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 284 (3) ◽  
pp. 935-935 ◽  
Keyword(s):  
Tissue Inhibitors Of Metalloproteinases ◽  
Gelatinase A ◽  
Tissue Inhibitors ◽  
Terminal Domain

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.

The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: A kinetic analysis of the inhibition of gelatinase A

Biochemistry ◽  
1993 ◽  
Vol 32 (16) ◽  
pp. 4330-4337 ◽  
Author(s):  
Frances Willenbrock ◽  
Thomas Crabbe ◽  
Patrick M. Slocombe ◽  
Chris W. Sutton ◽  
Andrew J. P. Docherty ◽  
...  
Keyword(s):  
Kinetic Analysis ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Gelatinase A ◽  
Tissue Inhibitors ◽  
Terminal Domain ◽  
Domain Interactions

scholarly journals Activation of gelatinase–tissue-inhibitors-of-metalloproteinase complexes by matrilysin

1998 ◽  
Vol 331 (3) ◽  
pp. 965-972 ◽  
Author(s):  
Dorothea C. von BREDOW ◽  
Anne E. CRESS ◽  
Eric W. HOWARD ◽  
Timothy G. BOWDEN ◽  
Raymond B. NAGLE
Keyword(s):  
Inflammatory Cells ◽  
Prostate Tissue ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Gelatinase A ◽  
Tissue Inhibitors ◽  
Gelatinase B ◽  
Tissue Inhibitors Of Metalloproteinase ◽  
Proteolytic Cascade ◽  
Human Prostate Tissue

Matrilysin, gelatinase A and gelatinase B are matrix metalloproteinases (MMPs) implicated in normal and pathological processes that require remodelling of the extracellular matrix. In human prostate tissue, matrilysin is synthesized in ducts surrounded by inflammatory cells, and focally in prostate carcinoma, but not in normal glands. Gelatinase B expression is restricted to inflammatory cells. Gelatinase A can be found in both benign and malignant prostate tissue. MMP activities are regulated by their transition from latent to activated forms, as well as by the presence of tissue inhibitors of metalloproteinases (TIMPs). We investigated whether matrilysin can activate progelatinases A and B in the presence of their bound inhibitors TIMP2 and TIMP1 respectively. Incubation of progelatinase B–TIMP1 complex with active matrilysin resulted in 78 and 68 kDa active forms, as measured by SDS–PAGE and enzyme activity assays. TIMP-free gelatinase B was also activated by matrilysin. In addition, activation of progelatinase B by matrilysin was demonstrated in the conditioned medium of phorbol ester-treated HT1080 cells, confirming the results obtained in the in vitro experiments. In contrast, matrilysin did not proteolytically cleave gelatinase A–TIMP2 complex, but led to a transient increase in gelatinolytic activity of the proenzyme. Matrilysin did not enhance the autocatalytic conversion of its own proform. The data presented here suggest that matrilysin participates in a proteolytic cascade and can activate gelatinases in the presence of TIMPs.

Different Domain Interactions Are Involved in the Binding of Tissue Inhibitors of Metalloproteinases to Stromelysin-1 and Gelatinase A

Biochemistry ◽  
1994 ◽  
Vol 33 (8) ◽  
pp. 2089-2095 ◽  
Author(s):  
Quang Nguyen ◽  
Frances Willenbrock ◽  
Mark I. Cockett ◽  
Mark O'Shea ◽  
Andrew J. P. Docherty ◽  
...  
Keyword(s):  
Tissue Inhibitors Of Metalloproteinases ◽  
Gelatinase A ◽  
Tissue Inhibitors ◽  
Domain Interactions

scholarly journals Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: associated activation of gelatinase A, gelatinase B and collagenase 3

1998 ◽  
Vol 331 (2) ◽  
pp. 453-458 ◽  
Author(s):  
Susan COWELL ◽  
Vera KNÄUPER ◽  
Margaret L. STEWART ◽  
Marie-Pia D'ORTHO ◽  
Heather STANTON ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Concanavalin A ◽  
Culture Medium ◽  
Interleukin 1 ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Gelatinase A ◽  
Tissue Inhibitors ◽  
Membrane Type ◽  
Activation Cascade

SW1353 chondrosarcoma cells cultured in the presence of interleukin-1, concanavalin A or PMA secreted procollagenase 3 (matrix metalloproteinase-13). The enzyme was detected in the culture medium by Western blotting using a specific polyclonal antibody raised against recombinant human procollagenase 3. Oncostatin M enhanced the interleukin-1-induced production of procollagenase 3, whereas interleukin-4 decreased procollagenase 3 synthesis. The enzyme was latent except when the cells had been treated with concanavalin A, when a processed form of 48 kDa, which corresponds to the active form, was found in the culture medium and collagenolytic activity was detected by degradation of 14C-labelled type I collagen. The concanavalin A-induced activation of procollagenase 3 coincided with the processing of progelatinase A (matrix metalloproteinase-2) by the cells, as measured by gelatin zymography. In addition, progelatinase B (matrix metalloproteinase-9) was activated when gelatinase A and collagenase 3 were in their active forms. Concanavalin A treatment of SW1353 cells increased the amount of membrane-type-1 matrix metalloproteinase protein in the cell membranes, suggesting that this membrane-bound enzyme participates in an activation cascade involving collagenase 3 and the gelatinases. This cascade was effectively inhibited by tissue inhibitors of metalloproteinases-2 and -3. Tissue inhibitor of metalloproteinases-1, which is a much weaker inhibitor of membrane-type 1 matrix metalloproteinase than tissue inhibitors of metalloproteinases-2 and -3 [Will, Atkinson, Butler, Smith and Murphy (1996) J. Biol. Chem. 271, 17119–17123], was a weaker inhibitor of the activation cascade.

