Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats

Biochemistry ◽  
1986 ◽  
Vol 25 (9) ◽  
pp. 2410-2417 ◽  
Author(s):  
Dominic W. Chung ◽  
Kazuo Fujikawa ◽  
Brad A. McMullen ◽  
Earl W. Davie
Keyword(s):  
Human Plasma ◽  
Serine Protease ◽  
Tandem Repeats

Activation of Kallikrein-Kinin System in Human Plasma with Purified Serine Protease from Dermatophagoides farinae

1990 ◽  
Vol 91 (1) ◽  
pp. 80-85 ◽  
Author(s):  
Katsunobu Takahashi ◽  
Takashi Aoki ◽  
Shoichi Kohmoto ◽  
Hiroyuki Nishimura ◽  
Yoh Kodera ◽  
...  
Keyword(s):  
Human Plasma ◽  
Serine Protease ◽  
Kinin System ◽  
Kallikrein Kinin System

Evidence for the presence of serine-protease in the preparation of the very low density lipoproteins in human plasma

Biochimie ◽  
1978 ◽  
Vol 60 (5) ◽  
pp. 529-533
Author(s):  
Norma Amit ◽  
Marise Ayrault-Jarrier ◽  
Monique Davril ◽  
Kia-Ki Han
Keyword(s):  
Human Plasma ◽  
Serine Protease ◽  
Low Density Lipoproteins ◽  
Low Density ◽  
Very Low Density Lipoproteins

Inhibition of Aeromonas sobria serine protease (ASP) by α2-macroglobulin

2012 ◽  
Vol 393 (10) ◽  
pp. 1193-1200 ◽  
Author(s):  
Yoji Murakami ◽  
Yoshihiro Wada ◽  
Hidetomo Kobayashi ◽  
Atsushi Irie ◽  
Makoto Hasegawa ◽  
...  
Keyword(s):  
Human Plasma ◽  
Serine Protease ◽  
Defense Mechanism ◽  
Gel Filtration ◽  
Correlation Spectroscopy ◽  
Coagulation Disorder ◽  
Dependent Manner ◽  
Aeromonas Sobria ◽  
Host Defense Mechanism

Abstract ASP is a serine protease secreted by Aeromonas sobria. ASP cleaves various plasma proteins, which is associated with onset of sepsis complications, such as shock and blood coagulation disorder. To investigate a host defense mechanism against this virulence factor, we examined the plasma for ASP inhibitor(s). Human plasma inhibited ASP activity for azocasein, which was almost completely abolished by treating plasma with methylamine, which inactivates α2-macroglobulin (α2-MG). The ASP-inhibitor complex in ASP-added plasma was not detected by immunoblotting using anti-ASP antibody; however, using gel filtration of the plasma ASP activity for an oligopeptide, the ASP substrate was eluted in the void fraction (Mw>200 000), suggesting ASP trapping by α2-MG. Indeed, human α2-MG inhibited ASP azocaseinolytic activity in a dose-dependent manner, rapidly forming a complex with the ASP. Fibrinogen degradation by ASP was completely inhibited in the presence of α2-MG. α1-Protease inhibitor, antithrombin, and α2-plasmin inhibitor neither inhibited ASP activity nor formed a complex with ASP. Surprisingly, ASP degraded these plasma serine protease inhibitors. Thus, α2-MG is the major ASP inhibitor in the human plasma and can limit ASP virulence activities in A. sobria infection sites. However, as shown by fluorescence correlation spectroscopy, slow ASP inhibition by α2-MG in plasma may indicate insufficient ASP control in vivo.

An Endogenous Protease Activating Plasma Inactive Renin

1978 ◽  
Vol 55 (s4) ◽  
pp. 133s-134s ◽  
Author(s):  
B. J. Leckie
Keyword(s):  
Human Plasma ◽  
Serine Protease ◽  
Protease Inhibitors ◽  
Trypsin Inhibitor ◽  
Soya Bean ◽  
Acid Activation ◽  
Bean Trypsin Inhibitor ◽  
Inactive Renin ◽  
Inhibited Acid ◽  
Endogenous Protease

1. The protease inhibitors Trasylol and soya-bean trypsin inhibitor prevented the activation of plasma inactive renin by acid. 2. N-Ethylmaleimide inhibited acid-activation to some extent but o-phenanthroline had no effect. 3. Acid-activation of the inactive renin in human plasma is mediated by a serine protease.

Structure of the Human Factor VII Gene

1987 ◽  
Author(s):  
Patrick J O'hara ◽  
Frank A Grant ◽  
A Betty ◽  
J Haldmen ◽  
Mark J Murray
Keyword(s):  
Serine Protease ◽  
Vitamin K ◽  
Protein C ◽  
Tandem Repeats ◽  
Human Factor ◽  
Factor Ix ◽  
Factor Vii ◽  
Factor X ◽  
X Protein ◽  
Additional Exon

