Results 261 to 270 of about 66,677 (282)

Specificity of Rat Liver Cathepsin D

Journal of Biochemistry, 1987
The specificity of highly purified rat liver cathepsin D was investigated by analyzing the digests of denatured proteins. At the P1 site, cathepsin D prefers hydrophobic residues except Ile and Val, that are branched at the beta-carbon. Strong and weak hydrophobicities are required at P1' and P2 sites, respectively.
T, Imoto, K, Okazaki, H, Koga, H, Yamada
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Cathepsin D activity in nasal polyps

Clinical Biochemistry, 2012
The aim of the study was to assess the activity of cathepsin D in polyps removed during first-time FESS surgery and in recurrent polyps removed during successive FESS surgeries.The study examined 24 polyps: 11 polyps were removed during first-time surgical procedures (termed primary polyps in the study), and 13 recurrent polyps were removed in ...
Katarzyna, Pawłowska-Góral, Jarosław, Markowski, Piotr, Wardas, Ewa, Kurzeja, Małgorzata, Witkowska   +4 more
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Cathepsin D Content in Colorectal Cancer

Oncology, 1995
Cathepsin D content and activity were determined in matched paired sets of colorectal tumor tissue and normal mucosa and correlated with a number of biological and clinical parameters. Significantly higher cathepsin D activity was measured in tumor cytosol compared to paired normal mucosa (p < 0.02), in Dukes’ stage A tumors compared to Dukes’ B and
Tumminello F. M., Gebbia N., Pizzolanti G., Russo A., Bazan V., Leto G.   +5 more
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Proteolysis of IGFBPs by cathepsin D in vitro and in cathepsin D-deficient mice

Progress in Growth Factor Research, 1995
Affinity-purified lysosomal protease cathepsin D cleaved recombinant human IGFBP-1 to -5 in fragments of defined sizes, while IGFBP-6 was not degraded. To assess the role of cathepsin D for proteolytic processing of IGFBP in vivo, serum from cathepsin D-deficient mice and conditioned media from cathepsin D-deficient fibroblasts and organ explants were ...
T, Braulke, M, Claussen, P, Saftig, M, Wendland, K, Neifer, B, Schmidt, J, Zapf, K, von Figura, C, Peters   +8 more
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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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IMMUNOHISTOCHEMICAL STUDY ON CATHEPSIN-B AND CATHEPSIN-D IN PANCREATIC-CANCER

Oncology Reports, 1994
Lysosomal enzymes, cathepsin B and D, have been studied in their possible relationship to the ability of malignant cells to invade and metastasize. In the current investigation, these cathepsins were detected immunohistochemically using avidin-biotin-peroxidase complex method in the pancreatic cancer cells of 21 patients.
B, Nakata, H, Appert, S, Lei, Y, Yamashita, Y, Chung, M, Sowa, J, Myles, C, Mao, J, Howard   +8 more
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Cathepsin D, but not cathepsin E, degrades desmosomes during epidermal desquamation

British Journal of Dermatology, 2004
We previously reported that an ambient aspartic proteinase is crucial to desquamation of the stratum corneum at pH 5. Identification of this aspartic proteinase by using enzyme inhibitors suggested it to be cathepsin D, although we could not exclude cathepsin E.To determine the identity of this aspartic proteinase and its distribution within the ...
S, Igarashi, T, Takizawa, T, Takizawa, Y, Yasuda, H, Uchiwa, S, Hayashi, H, Brysk, J M, Robinson, K, Yamamoto, M M, Brysk, T, Horikoshi   +10 more
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Studies on bovine spleen cathepsin D

1977
The purification procedure of cathepsin D which includes autolysis results in the destruction of the molecule to smaller polypeptide chains. Pure catepsin D obtained by the method which includes affinity chromatography, contains single polypeptide chain of 42000 daltons. The N-terminal amino acid is glycine.
V, Turk, I, Kregar, F, Gubensek, S, Lapanje, I, Urh, M, Kovacic   +5 more
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Thermal Stability of Cathepsin D

Journal of Food Science, 1989
ABSTRACT The effect of pH and temperature on Cathepsin D stability was examined using a hemoglobin assay following preincubation of the enzyme at various pH and temperature combinations. The results of the study showed that the enzyme retained 87% of its activity at 45°C (pH 3.5) when compared to a control at 37°C (pH 3.5).
ANNE M. DRAPER, MICHAEL G. ZEECE
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Immunohistochemical and Immunocytochemical Localization of Cathepsin E Compared with Cathepsin D

1991
Recent reports have suggested that cathepsin E is a non-lysosomal aspartic proteinase and that this enzyme participates in extralysosomal proteolysis.1–3 Although its enzymatic and structural properties have been demonstrated,4–7 its physiological function is still unknown.
H, Sakai, T, Saku, Y, Kato, K, Yamamoto
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