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.

Detection of low molecular weight cysteine proteinase inhibitors by time-resolved fluoroimmunoassay

1986 ◽  
Vol 86 (2) ◽  
pp. 243-247 ◽  
Author(s):  
I. Joronen ◽  
V.K. Hopsu-Havu ◽  
M. Manninen ◽  
A. Rinne ◽  
M. Järvinen ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Low Molecular Weight ◽  
Time Resolved ◽  
Cysteine Proteinase Inhibitors

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.

Three low molecular weight cysteine proteinase inhibitors of human seminal fluid: Purification and enzyme kinetic properties

Biochimie ◽  
2013 ◽  
Vol 95 (8) ◽  
pp. 1552-1559 ◽  
Author(s):  
Vikash Kumar Yadav ◽  
Nirmal Chhikara ◽  
Kamaldeep Gill ◽  
Sharmistha Dey ◽  
Sarman Singh ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Seminal Fluid ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Low Molecular Weight ◽  
Kinetic Properties ◽  
Enzyme Kinetic ◽  
Cysteine Proteinase Inhibitors

Proteinases inTrichomonas vaginalisandTritrichomonas mobilensisare not exclusively of cysteine type

Parasitology ◽  
1991 ◽  
Vol 102 (1) ◽  
pp. 113-115 ◽  
Author(s):  
P. Bózner ◽  
P. Demeš
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Trichomonas Vaginalis ◽  
Chelating Agents ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
The Other ◽  
Polyacrylamide Gels ◽  
Cysteine Proteinase Inhibitors

SUMMARYHigh molecular weight proteinases ofTrichomonas vaginalis(with apparentMrvalues 142 and > 220 kDa) andTritrichomonas mobilensis(Mr67, 86, 104 and 120 kDa), optimally active at pH 8, were analysed in gelatin-containing polyacrylamide gels. All of these proteinases were resistant to serine-, aspartic- as well as cysteine proteinase inhibitors. Both proteolytic bands inT. vaginalisand two proteinases inT. mobilensis(67 and 104 kDa) were inhibited by EDTA and EGTA suggesting that they belong to the metallo-proteinase class. The 67 kDa proteinase ofT. mobilensiswas inhibited also byo-phenanthroline. The other two bands ofT. mobilensis(86, 120 kDa) were not classified to any proteinase group since they appeared to be resistant to the chelating agents tested in this study.

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