P40. Identification of tissue inhibitor of metalloproteinases-2 (TIMP-2)-progelatinase complex as the third metalloproteinase inhibitor peak in rheumatoid synovial fluid

Bone ◽  
1994 ◽  
Vol 15 (1) ◽  
pp. 126
Author(s):  
TE Cawston ◽  
HF Bigg ◽  
IM Clark ◽  
BL Hazleman
Keyword(s):  
Synovial Fluid ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Tissue Inhibitor ◽  
Metalloproteinase Inhibitor ◽  
The Third ◽  
Rheumatoid Synovial Fluid

scholarly journals Metalloproteinase inhibition and erythroid potentiation are independent activities of tissue inhibitor of metalloproteinases-1

Blood ◽  
1995 ◽  
Vol 86 (12) ◽  
pp. 4506-4515 ◽  
Author(s):  
L Chesler ◽  
DW Golde ◽  
N Bersch ◽  
MD Johnson
Keyword(s):  
Growth Factor ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Factor Activity ◽  
Erythroid Progenitors ◽  
Protease Inhibition ◽  
Tissue Inhibitor ◽  
Vitro Assay ◽  
Erythroid Precursor ◽  
Metalloproteinase Inhibitor

Tissue inhibitor of metalloproteinases-1 (TIMP-1), the major physiological matrix metalloproteinase inhibitor and a potent antimetastatic factor, also stimulates the growth of erythroid progenitors (erythroid-potentiating activity). We analyzed the relationship between the growth factor activity and protease inhibition by preparing purified TIMP-1 “knockout” proteins lacking in vitro antiproteolytic activity. The growth-stimulatory effect of these N- terminal TIMP-1 point mutants, as tested in an in vitro assay using erythroid precursors (erythroid burst-forming units) was equal to that of unmutated TIMP-1. A fully antiproteolytic C-terminal TIMP-1 truncation also stimulated growth in the erythroid burst-forming unit assay. The results indicate that the influence of TIMP-1 on erythroid precursor growth is independent of its ability to inhibit metalloproteinases. TIMP-1 is analogous to proteins that have both proteolytic and growth factor activity, such as plasmin, thrombin, and urokinase. However, TIMP-1 is novel in this regard because it is a metalloproteinase inhibitor. We show that the antiproteolytic and growth factor activities of the TIMP-1 molecule are physically and functionally distinct.

The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitor activity [Erratum to document cited in CA115(9):88133x]

Biochemistry ◽  
1991 ◽  
Vol 30 (42) ◽  
pp. 10362-10362
Author(s):  
Gillian Murphy ◽  
Annick Houbrechts ◽  
Mark I. Cockett ◽  
Richard A. Williamson ◽  
Mark O'Shea ◽  
...  
Keyword(s):  
Tissue Inhibitor Of Metalloproteinases ◽  
Inhibitor Activity ◽  
Tissue Inhibitor ◽  
Metalloproteinase Inhibitor ◽  
Terminal Domain

scholarly journals TISSUE INHIBITOR OF METALLOPROTEINASES AND COLLAGENASE ACTIVITY IN SYNOVIAL FLUID OF HUMAN RHEUMATOID ARTHRITIS

1991 ◽  
Vol 12 (3) ◽  
pp. 169-173 ◽  
Author(s):  
TARO HAYAKAWA ◽  
KYOKO YAMASHITA ◽  
SHUJI KODAMA ◽  
HISASHI IWATA ◽  
KAZUSHI IWATA
Keyword(s):  
Synovial Fluid ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Collagenase Activity ◽  
Tissue Inhibitor

scholarly journals Purification of a metalloproteinase inhibitor from human rheumatoid synovial fluid

1985 ◽  
Vol 231 (3) ◽  
pp. 505-510 ◽  
Author(s):  
E Mercer ◽  
T E Cawston ◽  
M de Silva ◽  
B L Hazleman
Keyword(s):  
Synovial Fluid ◽  
Culture Medium ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Serine Proteinase ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Metalloproteinase Inhibitor ◽  
Bacterial Collagenase ◽  
Rheumatoid Synovial Fluid

