PARTICULATE MATTER INDUCTION OF PULMONARY GELATINASE A, GELATINASE B, AND TISSUE INHIBITOR OF METALLOPROTEINASE EXPRESSION

2000 ◽  
Vol 12 (sup2) ◽  
pp. 105-119
Author(s):  
Wei-Yi Su, Duke University Medical Center,
Keyword(s):  
Particulate Matter ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Gelatinase A ◽  
Tissue Inhibitor ◽  
Gelatinase B

scholarly journals Identification of complexes of gelatinase A and tissue inhibitor of metalloproteinase-2 in human follicular fluid

2003 ◽  
Vol 2 (3) ◽  
pp. 115-119 ◽  
Author(s):  
Ken-Ichi Shimokawa ◽  
Masatoki Katayama ◽  
Yoshifumi Matsuda ◽  
Hidenobu Takahashi ◽  
Izumi Hara ◽  
...  
Keyword(s):  
Follicular Fluid ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Gelatinase A ◽  
Tissue Inhibitor ◽  
Human Follicular Fluid

scholarly journals The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases

1992 ◽  
Vol 283 (3) ◽  
pp. 637-641 ◽  
Author(s):  
G Murphy ◽  
F Willenbrock ◽  
R V Ward ◽  
M I Cockett ◽  
D Eaton ◽  
...  
Keyword(s):  
Kinetic Studies ◽  
Full Length ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Gelatinase A ◽  
Truncated Form ◽  
Tissue Inhibitor ◽  
Tissue Inhibitors ◽  
Terminal Domain

Recombinant 72 kDa gelatinase A and a truncated form lacking the C-terminal domain were shown to be activated by organomercurials and to possess similar activities towards a number of substrates. The truncated proenzyme differed from the full-length gelatinase in that it could not be activated by a membrane activator and did not bind tissue inhibitor of metalloproteinase (TIMP)-2. Kinetic studies also showed that the inhibition of the activated truncated enzyme, by both TIMP-1 and TIMP-2, was considerably decreased compared with the full-length enzyme. We conclude that the C-terminal domain plays an important role in the regulation of gelatinase A by a potential physiological activator and inhibitors.

Triiodothyronine induces collagenase-3 and gelatinase B expression in murine osteoblasts

1999 ◽  
Vol 277 (3) ◽  
pp. E496-E504 ◽  
Author(s):  
Renata C. Pereira ◽  
Vanda Jorgetti ◽  
Ernesto Canalis
Keyword(s):  
Bone Resorption ◽  
Bone Matrix ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Osteoblastic Cells ◽  
Matrix Remodeling ◽  
Mrna Levels ◽  
Gelatinase A ◽  
Matrix Metalloprotease ◽  
Gelatinase Activity ◽  
Gelatinase B

Triiodothyronine (T3) increases bone resorption, but its effects on matrix metalloprotease (MMP) expression in bone are unknown. We tested the effects of T3 on collagenase-3 and gelatinase A and B expression in MC3T3 osteoblastic cells. T3 at 1 nM to 1 μM for 24–72 h increased collagenase-3 and gelatinase B mRNA levels, but it did not increase gelatinase A transcripts. In addition, T3 increased immunoreactive collagenase and gelatinase activity. Cycloheximide prevented the stimulatory effect of T3 on collagenase-3 but not on gelatinase B transcripts. Indomethacin did not prevent the effect of T3 on either MMP. T3 did not alter the decay of collagenase-3 or gelatinase B mRNA in transcriptionally arrested MC3T3 cells, and it increased the rate of collagenase-3 and gelatinase B gene transcription. Although T3enhanced the expression of the tissue inhibitor of metalloproteinase-1 in MC3T3 cells, it increased collagen degradation in cultured intact rat calvariae. In conclusion, T3 increases collagenase-3 and gelatinase B synthesis in osteoblasts by transcriptional mechanisms. This effect may contribute to the actions of T3 on bone matrix remodeling.

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