Structural features of the reprolysin atrolysin C and tissue inhibitors of metalloproteinases (TIMPs) interaction

2006 ◽  
Vol 347 (3) ◽  
pp. 641-648 ◽  
Author(s):  
Antônio F.M. Pinto ◽  
Renata M.S. Terra ◽  
Jorge A. Guimarães ◽  
Masahide Kashiwagi ◽  
Hideaki Nagase ◽  
...  
Keyword(s):  
Structural Features ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Tissue Inhibitors

Role of TIMPs (tissue inhibitors of metalloproteinases) in pericellular proteolysis: the specificity is in the detail

2003 ◽  
Vol 70 ◽  
pp. 65-80 ◽  
Author(s):  
Gillian Murphy ◽  
Vera Knäuper ◽  
Meng-Huee Lee ◽  
Augustin Amour ◽  
Joanna R. Worley ◽  
...  
Keyword(s):  
Cell Surface ◽  
Specific Binding ◽  
Heparan Sulphate ◽  
Structural Features ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Tissue Inhibitors ◽  
The Matrix ◽  
Membrane Type ◽  
Factor Α ◽  
Pericellular Proteolysis

Pericellular proteolysis represents one of the key modes by which the cell can modulate its environment, involving not only turnover of the extracellular matrix but also the regulation of cell membrane proteins, such as growth factors and their receptors. The metzincins are active players in such proteolytic events, and their mode of regulation is therefore of particular interest and importance. The TIMPs (tissue inhibitors of metalloproteinases) are established endogenous inhibitors of the matrix metalloproteinases (MMPs), and some have intriguing abilities to associate with the pericellular environment. It has been shown that TIMP-2 can bind to cell surface MT1-MMP (membrane-type 1 MMP) to act as a 'receptor' for proMMP-2 (progelatinase A), such that the latter can be activated efficiently in a localized fashion. We have examined the key structural features of TIMP-2 that determine this unique function, showing that Tyr\36 and Glu192-Asp193 are vital for specific interactions with MT1-MMP and proMMP-2 respectively, and hence activation of proMMP-2. TIMP-3 is sequestered at the cell surface by association with the glycosaminoglycan chains of proteoglycans, especially heparan sulphate, and we have shown that it may play a role in the regulation of some ADAMs (a disintegrin and metalloproteinases), including tumour necrosis factor α-converting enzyme (TACE; ADAM17). We have established that key residues in TIMP-3 determine its interaction with TACE. Further studies of the features of TIMP-3 that determine specific binding to both ADAM and glycosaminoglycan are required in order to understand these unique properties.

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

Expression of matrix metalloproteinases (MMPs-2, -7, -9, and -26) and tissue inhibitors of metalloproteinases (TIMPs-1 and -2) in pleomorphic adenomas and adenoid cystic carcinomas

2018 ◽  
Vol 275 (12) ◽  
pp. 3075-3082 ◽  
Author(s):  
Valéria Souza Freitas ◽  
Jean Nunes dos Santos ◽  
Pedro Paulo de Andrade Santos ◽  
Cassiano Francisco Weege Nonaka ◽  
Leão Pereira Pinto ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Tissue Inhibitors ◽  
Adenoid Cystic ◽  
Pleomorphic Adenomas

scholarly journals Expression of Matrix Metalloproteinases, Tissue Inhibitors of Metalloproteinases, and Interleukins in Vertebral Cartilage Endplate

2018 ◽  
Vol 10 (4) ◽  
pp. 306-311 ◽  
Author(s):  
Jian-feng Zhang ◽  
Gang-liang Wang ◽  
Zhi-jie Zhou ◽  
Xiang-qian Fang ◽  
Shuai Chen ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Tissue Inhibitors ◽  
Cartilage Endplate

Gene Therapy for Vein Graft Failure Using Tissue Inhibitors of Metalloproteinases

1999 ◽  
Vol 97 (s41) ◽  
pp. 15P-15P
Author(s):  
SJ George ◽  
AH Baker ◽  
GD Angelini ◽  
AC Newby
Keyword(s):  
Gene Therapy ◽  
Vein Graft ◽  
Graft Failure ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Tissue Inhibitors ◽  
Vein Graft Failure
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