A metalloproteinase inhibitor present in human rheumatoid synovial fluid was purified by a combination of heparin-Sepharose chromatography, concanavalin A-Sepharose chromatography, ion-exchange chromatography and gel filtration. The Mr of the purified inhibitor was 28000 by SDS/polyacrylamide-gel electrophoresis and 30000 by gel filtration. The inhibitor blocked the activity of the metalloproteinases collagenase, gelatinase and proteoglycanase, but not thermolysin or bacterial collagenase. The serine proteinase trypsin was not inhibited. The inhibitory activity was lost after treatment with trypsin (0.5 micrograms/ml) at 37 degrees C for 30 min, 4-aminophenylmercuric acetate (1 mM) at 37 degrees C for 3 h, after incubation for 30 min at 90 degrees C and by reduction and alkylation. These properties suggest that the inhibitor closely resembles the tissue inhibitor of metalloproteinases (‘TIMP’) recently purified from connective-tissue culture medium.

scholarly journals Large inhibitor of metalloproteinases (LIMP) contains tissue inhibitor of metalloproteinases (TIMP)-2 bound to 72,000-Mr progelatinase

1992 ◽  
Vol 285 (1) ◽  
pp. 143-147 ◽  
Author(s):  
V A Curry ◽  
I M Clark ◽  
H Bigg ◽  
T E Cawston
Keyword(s):  
Extracellular Matrix ◽  
Connective Tissue ◽  
Inhibitory Activity ◽  
Culture Medium ◽  
Lung Fibroblasts ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Tissue Inhibitor ◽  
Metalloproteinase Inhibitor ◽  
Cells In Culture ◽  
Foetal Lung

Connective-tissue cells in culture produce a family of metalloproteinases which, once activated, can degrade all the components of the extracellular matrix. These potent enzymes are all inhibited by the tissue inhibitor of metalloproteinases (TIMP), and it was thought that this inhibitor was solely responsible for the inhibition of these enzymes within connective tissue. However, other inhibitors have recently been described, including large inhibitor of metalloproteinases (LIMP) present in the culture medium of human foetal lung fibroblasts. Here we show that a large proportion of the inhibitory activity of LIMP consists of 72,000-M(r)-progelatinase bound to TIMP-2, a recently discovered low-M(r) metalloproteinase inhibitor closely related to TIMP. The physiological implications of the secretion of a complex of 72,000-M(r) progelatinase and TIMP-2 are discussed, and the separation of the complex in 6 M-urea is described.

scholarly journals The complex between a tissue inhibitor of metalloproteinases (TIMP-2) and 72-kDa progelatinase is a metalloproteinase inhibitor

1991 ◽  
Vol 198 (3) ◽  
pp. 775-781 ◽  
Author(s):  
Hansjorg KOLKENBROCK ◽  
Dagmar ORGEL ◽  
Adelheid HECKER-KIA ◽  
Wolfgang NOACK ◽  
Norbert ULBRICH
Keyword(s):  
Tissue Inhibitor Of Metalloproteinases ◽  
Tissue Inhibitor ◽  
Metalloproteinase Inhibitor

scholarly journals Rapid purification of tissue inhibitor of metalloproteinases from human plasma and identification as a γ-serum protein

1986 ◽  
Vol 238 (3) ◽  
pp. 677-682 ◽  
Author(s):  
T E Cawston ◽  
D N Noble ◽  
G Murphy ◽  
A J Smith ◽  
C Woodley ◽  
...  
Keyword(s):  
Synovial Fluid ◽  
Amniotic Fluid ◽  
Culture Medium ◽  
Gel Filtration ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Human Amniotic Fluid ◽  
Tissue Inhibitor ◽  
Serum Component ◽  
Rapid Purification ◽  
Human Synovial Fluid

A rapid method is described for the purification of human tissue inhibitor of metalloproteinases (TIMP) from plasma which involves immuno-affinity chromatography and gel filtration. The purified plasma inhibitor is immunologically identical with the TIMP previously purified from human amniotic fluid, human synovial fluid and human fibroblast culture medium. It is proposed that this inhibitor is identical with the plasma inhibitor previously named ‘B1 anticollagenase’, although the plasma inhibitor was shown to migrate as a gamma-serum component.

Sign in / Sign up

Export Citation Format

Share Document