Results 211 to 220 of about 20,584 (256)

Cathepsin L, But Not Cathepsin B, Is a Potential Kininogenase

Biological Chemistry, 2001
Although papain-like enzymes are strongly inhibited by their natural tight-binding inhibitors of the cystatin superfamily, cathepsins B and L may still retain some residual proteolytic activity toward Z-Phe-Arg-AMC in the presence of an excess of kininogen. This activity is abolished by adding E-64 or chicken cystatin.
C, Desmazes, F, Gauthier, G, Lalmanach
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Cathepsin K and the Design of Inhibitors of Cathepsin K

Current Pharmaceutical Design, 2000
Cathepsin K, a cysteine protease of the papain family, was identified by sequencing complementary DNA libraries derived from osteoclasts. Cathepsin K can cleave bone proteins such as Type I collagen, osteopontin, and osteonectin. The localization and maturation of cathepsin K in activated osteoclasts have been characterized.
D S, Yamashita, R A, Dodds
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Improved purification of cathepsin B1 and cathepsin B2

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1975
An 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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Cathepsin B in osteoblasts

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., BECCARI, Tommaso, COSTANZI, Egidia, Di Maggio D.   +3 more
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Anti-Cathepsin L Monoclonal Antibodies That Distinguish Cathepsin L from Cathepsin V

Biological Chemistry, 2001
Cathepsin 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, T, Bevec, D, Barlic-Maganja, F, Gubensek, V, Turk   +4 more
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Cathepsin L in glioma progression: Comparison with cathepsin B

Cancer Detection and Prevention, 2005
Lysosomal 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, Rajko, Kavalar, Miha, Trinkaus, Tamara T, Lah   +3 more
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CATHEPSIN B, CATHEPSIN C AND ARYLAMIDASE IN RABBIT CORNEA

Acta Ophthalmologica, 1982
The 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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New Functional Aspects of Cathepsin D and Cathepsin E

Molecules and Cells, 2000
Cathepsin D (CD) and cathepsin E are representative lysosomal and nonlysosomal aspartic proteinases, respectively, and play an important role in the degradation of proteins, the generation of bioactive proteins, antigen processing, etc. Recenty, several lines of evidence have suggested the involvement of these two enzymes in the execution of neuronal ...
T, Tsukuba, K, Okamoto, Y, Yasuda, W, Morikawa, H, Nakanishi, K, Yamamoto   +5 more
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Human Cathepsins F and W: A New Subgroup of Cathepsins

Biochemical and Biophysical Research Communications, 1999
Human cathepsin F is a recently described papain-like cysteine protease of unknown function. To investigate the evolutionary relatedness to other human cathepsins, we determined the genomic organization and the chromosomal localization of cathepsin F and isolated its putative promoter region.
T, Wex, B, Levy, H, Wex, D, Brömme
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Cathepsin E and cathepsin D

1999
Aspartic proteinases are produced by a number of cells and tissues. These enzymes share a high degree of similarity which involves primary structures, and most of them are active predominantly in the acidic pH range. Eukaryotic aspartic proteinases (i.e.
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