The role of matrix metalloproteinase 9 and its inhibitors in scarring processes following surgery for primary open-angle glaucoma

2019 ◽  
pp. 72-80
Author(s):  
Е.В. Маркелова ◽  
О.В. Овчинникова ◽  
А.С. Хохлова ◽  
Л.П. Догадова ◽  
А.В. Костюшко ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Postoperative Period ◽  
Open Angle Glaucoma ◽  
Matrix Metalloproteinase 9 ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Open Angle ◽  
Tissue Inhibitors ◽  
Surgery Outcome ◽  
Metalloproteinase 9

Оперативное вмешательство - один из основных методов лечения глаукомы. Однако развитие избыточного рубцевания созданных путей оттока определяет результат хирургического лечения в отдаленные сроки. Процессы рубцевания на данный момент недостаточно изучены. Цель исследования - оценка роли матриксной металлопротеиназы-9, ее ингибиторов в процессах рубцевания у больных с первичной открытоугольной глаукомой после оперативного лечения. Методика. Для выявления возможных маркеров избыточного рубцевания методом твердофазного иммуноферментного анализа определяли содержание матриксных металлопротеиназ-9, тканевых ингибиторов металлопротеиназ 2 и -3 в слезной жидкости у 37 пациентов с активной стадией первичной остроугольной глаукомы в динамике послеоперационного периода. Средний возраст пациентов составил 52,8 лет. В зависимости от исхода оперативного вмешательства все пациенты были разделены на 2 группы - с благоприятным исходом (без избыточного рубцевания) и с неблагоприятным исходом (с избыточным рубцеванием) на месте сформированных дополнительных путей оттока внутриглазной жидкости в послеоперационном периоде. Группа контроля включала 20 человек в возрасте от 50 до 66 лет без сопутствующей офтальмологической и соматической патологии в стадии обострения. Результаты. В динамике показано изменение концентрации матриксной металлопротеиназы-9 и ее ингибиторов в послеоперационном периоде. Анализ данных свидетельствует об обратной зависимости уровня матриксной металлопротеиназы-9 и тканевых ингибиторов металлопротеиназы 2 и 3 типов с исходом операции - чем выше концентрация металлопротеиназы-9 и ниже концентрация тканевых ингибиторов металлопротеиназ 2, -3 в слезной жидкости, тем выше вероятность неблагоприятного исхода в виде рубцевания сформированных дополнительных путей оттока внутриглазной жидкости в послеоперационном периоде. Заключение. Мониторинг уровня металлопротеиназ и их тканевых ингибиторов после проведения хирургического лечения пациентов с первичной открытоугольной глаукомой позволяет прогнозировать раннее рубцевание, дает возможность разработки новых методов лечения как в раннем, так и в позднем послеоперационном периоде. Surgery is one of the major treatments for glaucoma; however excessive scarring of created outflow patways affects the long-term outcome. At the present time, scarring processes are not sufficiently studied. Aim. To evaluate the role of matrix metalloproteinase 9 and its inhibitors in scarring after surgical treatment of open-angle glaucoma. Methods. Concentrations of matrix metalloproteinase 9 and tissue inhibitors of metalloproteinases 2 and 3 were measured in tear fluid of 37 patients (mean age, 52.8) with active primary open-angle glaucoma in dynamics during the postoperative period to identify possible markers of excessive scarring. Based on the surgery outcome, all patients were divided into two groups, with a favorable outcome (without excessive scarring) and an unfavorable outcome (with excessive scarring) in the created additional outflow pathways for the intraocular fluid in the postoperative period. The control group included 20 subjects aged 50-66 without eye disease or somatic disease at exacerbation stage. Results. Analysis of changes in concentrations of matrix metalloproteinase 9 and its inhibitors in the postoperative period showed their inverse relationship with the surgery outcome. The higher was the metalloproteinase 9 level and the lower the level of tissue inhibitors of metalloproteinases 2 and 3 the higher was the probability of unfavorable outcome evident as excessive scarring of the formed additional pathways for tear fluid outflow in the postoperative period. Conclusion. Postoperative monitoring of metalloproteinases and their tissue inhibitors allows to predict early scarring and to develop new treatments both in early and late postoperative periods.

Role of Metalloproteinases and Tissue Inhibitors of Metalloproteinases During Cardiopulmonary Bypass in Rats

ASAIO Journal ◽  
2012 ◽  
Vol 58 (3) ◽  
pp. 204-211 ◽  
Author(s):  
Ralf Guenzinger ◽  
Harald Lahm ◽  
Michael Wottke ◽  
Ruediger Lange
Keyword(s):  
Cardiopulmonary Bypass ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Tissue Inhibitors
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