Localization of cysteine proteinases and an endogenous cysteine proteinase inhibitor in cultured muscle cells

1985 ◽  
Vol 13 (6) ◽  
pp. 1018-1021 ◽  
Author(s):  
J. W. C. BIRD ◽  
L. WOOD ◽  
I. SOHAR ◽  
E. FEKETE ◽  
R. COLELLA ◽  
...  
Keyword(s):  
Proteinase Inhibitor ◽  
Cysteine Proteinase ◽  
Muscle Cells ◽  
Cysteine Proteinase Inhibitor ◽  
Cysteine Proteinases

scholarly journals Expression of Cysteine Proteinases Cathepsins B and K and of Cysteine Proteinase Inhibitor Cystatin C in Giant Cell Tumor of Tendon Sheath

2001 ◽  
Vol 14 (4) ◽  
pp. 318-324 ◽  
Author(s):  
Torsten Hansen ◽  
Peter K Petrow ◽  
Andreas Gaumann ◽  
Gernot M Keyszer ◽  
Mike Otto ◽  
...  
Keyword(s):  
Giant Cell Tumor ◽  
Giant Cell ◽  
Cystatin C ◽  
Proteinase Inhibitor ◽  
Cysteine Proteinase ◽  
Tendon Sheath ◽  
Cell Tumor ◽  
Cysteine Proteinase Inhibitor ◽  
Cysteine Proteinases

Involvement of cysteine proteinases in excystment of Paragonimus ohirai metacercariae induced by sodium cholate and A23187

2003 ◽  
Vol 77 (1) ◽  
pp. 21-26 ◽  
Author(s):  
T. Ikeda
Keyword(s):  
Proteinase Inhibitor ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Serine Proteinase ◽  
Sodium Cholate ◽  
Cysteine Proteinase Inhibitor ◽  
Cysteine Proteinases ◽  
Serine Proteinase Inhibitor ◽  
Similar Activity

AbstractThe involvement of intrinsic proteinases in the excystment of Paragonimus ohirai metacercariae was studied in in vitro excystment induced by sodium (Na) cholate, a bile salt and A23187, a Ca2+ ionophore. The effects of various proteinase inhibitors on the in vitro excystment were examined and similar inhibitory profiles were obtained. Benzyloxycarbonyl-L-leucyl-L-leucinal (Z-Leu-Leu-H), a cysteine proteinase inhibitor and 4-(2-aminoethyl)-benzenesulfonyl fluoride (Pefabloc SC), a serine proteinase inhibitor completely inhibited excystment, while L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido (4-guanidino)-butane (E-64), a cysteine proteinase inhibitor and leupeptin, a cysteine/serine proteinase inhibitor permitted partial excystment at a lower rate, but inhibited it from proceeding from the partial excystment stage. In secretions released from metacercariae during excystment, proteinase activities detected towards various fluorogenic peptidyl substrates were almost completely inhibited by Z-Leu-Leu-H and E-64, but not by Pefabloc SC. Sodium cholate induced a higher secretion of cysteine proteinases and a higher rate of excystment than A23187. Profiles of cysteine proteinase activities towards five peptidyl substrates detected were markedly different among the two secretions and the lysate of newly excysted juveniles. Newly excysted juveniles released cysteine proteinases with similar activity profiles and levels to metacercariae induced by Na cholate-incubation, whereas the release of cysteine proteinases was reduced compared with metacercariae induced by A23187-incubation. These results provide valuable information about the involvement of intrinsic proteinases in metacercarial excystment.

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.

scholarly journals A novel cysteine proteinase inhibitor from seeds of Enterolobium contortisiliquum and its effect on Callosobruchus maculatus larvae

2021 ◽  
Vol 25 ◽  
pp. 100876
Author(s):  
Natalia N.S. Nunes ◽  
Rodrigo S. Ferreira ◽  
Leonardo F.R. de Sá ◽  
Antônia Elenir A. de Oliveira ◽  
Maria Luiza V. Oliva
Keyword(s):  
Proteinase Inhibitor ◽  
Callosobruchus Maculatus ◽  
Cysteine Proteinase ◽  
Cysteine Proteinase Inhibitor

Purification and Structure of a Novel Cysteine Proteinase Inhibitor, Strepin P-1

1985 ◽  
Vol 49 (3) ◽  
pp. 799-805
Author(s):  
Kyoichi Ogura ◽  
Mitsuru Maeda ◽  
Masami Nagai ◽  
Takaharu Tanaka ◽  
Kyosuke Nomoto ◽  
...  
Keyword(s):  
Proteinase Inhibitor ◽  
Cysteine Proteinase ◽  
Cysteine Proteinase Inhibitor
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