scholarly journals A cysteine proteinase secreted from human breast tumours is immunologically related to cathepsin B

1982 ◽  
Vol 207 (3) ◽  
pp. 633-636 ◽  
Author(s):  
A D Recklies ◽  
A R Poole ◽  
J S Mort
Keyword(s):  
Cathepsin B ◽  
Human Liver ◽  
Cysteine Proteinase ◽  
Human Breast ◽  
Breast Tumours ◽  
Monospecific Antiserum ◽  
Thiol Proteinase

The stable cathepsin B-like cysteine (thiol) proteinase secreted from human breast tumours in culture was shown to be destabilized by mercurial compounds. After such treatment the enzyme cross-reacts in a radioimmunoassay with a monospecific antiserum to human liver cathepsin B. It is suggested that the secreted enzyme may be a precursor form of lysosomal cathepsin B.

scholarly journals A catalytically active high-Mr form of human cathepsin B from sputum

1988 ◽  
Vol 254 (3) ◽  
pp. 693-699 ◽  
Author(s):  
D J Buttle ◽  
B C Bonner ◽  
D Burnett ◽  
A J Barrett
Keyword(s):  
Lysosomal Enzyme ◽  
Active Site ◽  
Cathepsin B ◽  
Human Liver ◽  
Cysteine Proteinase ◽  
Truncated Form ◽  
Physiological Importance ◽  
Catalytically Active ◽  
Human Cathepsin ◽  
Chicken Cystatin

A cysteine proteinase from purulent sputum was partially purified by a method involving affinity chromatography on Sepharose-aminohexanoylphenylalanylglycinaldehyde semicarbazone. It was immunologically related to lysosomal cathepsin B from human liver and was similar in many, but not all, other aspects. It was catalytically active, as demonstrated by active-site-directed radioiodination, and hydrolysed three cathepsin B substrates, two with Km values similar to those of lysosomal cathepsin B. In addition, the rates of inactivation of the sputum and lysosomal forms of the enzyme by L-3-carboxy-2,3-transepoxypropionyl-leucylamido(4-guanidino) butane (Compound E-64) were very similar. However, the sputum enzyme differed from lysosomal cathepsin B in the following respects. Inhibition by chicken cystatin was much weaker for sputum cathepsin B than for the lysosomal enzyme. Sputum cathepsin B had greater stability at pH 7.5 and a higher apparent Mr, even after deglycosylation, than lysosomal cathepsin B. We conclude that the form of cathepsin B found in sputum is probably a truncated form of human procathepsin B, with some differences in properties that could be of physiological importance.

Cytochemical and biochemical evidence of cathepsin B in malignant, transformed and normal breast epithelial cells

1987 ◽  
Vol 87 (1) ◽  
pp. 145-154
Author(s):  
E. Krepela ◽  
J. Bartek ◽  
D. Skalkova ◽  
J. Vicar ◽  
D. Rasnick ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Cathepsin B ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Normal Breast ◽  
Breast Cancer Cell Lines ◽  
Human Breast ◽  
Breast Epithelial Cells ◽  
Breast Epithelial ◽  
Normal Breast Epithelial Cells

Human breast cancer cell lines, as well as transformed mammary epithelial cells (HBL-100) and growth-stimulated normal breast epithelial cells showed positive cytochemical reaction with the proteinase substrate 2-(N-benzyloxycarbonyl-L-arginyl-L-arginylamido)-4-methoxynapht halene, in the presence of 5-nitrosalicylaldehyde. The reaction product, small fluorescent granules, was distributed throughout the cytoplasm, in the perinuclear zone, in some cytoplasmic projections, and at the cell surface. Using a panel of various proteinase inhibitors, we found that the formation of the reaction product was an enzymic function of a cysteine proteinase. Using the substrate 7-(N-benzyloxycarbonyl-L-arginyl-L-arginylamido)-4-methylcoumarin, we evaluated some biochemical properties of the cysteine proteinase, including pH-activity profile, pH stability, apparent relative molecular mass and sensitivity toward various proteinase inhibitors. We found that the proteinase from the studied breast epithelial cells exhibited characteristics of a mature form of cathepsin B. Taken together, the cytochemical and biochemical data provide evidence that human breast epithelial cells of cancer origin, as well as in the transformed or growth-stimulated state express active cathepsin B and compartmentalize it into specific subcellular sites.

scholarly journals Action of human liver cathepsin B on the oxidized insulin B chain

1983 ◽  
Vol 213 (2) ◽  
pp. 467-471 ◽  
Author(s):  
M J McKay ◽  
M K Offermann ◽  
A J Barrett ◽  
J S Bond
Keyword(s):  
Amino Acid ◽  
Cathepsin B ◽  
Human Liver ◽  
Degradation Products ◽  
Cysteine Proteinase ◽  
Cathepsin L ◽  
Amino Acid Content ◽  
Peptide Bond ◽  
Cleavage Sites ◽  
Amino Acid Residues

The lysosomal cysteine proteinase cathepsin B (from human liver) was tested for its peptide-bond specificity against the oxidized B-chain of insulin. Sixteen peptide degradation products were separated by high-pressure liquid chromatography and thin-layer chromatography and were analysed for their amino acid content and N-terminal amino acid residue. Five major and six minor cleavage sites were identified; the major cleavage sites were Gln(4)-His(5), Ser(9)-His(10), Glu(13)-Ala(14), Tyr(16)-Leu(17) and Gly(23)-Phe(24). The findings indicate that human cathepsin B has a broad specificity, with no clearly defined requirement for any particular amino acid residues in the vicinity of the cleavage sites. The enzyme did not display peptidyldipeptidase activity with this substrate, and showed a specificity different from those reported for two other cysteine proteinases, papain and rat cathepsin L.

