نتایج جستجو برای: metalloproteinases

تعداد نتایج: 14679  

2007
Anita Rogowicz Dorota Zozulińska Bogna Wierusz-Wysocka

Cardiovascular complications are the leading cause of increasing and premature mortality in diabetic patients. Matrix metalloproteinases (MMPs) play an important role in the development and progression of vascular lesions. Matrix metalloproteinases are members of endopeptidases and are capable of degrading many extracellular matrix components. Results of recent studies indicated that non-pharma...

Journal: :Reviews of reproduction 1998
E W McIntush M F Smith

Growth and ovulation of follicles, and development, maintenance, and regression of the corpus luteum depend on cyclical remodelling of the extracellular matrix. The extracellular matrix consists of proteinaceous and non-proteinaceous components and provides the tissue-specific, extracellular architecture to which cells attach, and modulates the activities of cells through cell surface receptors...

2016
Brandon J Rose David L Kooyman

Matrix metalloproteinases are a class of enzymes involved in the degradation of extracellular matrix molecules. While these molecules are exceptionally effective mediators of physiological tissue remodeling, as occurs in wound healing and during embryonic development, pathological upregulation has been implicated in many disease processes. As effectors and indicators of pathological states, mat...

2005
Tim E. CAWSTON Valerie A. CURRY

Connective-tissue cells 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 the levels of this inhibitor controlled the extracellular activity of these enzymes. We recently detected a new metalloproteinase inhi...

Journal: :Arteriosclerosis, thrombosis, and vascular biology 2006
Todd S Perlstein Richard T Lee

Smoking causes up to 11% of total global cardiovascular deaths. Smoking has numerous effects that may promote atherosclerosis through vascular inflammation and oxidative stress, but the pathogenesis of smoking-related cardiovascular disease remains incompletely understood. The matrix metalloproteinases, a family of endopeptidases that can degrade extracellular matrix components in both physiolo...

Journal: :Genes & development 1989
C A Brenner R R Adler D A Rappolee R A Pedersen Z Werb

Extracellular matrix (ECM) remodeling accompanies cell migration, cell-cell interactions, embryo expansion, uterine implantation, and tissue invasion during mammalian embryogenesis. We have found that mouse embryos secrete functional ECM-degrading metalloproteinases, including collagenase and stromelysin, that are inhibitable by the tissue inhibitor of metalloproteinases (TIMP) and that are reg...

2018
Chengxian Yang Xinjie Bao Renzhi Wang

Though pituitary adenomas are benign tumors in most cases, a considerable fraction of PAs behave in a malignantlike manner and invade to the adjacent structures in sellar region, especially the cavernous sinuses. Cancer-cell invasion and metastasis remain a great challenge for physicians and surgeons in spite of emerging advances in drug therapy and surgical Treatment. matrix metalloproteinases...

Journal: :Current medicinal chemistry 2009
Nian-Guang Lia Zhi-Hao Shib Yu-Ping Tang Jin-Ao Duan

The matrix metalloproteinases are a family of nearly 30 enzymes that are intimately involved in tissue remodeling. Disease processes associated with the matrix metalloproteinases are generally related to imbalance between the inhibition and activation of matrix metalloproteinases resulting in excessive degradation of the extracellullar matrix. These include osteoarthritis, rheumatoid arthritis,...

Journal: :The Journal of biological chemistry 2007
Janelle L Lauer-Fields Mare Cudic Shuo Wei Frank Mari Gregg B Fields Keith Brew

The sarafotoxins and endothelins are approximately 25-residue peptides that spontaneously fold into a defined tertiary structure with specific pairing of four cysteines into two disulfide bonds. Their structures show an interesting topological similarity to the core of the metalloproteinase interaction sites of the tissue inhibitors of metalloproteinases. Previous work indicates that sarafotoxi...

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