Expression of High Molecular Weight Cysteine Proteinase Inhibitor in Ovarian Cancer Tissues: Regulation of Cathepsin B Expression by Placental CPI

2003 ◽  
Vol 384 (7) ◽  
Author(s):  
M. Siewiński ◽  
Y. Saleh ◽  
A. Popiela ◽  
P. Ziólkowski ◽  
M. Jeleń ◽  
...  
Keyword(s):  
Ovarian Cancer ◽  
Molecular Weight ◽  
High Molecular Weight ◽  
Cathepsin B ◽  
Proteinase Inhibitor ◽  
Cysteine Proteinase ◽  
Cysteine Proteinase Inhibitor ◽  
Cancer Tissues

scholarly journals Cystatin F Is a Glycosylated Human Low Molecular Weight Cysteine Proteinase Inhibitor

1998 ◽  
Vol 273 (38) ◽  
pp. 24797-24804 ◽  
Author(s):  
Jian Ni ◽  
Marcia Alvarez Fernandez ◽  
Lena Danielsson ◽  
Rajeev A. Chillakuru ◽  
Junli Zhang ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Proteinase Inhibitor ◽  
Cysteine Proteinase ◽  
Low Molecular Weight ◽  
Cysteine Proteinase Inhibitor

Effect of Cysteine Proteinase Inhibitors on Murine B16 Melanoma Cell Invasion in vitro

2002 ◽  
Vol 383 (5) ◽  
pp. 839-842 ◽  
Author(s):  
Natasa Sever ◽  
Metka Filipic ◽  
Joze Brzin ◽  
Tamara T. Lah
Keyword(s):  
Cell Invasion ◽  
Cathepsin B ◽  
Proteinase Inhibitor ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Cathepsin L ◽  
Cysteine Proteinase Inhibitor ◽  
Cysteine Proteinases ◽  
Cysteine Proteinase Inhibitors

Abstract Various types of proteinases are implicated in the malignant progression of human and animal tumors. Proteinase inhibitors may therefore be useful as therapeutic agents in antiinvasive and antimetastatic treatment. The aims of this study were (1) to estimate the relative importance of proteinases in B16 cell invasion in vitro using synthetic, classspecific proteinase inhibitors and (2) to assess the inhibitory effect of some naturally occurring cysteine proteinase inhibitors. Serine proteinase inhibitor reduced invasiveness by up to 24%, whereas inhibition of aspartic proteinases reduced invasion by 11%. Synthetic inhibitors of cysteine proteinases markedly impaired invasion: cathepsin B inhibitors, particularly Ca 074Me, inhibited invasion from 20 40%, whereas cathepsin L inhibitor Clik 148 reduced invasion by 11%. The potato cysteine proteinase inhibitor PCPI 8.7 inhibited invasion by 21%, whereas another potato inhibitor, PCPI 6.6, and the mushroom cysteine proteinase inhibitor clitocypin had no effects. As the inhibitors that inhibited cathepsin B were in general more efficient at impairing the invasiveness, we conclude that of the two cysteine proteinases, cathepsin B plays a more important role than cathepsin L in murine melanoma cell invasion.

Inhibition of the cathepsin B like proteinase by a low molecular weight cysteine-proteinase inhibitor from ascitic fluid and plasma α2 macroglobulin

1986 ◽  
Vol 64 (12) ◽  
pp. 1218-1225 ◽  
Author(s):  
Maurice Pagano ◽  
Daniel Keppler ◽  
Veronique Fumeron-Dalet ◽  
Robert Engler
Keyword(s):  
Molecular Weight ◽  
Ascitic Fluid ◽  
Cathepsin B ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Low Molecular Weight ◽  
Cysteine Proteinase Inhibitor ◽  
Cysteine Proteinase Inhibitors ◽  
Α2 Macroglobulin ◽  
Endopeptidase Activity

The cathepsin B like proteinase present in ascitic fluid of a patient with neoplasia has been purified and characterized after pepsin activation. From this fluid we have prepared the low molecular weight (LMW) cysteine-proteinase inhibitors. Three major inhibitor forms were found with isoelectric points of 7.4, 5.4, and 5.1, respectively. The interaction of the enzyme with the former inhibitor was studied because this inhibitor was the most abundant. The Ki value was found to be 4.3 × 10−8 M. Two molecules of this proteinase were bound by one molecule of plasma α2 macroglobulin (α2M). The LMW inhibitor was able to bind to the enzyme entrapped in α2M and reduced its endopeptidase activity on benzyloxycarbonyl-L-phenylalanyl-L-arginine-4-methyl-7-coumarylamide. These results may have a physiological significance in the regulation of the enzyme which, among other extracellular hydrolases, probably plays an important role in tumor invasion.

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