Characterization of a thiol proteinase secreted by malignant human breast tumours

1980 ◽  
Vol 614 (1) ◽  
pp. 134-143 ◽  
Author(s):  
John S. Mort ◽  
Anneliese D. Recklies ◽  
A.Robin Poole
Keyword(s):  
Human Breast ◽  
Breast Tumours ◽  
Thiol Proteinase

The expression of cytochrome P450 enzymes in human breast tumours and normal breast tissue

2001 ◽  
Vol 70 (1) ◽  
pp. 47-54 ◽  
Author(s):  
Mumtaz Iscan ◽  
Tuula Klaavuniemi ◽  
Tulay Çoban ◽  
Nilgun Kapucuoğlu ◽  
Olavi Pelkonen ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Breast Tissue ◽  
Normal Breast Tissue ◽  
Normal Breast ◽  
Human Breast ◽  
Cytochrome P450 Enzymes ◽  
Breast Tumours

scholarly journals CP30, a Cysteine Proteinase Involved inTrichomonas vaginalis Cytoadherence

2000 ◽  
Vol 68 (9) ◽  
pp. 4907-4912 ◽  
Author(s):  
M. Remedios Mendoza-López ◽  
Cecilia Becerril-Garcia ◽  
Loriz V. Fattel-Facenda ◽  
Leticia Avila-Gonzalez ◽  
Martha E. Ruíz-Tachiquín ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Hela Cell ◽  
Trichomonas Vaginalis ◽  
Cysteine Proteinase ◽  
Collagen Iv ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Cell Monolayers ◽  
Thiol Proteinase

ABSTRACT We describe here the participation of a Trichomonas vaginalis 30-kDa proteinase (CP30) with affinity to the HeLa cell surface in attachment of this parasite to host epithelial cells. The CP30 band is a cysteine proteinase because its activity was inhibited by E-64, a thiol proteinase inhibitor. In two-dimensional substrate gel electrophoresis of total extracts of the trichomonad isolate CNCD 147, three spots with proteolytic activity were detected in the 30-kDa region, in the pI range from 4.5 to 5.5. Two of the spots (pI 4.5 and 5.0) bound to the surfaces of fixed HeLa cells corresponding to the CP30 band. The immunoglobulin G fraction of the rabbit anti-CP30 antiserum that recognized a 30-kDa band by Western blotting and immunoprecipitated CP30 specifically inhibited trichomonal cytoadherence to HeLa cell monolayers in a concentration-dependent manner and reacted with CP30 at the parasite surface. CP30 degraded proteins found on the female urogenital tract, including fibronectin, collagen IV, and hemoglobin. Interestingly, CP30 digested fibronectin and collagen IV only at pH levels between 4.5 and 5.0. Moreover, trichomonosis patients whose diagnosis was confirmed by in vitro culture possessed antibody to CP30 in both sera and vaginal washes, and CP30 activity was found in vaginal washes. Our results suggest that surface CP30 is a cysteine proteinase necessary for trichomonal adherence to human epithelial cells.

A cross-linking assay allows the detection of receptors for the somatostatin analogue, lanreotide in human breast tumours

1993 ◽  
Vol 29 (11) ◽  
pp. 1589-1592 ◽  
Author(s):  
Grégoire Prévost ◽  
Philippe Provost ◽  
Valérie Sallé ◽  
Monique Lanson ◽  
François Thomas
Keyword(s):  
Cross Linking ◽  
Somatostatin Analogue ◽  
Human Breast ◽  
Breast Tumours

scholarly journals Rapid assay for thein vitro chemosensitivity testing of human breast tumours

1989 ◽  
Vol 11 (6) ◽  
pp. 244-244
Author(s):  
R. F. M. Oude Elferink ◽  
H. M. J. Goldschmidt ◽  
H. J. Majoor ◽  
J. F. Leijten
Keyword(s):  
Human Breast ◽  
Breast Tumours ◽  
Chemosensitivity Testing ◽  
Rapid Assay

Significance of Ca antigen expression in human breast tumours

1985 ◽  
Vol 13 (2) ◽  
pp. 458-458
Author(s):  
DAKSHA P. TRIVEDI ◽  
HAROLD BAUM ◽  
MICHAEL BAUM
Keyword(s):  
Antigen Expression ◽  
Human Breast ◽  
Breast Tumours
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