Transport of urokinase across the intestinal tract of normal human subjects with stimulation of synthesis and/or release of urokinase-type proteins.

Toki, Naotika; Sumi, Hiroyuki; Sasaki, Koji; Boreisha, Irena G.; Robbins, Kenneth C.

doi:10.1172/jci111818

Cited by 36 publications

(18 citation statements)

References 27 publications

(15 reference statements)

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“…The production was confirmed by MULLERTZ et al (1984), but they neglected it because of the small amount involved. However, TOKI et al (1985) estimated a large amount of the production in the blood after oral administration of clinicaltype high molecular weight UK.…”

Section: Discussionmentioning

confidence: 99%

Production of the modified form of human plasminogen by .ALPHA.2-macroglobulin-plasmin complexes.

et al. 1985

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It has been speculated that the modified form of plasminogen, a precursor of proteolytic enzyme plasmin in plasma, plays an important role in fibrinolysis in the blood. The present study was undertaken to examine the production by a2-macroglobulin-plasmin complexes. a2-macroglobulin-plasmin complexes were purified from urokinase-activated plasma by affinity chromatography on lysine-Sepharose and gel filtration on Ultrogel AcA 22. The plasmin complex converted native plasminogen into the modified form more easily in the presence of s-aminocaproic acid.The modification of native plasminogen by a2-macroglobulin-bound plasmin was completely inhibited by aprotinin, and partly by soybean trypsin inhibitor. a2-macroglobulin-bound plasmin produced modified plasminogen in human plasma where potent plasmin inhibitors exist, though the degree of production was small. The present results support the speculation of the important role of the modified form in vivo.

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Section: Discussionmentioning

confidence: 99%

Production of the modified form of human plasminogen by .ALPHA.2-macroglobulin-plasmin complexes.

et al. 1985

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“…Nevertheless, it has been demonstrated that the active component(s) can be absorbed through the intestinal tract and express their action in the circulation. Nattokinase may induce prourokinase release from liver and thus activate plasminogen in the circulation as suggested for urokinase [5]. In addition, Urano et al [13] demonstrated that their specific nattokinases, subtilisin NAT, inactivated plaminogen activator inhibitor (PAI-1) resulting in enhanced fibrinolysis in vitro.…”

Section: Introductionmentioning

confidence: 98%

“…However, the biological activity of these substances is short lived in the circulation after intravenous administration and there is a significant risk of hemorrhagic complications with a pronounced activation of fibrinolytic activity in whole blood in some circumstances [1][2][3]. Sumi and his colleagues [4,5] were the first to demonstrate fibrinolytic activity in vivo after oral administration of the fibrinolytic enzyme, urokinase. The enzyme was shown to cross the intestinal tract and stimulate systemic fibrinolytic activity.…”

Section: Introductionmentioning

confidence: 99%

The Effect of Dietary Bacillus Natto Productive Protein on in vivo Endogenous Thrombolysis

Yamashita

Oda²,

Giddings³

et al. 2003

Pathophysiol Haemos Thromb

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The influence of dietary bacillus natto productive protein (BNPP) on endogenous thrombolysis was investigated in the rat. Animals were given a standard feed for 14 weeks, to which 0.2 or 1% BNPP was added. Thrombolysis was evaluated using an He-Ne laser-induced thrombosis model in mesenteric microvessels. Changes in thrombus volume, reflecting thrombolysis, decreased to 82% of the initial value in the control group. In contrast, the thrombus volume decreased to 67% in the animals fed 0.2% BNPP, and decreased to 51% in the group given 1% BNPP. The extent of thrombolysis in the 1% BNPP group was equivalent to that seen in animals treated with a bolus intravenous infusion of 0.2 mg/kg tissue plasminogen activator. The results demonstrated that the dietary administration of BNPP enhanced endogenous thrombolysis in a dose-dependent manner. Argatroban (2 mg/kg/h) enhanced endogenous fibrinolysis only in control animals, but not in the BNPP groups. The results support the suggestion that dietary supplementation with BNPP may provide a simple means to promote fibrinolysis not only in the treatment of thromboembolism but also in the prevention of venous occlusion.

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“…12) The usage of proteases by oral administration has also been assessed [13][14][15] for the application of proteases to thromy To whom correspondence should be addressed. Tel: +81-538-21-1134; Fax: +81-538-21-1135; E-mail: sugimoto-s@mercian.co.jp Abbreviations: FP, protease from Fusarium sp.…”

mentioning

confidence: 99%

The Fibrinolytic Activity of a Novel Protease Derived from a Tempeh Producing Fungus,Fusariumsp. BLB

Sugimoto

Fujii

Morimiya

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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Transport of urokinase across the intestinal tract of normal human subjects with stimulation of synthesis and/or release of urokinase-type proteins.

Abstract: Oral administration of clinical-type high molecular weight urokinase (HMW-UK) in a single dose of 30,000-60,000 International Units (IU)

Cited by 36 publications

References 27 publications

Production of the modified form of human plasminogen by .ALPHA.2-macroglobulin-plasmin complexes.

Production of the modified form of human plasminogen by .ALPHA.2-macroglobulin-plasmin complexes.

The Effect of Dietary Bacillus Natto Productive Protein on in vivo Endogenous Thrombolysis

The Fibrinolytic Activity of a Novel Protease Derived from a Tempeh Producing Fungus,Fusariumsp. BLB

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