Factor VII is a member of a family of vitamin K-dependent, gamma-carboxylated plasma protein which includes factor IX, factor X, protein C, protein S and prothrombin. Activated factor VII (factor Vila) is a plasma serine protease which participates in a cascade of reactions leading to the coagulation of blood. Two overlapping genomic clones containing sequences encoding human factor VII were isolated and characterized. The complete sequence of the gene was determined and found to span 12.8 kilobases. The mRNA for factor VII as demonstrated by cDNA cloning is polyadenylated at multiple sites but contains only one AAUAAA poly-A signal sequence. The mRNA can undergo alternative splicing forming one transcript containing eight segments as exons and another with an additional exon which encodes a larger pre-pro leader sequence. The portion of the pre-pro leader coded for by the additional exon has no known counterpart in the other vitamin K-dependent proteins. The positions of the introns with respect to the amino acid sequence encoded by the eight essential exons of factor VII are the same as those present in factor IX, factor X, protein C and the first three exons of prothrombin. These exons code for domains generally conserved among members of this gene family, including a pre-pro leader (the essential exon la and alternative exon lb), a gamma-carboxylated domain (exons 2 and 3) a growth factor domain (exons 4 and 5) an activation region (exon 6) and a serine protease (exon 8). The corresponding introns in these genes are dissimilar with respect to size and sequence, with the exception of the third intron in factor VII and protein C. Four introns and a portion of exon 8 in factor VII contain regions made up of tandem repeats of oligonucleotide monomer elements. More than a quarter of the intron sequences and more than a third of the 3' untranslated portion of the mRNA transcript consist of these minisatellite tandem repeats. This type of structure is responsible for polymorphisms due to allelic variation in repeat copy number in other areas of the human genome. Tandem repeats can evolve as a result of random crossover in DNA whose sequence is not maintained by selection. This suggests that much of the sequence information present in the introns and untranslated portion of the message is dispensable.

Effects of iron and carbon monoxide on Lachesis muta muta venom-mediated degradation of plasmatic coagulation

2016 ◽  
Vol 36 (7) ◽  
pp. 727-733 ◽  
Author(s):  
VG Nielsen ◽  
RW Matika
Keyword(s):  
Carbon Monoxide ◽  
Human Plasma ◽  
Serine Protease ◽  
Analytical Techniques ◽  
Clinical Consequence ◽  
Mediated Effects ◽  
Plasmatic Coagulation ◽  
Lachesis Muta ◽  
Co Addition ◽  
Heparin Exposure

Hypofibrinogenemia is an important clinical consequence following envenomation by Lachesis muta muta, usually attenuated or prevented by administration of antivenom. The venom of L. m. muta contains both a metalloproteinase fibrinogenase and a serine protease thrombin-like enzyme, and exposure of fibrinogen to iron (Fe) and carbon monoxide (CO) has been demonstrated to decrease its catalysis by such enzymes. Using thrombelastographic analytical techniques, it was determined that this venom displayed weak procoagulant effects combined with fibrinogenolytic effects, and pretreatment of plasma with Fe and CO markedly attenuated venom-mediated effects. Additional experiments involving heparin exposure and varying calcium concentrations demonstrated that modification of fibrinogen with Fe and CO in human plasma rendered fibrinogen not recognizable to the fibrinogenolytic metalloproteinase but did not prevent polymerization by the thrombin-like serine protease. Lastly, when venom was exposed to CO in isolation and then placed in plasma, the fibrinogenase was inhibited but the thrombin-like enzyme was not inhibited. In sum, utilizing relatively facile modifications, we demonstrated with thrombelastography that Fe and/or CO addition can protect human plasmatic coagulation from fibrinogenase activity but not the effects of the thrombin-like activity of L. m. muta venom.

Excessively activated plasminogen in human plasma cleaves VWF multimers and reduces collagen-binding activity

2020 ◽  
Vol 168 (4) ◽  
pp. 355-363
Author(s):  
Kenshi Togashi ◽  
Satoshi Suzuki ◽  
Sae Morita ◽  
Yuki Ogasawara ◽  
Yasutada Imamura ◽  
...  
Keyword(s):  
Shear Stress ◽  
Human Plasma ◽  
Serine Protease ◽  
Von Willebrand Factor ◽  
Binding Activity ◽  
Cleavage Sites ◽  
Binding Ability ◽  
Collagen Binding ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract Plasmin (Pm) is a serine protease that can dissolve fibrin clots. Several possible functions of Pm in blood other than fibrinolysis have been proposed. To explore the effects of Pm on primary haemostasis, we evaluated the cleavage of von Willebrand factor multimers (VWFMs) in human plasma by streptokinase (SK)-activated plasminogen (Pg) and the binding ability of the digested VWFMs to collagen. SK-activated Pg and ADAMTS13 (a VWF-cleaving enzyme) in human plasma cleaved VWFMs in conformation-dependent manners through dialysis to the urea-containing buffer. However, VWFMs in human plasma under vortex-based shear stress were cleaved by SK-activated Pg but not by ADAMTS13. These results suggested that the VWFM-cleavage sites in human plasma are exposed to some extent by vortex-based shear stress for Pm but not for ADAMTS13. Additionally, we revealed that cleavage by SK-activated Pg reduced VWFMs’ binding ability to collagen, and VWFMs in human plasma were cleaved by Pm at several sites. These results suggest that SK-activated Pg degrades VWFMs, reduces their binding abilities to collagen and affects primary haemostasis. Because excessive Pg activation can degrade fibrinogen/fibrin, we propose that SK-activated Pg in blood may cause impaired primary and secondary haemostasis.

scholarly journals Activation of the Kallikrein-Kinin System in Human Plasma by a Serine Protease from Mites.

1991 ◽  
Vol 10 (1) ◽  
pp. 15-20 ◽  
Author(s):  
Shoichi KOHMOTO ◽  
Yoh KODERA ◽  
Katsunobu TAKAHASHI ◽  
Hiroyuki NISHIMURA ◽  
Ayako MATSUSHIMA ◽  
...  
Keyword(s):  
Human Plasma ◽  
Serine Protease ◽  
Kinin System ◽  
Kallikrein Kinin System
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