The trypsin inhibitor-like domain is required for a serine protease inhibitor of Haemonchus contortus to inhibit host coagulation

2021 ◽  
Author(s):  
Fei Wu ◽  
Hui Zhang ◽  
Jingru Zhou ◽  
Jie Wu ◽  
Danni Tong ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Serine Protease ◽  
Trypsin Inhibitor ◽  
Haemonchus Contortus ◽  
Serine Protease Inhibitor

scholarly journals 3' Noncoding sequences of the CTA 1 gene enhance expression of the recombinant serine protease inhibitor, CPTI II, in Saccharomyces cerevisiae.

1996 ◽  
Vol 43 (3) ◽  
pp. 525-529 ◽  
Author(s):  
M Stankiewicz ◽  
B Rempoła ◽  
M Fikus
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protease Inhibitor ◽  
Serine Protease ◽  
Trypsin Inhibitor ◽  
Yeast Strain ◽  
Serine Protease Inhibitor ◽  
Expression Cassette ◽  
Noncoding Sequences ◽  
Gene Coding

Expression of the gene coding for the recombinant trypsin inhibitor, CPTI II, was enhanced tenfold when yeast transcription terminating sequences were added to the expression cassette of the pJK6 yeast vector. The yield was further increased about 20% in the BJ5464 yeast strain, defective in vacuolar proteases.

Serine Protease Inhibitor Kazal Type 1 (SPINK1): Beyond the Trypsin Inhibitor

2009 ◽  
Vol 5 (2) ◽  
pp. 110-116 ◽  
Author(s):  
Masaki Ohmuraya ◽  
Nobuyuki Ozaki ◽  
Masahiko Hirota ◽  
Hideo Baba ◽  
Ken-ichi Yamamura
Keyword(s):  
Protease Inhibitor ◽  
Serine Protease ◽  
Trypsin Inhibitor ◽  
Serine Protease Inhibitor

scholarly journals A trypsin-like platelet protease propagates protease-activated receptor-1 cleavage and platelet activation

1998 ◽  
Vol 336 (2) ◽  
pp. 283-285 ◽  
Author(s):  
Frederick A. OFOSU ◽  
John FREEDMAN ◽  
Lori DEWAR ◽  
Yinqi SONG ◽  
John W. FENTON
Keyword(s):  
Protease Inhibitor ◽  
Serine Protease ◽  
G Protein ◽  
Platelet Activation ◽  
Trypsin Inhibitor ◽  
Cysteine Proteases ◽  
Serine Protease Inhibitor ◽  
Soybean Trypsin Inhibitor ◽  
Perivascular Cells ◽  
Protease Activated Receptor 1

Protease-activated receptor-1 (PAR-1) is a G-protein-linked receptor on platelets and perivascular cells activated by α-thrombin and the PAR-1-activating peptide, SFLLRN. α-Thrombin activates PAR-1 by cleaving it at R41–S42 to release the 41-residue peptide TR(1–41). Unexpectedly, platelet activation with SFLLRN was also associated with PAR-1 cleavage and the release of TR(1–41). Both PAR-1 cleavage and platelet activation resulting from SFLLRN addition to platelets were markedly inhibited by the serine protease inhibitor 4,2-(aminoethyl)-benzene sulphonylfluoride·HCl (pefabloc SC) and soybean trypsin inhibitor, but not by inhibitors of calpain, cysteine proteases or metalloproteases. Thus, a trypsin-like platelet protease propagates SFLLRN-dependent PAR-1 cleavage and platelet activation.

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