Results 261 to 270 of about 113,729 (277)

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
openaire   +1 more source

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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Cathepsin E and Cathepsin D: Biosynthesis, Processing and Subcellular Location

1995
Intracellular protein turnover occurs via two major pathways, lysosomal and nonlysosomal proteolytic pathways. Cathepsins D (CD) and E (CE) are two major intracellular aspartic proteinases in mammalian cells. Besides their structural and immunological distinction (1–5), they are different in both tissue distribution and intracellular localization (4, 6)
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Cathepsin D in laryngeal cancer

Pathology, research and practice, 1997
Prognostic valuae of Cathepsin D in the epitel and stroma laryngeal carcinoma.
Seiwerth, Sven, Vasilj, Ankica, Konjevoda, Paško, Manojlović, Spomenka, Bura, Mladen, Klapan, Ivan, Đanić, Davor   +6 more
openaire   +3 more sources

Cathepsin D in erythroid cells.

Progress in clinical and biological research, 1990
We have detected, solubilized, and purified to near-homogeneity a membrane-bound acid protease from rabbit reticulocytes. Chemical, physical, immunological, and catalytic characterization demonstrate that the enzyme is cathepsin D. With cytochrome b5 as substrate, the enzyme shows a surprisingly high pH optimum and is stimulated by ATP and DPG ...
D E, Hultquist, C, Rodriguez, D A, Schafer   +2 more
openaire   +1 more source

Cathepsin D

2019
Martin Fusek, Václav Větvička
openaire   +1 more source

Cathepsin D and breast cancer

European Journal of Cancer, 1996
B R, Westley, F E, May
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