scholarly journals Cathepsin B: an alternative protease for the generation of an aggrecan ‘metalloproteinase’ cleavage neoepitope

1998 ◽  
Vol 335 (3) ◽  
pp. 491-494 ◽  
Author(s):  
John S. MORT ◽  
Marie-Claude MAGNY ◽  
Eunice R. LEE
Keyword(s):  
Matrix Metalloproteinases ◽  
Cysteine Protease ◽  
Cathepsin B ◽  
Cartilage Proteoglycan ◽  
Metalloproteinase Activity

Previously, only matrix metalloproteinases were believed capable of cleaving the cartilage proteoglycan, aggrecan, between Asn341 and Phe342, to yield a small G1 fragment terminating in the residues VDIPEN. We show that the combined endo- and exopeptidase activities of the cysteine protease, cathepsin B, also generate this epitope, suggesting that it should no longer be considered as an exclusive marker of metalloproteinase activity.

Matrix metalloproteinases in stroke

2017 ◽  
pp. 110-117
Author(s):  
А.А. Пальцын
Keyword(s):  
Matrix Metalloproteinases ◽  
Enzyme System ◽  
Enzyme Complex ◽  
Pathogenic Factors ◽  
Pathogenic Action ◽  
Activity Of Enzymes ◽  
Living Tissues ◽  
Current Reconstruction ◽  
Metalloproteinase Activity

Матриксные металлопротеиназы - ферментный комплекс, необходимый для сохранения гомеостаза. Он участник нормальной, постоянно текущей реконструкции всех живых тканей. Действие патогенных факторов нарушает слаженную работу этого комплекса. Часто нарушение выражается излишней активностью ферментов, усиливающей патогенное действие. Однако и заживление, форсированное новообразование тканевых элементов, может происходить только при повышенной, в сравнении с нормой, активности металлопротеиназ. Такая ситуация требует от медицины умения разумно вмешиваться в работу ферментной системы. В статье представлены некоторые результаты этих вмешательств. Matrix metalloproteinases - enzyme complex necessary for maintenance of the homeostasis. He is a participant of normal, constantly current reconstruction of all living tissues. Action of pathogenic factors breaks harmonious work of this complex. Often violation is expressed by the excessive activity of enzymes amplifying pathogenic action. However and healing, which is accelerated new growth of tissue elements, can happen only at raised, compared with norm, metalloproteinase activity. Such situation demands from medicine of ability participate reasonably in work of enzyme system. The article presents some of the results of these actions.

Matrix metalloproteinases, inflammation and atherosclerosis: therapeutic perspectives

2004 ◽  
Vol 42 (2) ◽  
Author(s):  
Jean-Louis Beaudeux ◽  
Philippe Giral ◽  
Eric Bruckert ◽  
Marie-José Foglietti ◽  
M. John Chapman
Keyword(s):  
Matrix Metalloproteinases ◽  
Atherosclerotic Lesion ◽  
Left Ventricular ◽  
Vascular Pathology ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Tissue Remodelling ◽  
Plaque Instability ◽  
Plaque Disruption ◽  
Extracellular Matrix Remodelling ◽  
Metalloproteinase Activity

AbstractMatrix metalloproteinases (MMPs), also called matrixins, are proteinases that participate in extracellular matrix remodelling and degradation. Under normal physiological conditions, the activities of MMPs are precisely regulated at the level of transcription, of activation of the pro-MMP precursor zymogens and of inhibition by endogenous inhibitors (tissue inhibitors of metalloproteinases; TIMPs). Alteration in the regulation of MMP activity is implicated in diseases such as cancer, fibrosis, arthritis and atherosclerosis. The pathological effects of MMPs and TIMPs in cardiovascular diseases involve vascular remodelling, atherosclerotic plaque instability and left ventricular remodelling after myocardial infarction. Since excessive tissue remodelling and increased matrix metalloproteinase activity have been demonstrated during atherosclerotic lesion progression (including plaque disruption), MMPs represent a potential target for therapeutic intervention aimed at modification of vascular pathology by restoring the physiological balance between MMPs and TIMPs. This review describes the members of the MMP and TIMP families and discusses the structure, function and regulation of MMP activity; finally, pharmacological approaches to MMP inhibition are highlighted.

Characterisation of cathepsin B-like cysteine protease of Lepeophtheirus salmonis

Aquaculture ◽  
2010 ◽  
Vol 310 (1-2) ◽  
pp. 38-42 ◽  
Author(s):  
Eleanor Cunningham ◽  
Elaine McCarthy ◽  
Lorraine Copley ◽  
Dave Jackson ◽  
David Johnson ◽  
...  
Keyword(s):  
Cysteine Protease ◽  
Cathepsin B ◽  
Lepeophtheirus Salmonis

Inhibition of cathepsin B reduces β-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: evidence for cathepsin B as a candidate β-secretase of Alzheimer's disease

2005 ◽  
Vol 386 (9) ◽  
Author(s):  
Vivian Hook ◽  
Thomas Toneff ◽  
Matthew Bogyo ◽  
Doron Greenbaum ◽  
Katalin F. Medzihradszky ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cysteine Protease ◽  
Cathepsin B ◽  
Protease Activity ◽  
Chromaffin Cells ◽  
Secretory Pathway ◽  
Secretory Vesicles ◽  
Cysteine Protease Activity ◽  
Regulated Secretory Pathway

AbstractThe regulated secretory pathway of neurons is the major source of extracellular Aβ that accumulates in Alzheimer's disease (AD). Extracellular Aβ secreted from that pathway is generated by β-secretase processing of amyloid precursor protein (APP). Previously, cysteine protease activity was demonstrated as the major β-secretase activity in regulated secretory vesicles of neuronal chromaffin cells. In this study, the representative cysteine protease activity in these secretory vesicles was purified and identified as cathepsin B by peptide sequencing. Immunoelectron microscopy demonstrated colocalization of cathepsin B with Aβ in these vesicles. The selective cathepsin B inhibitor, CA074, blocked the conversion of endogenous APP to Aβ in isolated regulated secretory vesicles. In chromaffin cells, CA074Me (a cell permeable form of CA074) reduced by about 50% the extracellular Aβ released by the regulated secretory pathway, but CA074Me had no effect on Aβ released by the constitutive pathway. Furthermore, CA074Me inhibited processing of APP into the COOH-terminal β-secretase-like cleavage product. These results provide evidence for cathepsin B as a candidate β-secretase in regulated secretory vesicles of neuronal chromaffin cells. These findings implicate cathepsin B as β-secretase in the regulated secretory pathway of brain neurons, suggesting that inhibitors of cathepsin B may be considered as therapeutic agents to reduce Aβ in AD.

scholarly journals Eimeripain, a Cathepsin B-Like Cysteine Protease, Expressed throughout Sporulation of the Apicomplexan Parasite Eimeria tenella

PLoS ONE ◽  
2012 ◽  
Vol 7 (3) ◽  
pp. e31914 ◽  
Author(s):  
Anaïs Rieux ◽  
Simon Gras ◽  
Fabien Lecaille ◽  
Alisson Niepceron ◽  
Marilyn Katrib ◽  
...  
Keyword(s):  
Cysteine Protease ◽  
Cathepsin B ◽  
Apicomplexan Parasite ◽  
Eimeria Tenella
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