Results 321 to 330 of about 84,247 (372)
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The International Journal of Biochemistry & Cell Biology, 1997
Cathepsin B is a lysosomal cysteine protease of the papain family. It functions in intracellular protein catabolism and in certain situations may also be involved in other physiological processes, such as processing of antigens in the immune response, hormone activation and bone turnover.
J S, Mort, D J, Buttle
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Cathepsin B is a lysosomal cysteine protease of the papain family. It functions in intracellular protein catabolism and in certain situations may also be involved in other physiological processes, such as processing of antigens in the immune response, hormone activation and bone turnover.
J S, Mort, D J, Buttle
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Cysteine cathepsins as therapeutic targets in inflammatory diseases
Expert opinion on therapeutic targets, 2020Introduction: Cysteine cathepsins are involved in the development and progression of numerous inflammation-associated diseases such as cancer, arthritis, bone and immune disorders.
Matej Vizovišek +5 more
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Anti-Cathepsin L Monoclonal Antibodies That Distinguish Cathepsin L from Cathepsin V
Biological Chemistry, 2001Cathepsin L is a lysosomal cysteine protease involved in intracellular protein degradation. Recently, several new cysteine proteases have been identified. Human cathepsin V, a thymus- and testis-specific human cysteine protease, shares 78% sequence identity with human cathepsin L.
N, Kopitar-Jerala +4 more
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Apoptosis, 2006
Apoptosis can be mediated by different mechanisms. There is growing evidence that different proteolytic enzymes are involved in the regulation of apoptosis. Cathepsins are proteases which, under physiologic conditions, are localized intralysosomally.
C E, Chwieralski, T, Welte, F, Bühling
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Apoptosis can be mediated by different mechanisms. There is growing evidence that different proteolytic enzymes are involved in the regulation of apoptosis. Cathepsins are proteases which, under physiologic conditions, are localized intralysosomally.
C E, Chwieralski, T, Welte, F, Bühling
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Host Cell Proteases: Cathepsins
Activation of Viruses by Host Proteases, 2018Cathepsins are proteolytic enzymes with a broad spectrum of substrates. They are known to reside within endo-lysosomes where they acquire optimal conditions for proteolytic activity and substrate cleavage.
K. Brix
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Improved purification of cathepsin B1 and cathepsin B2
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1975An improved purification of the cathepsins B1 and B2 from bovine spleen is described. In addition to the formerly used procedure, chromatography with DEAE-Sephadex or -cellulose and mercurated agarose is used. Both enzymes are obtained in an electrophoretically pure form but consist of two or more isoenzymes.
K, Otto, H, Riesenkönig
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Biochimica et Biophysica Acta (BBA) - General Subjects, 2003
Active cathepsin B has been found in cell extract and medium of human osteoblast-like cells and MG-63 cells. The released form is stable at neutral and alkaline pH and, in both cell types, intracellular and extracellular cathepsin B activities are increased by interleukin-1 beta (IL-1beta) and parathyroid hormone (PTH).
Aisa M. C. +3 more
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Active cathepsin B has been found in cell extract and medium of human osteoblast-like cells and MG-63 cells. The released form is stable at neutral and alkaline pH and, in both cell types, intracellular and extracellular cathepsin B activities are increased by interleukin-1 beta (IL-1beta) and parathyroid hormone (PTH).
Aisa M. C. +3 more
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Cathepsin L in glioma progression: Comparison with cathepsin B
Cancer Detection and Prevention, 2005Lysosomal cysteine cathepsins have been implicated in tumor progression. This study is aimed to reveal differential expression and compare the prognostic significance of cathepsins B and L in glioma patients.The histological slides of 82 patients with primary astrocytic tumors were reviewed.
Tadej, Strojnik +3 more
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CATHEPSIN B, CATHEPSIN C AND ARYLAMIDASE IN RABBIT CORNEA
Acta Ophthalmologica, 1982The 3 peptide hydrolases cathepsin B, cathepsin C and arylamidase have been assayed in rabbit cornea with the use of fluorigenic derivatives of β‐naphthylamine. The optimal reaction conditions and kinetic properties are described. The assay procedures which are simple and very sensitive can be used for studying the release of these enzymes from corneal
K, Schive, G, Volden
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