scholarly journals The Hyaluronan-Binding Serine Protease from Human Plasma Cleaves HMW and LMW Kininogen and Releases Bradykinin

2002 ◽  
Vol 383 (10) ◽  
Author(s):  
M. Etscheid ◽  
N. Beer ◽  
E. Fink ◽  
R. Seitz ◽  
J. Dodt
Keyword(s):  
Human Plasma ◽  
Serine Protease ◽  
Hyaluronan Binding

Proteolytic Activation and Inactivation of the Serine Protease Activity of Plasma Hyaluronan Binding Protein.

2001 ◽  
Vol 24 (5) ◽  
pp. 448-452 ◽  
Author(s):  
Nam-Ho CHOI-MIURA ◽  
Katsuhiko TAKAHASHI ◽  
Madoka YODA ◽  
Kiyomi SAITO ◽  
Toshio MAZDA ◽  
...  
Keyword(s):  
Serine Protease ◽  
Protease Activity ◽  
Binding Protein ◽  
Proteolytic Activation ◽  
Serine Protease Activity ◽  
Hyaluronan Binding

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

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

scholarly journals Regulation Mechanism of the Serine Protease Activity of Plasma Hyaluronan Binding Protein.

2001 ◽  
Vol 24 (3) ◽  
pp. 221-225 ◽  
Author(s):  
Nam-Ho CHOI-MIURA ◽  
Kiyomi SAITO ◽  
Katsuhiko TAKAHASHI ◽  
Madoka YODA ◽  
Motowo TOMITA
Keyword(s):  
Serine Protease ◽  
Protease Activity ◽  
Binding Protein ◽  
Regulation Mechanism ◽  
Serine Protease Activity ◽  
Hyaluronan Binding

scholarly journals Plasma Hyaluronan-binding Protein Is a Serine Protease

2000 ◽  
Vol 275 (30) ◽  
pp. 22978-22985 ◽  
Author(s):  
Alexander A. Vostrov ◽  
Wolfgang W. Quitschke
Keyword(s):  
Serine Protease ◽  
Binding Protein ◽  
Hyaluronan Binding

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.

Activation of proPHBSP, the Zymogen of a Plasma Hyaluronan Binding Serine Protease, by an Intermolecular Autocatalytic Mechanism

2000 ◽  
Vol 381 (12) ◽  
Author(s):  
Michael Etscheid ◽  
Andreas Hunfeld ◽  
Herbert König ◽  
Rainer Seitz ◽  
Johannes Dodt
Keyword(s):  
Serine Protease ◽  
Hyaluronan Binding ◽  
Autocatalytic Mechanism
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