Rabbit calvarial osteoblasts in culture constitutively synthesize progelatinase-A, and TIMP-1 and TIMP-2.
Defining the TIMPs (tissue inhibitors of metalloproteinases) produced by non-human bone cells is important because animal models and cells are used extensively for research on bone resorption, and because TIMP-2 can bind to and prevent activation of progelatinase-A. By zymography we show that rabbit calvarial osteoblasts in culture constitutively synthesize TIMP-2 in addition to TIMP-1 and progelatinase-A. Previously we found that human osteoblasts produced only low levels of TIMP-2 under any conditions. We also show that stimulated rabbit osteoblasts can degrade a type I collagen film even though both TIMPs are being synthesized.
Meikle
M C
MC
Cell and Molecular Biology Department, Strangeways Research Laboratory, Cambridge, UK.
Bord
S
S
Hembry
R M
RM
Reynolds
J J
JJ
D000818:Animals; D002478:Cells, Cultured; D003094:Collagen / Q000378:metabolism; D004792:Enzyme Precursors / Q000096:biosynthesis*; D018093:Gelatinases / Q000096:biosynthesis*; D006023:Glycoproteins / Q000096:biosynthesis*; D008666:Metalloendopeptidases / Q000096:biosynthesis*; D010006:Osteoblasts / Q000378:metabolism*; D014176:Protein Biosynthesis; D011817:Rabbits; D019716:Tissue Inhibitor of Metalloproteinase-2; D019714:Tissue Inhibitor of Metalloproteinases
D004792:Enzyme Precursors; D006023:Glycoproteins; D019714:Tissue Inhibitor of Metalloproteinases; D019716:Tissue Inhibitor of Metalloproteinase-2; D003094:Collagen; D018093:Gelatinases; D008666:Metalloendopeptidases; C069860:progelatinase