase inhibitor. Comparative studies in human connective tissues, serum, and amniotic fluid
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