Experimental model of venous thrombosis in rats and effect of some agents

Kumada, Toshihiko; Ishihara, Mamoru; Ogawa, Hidemasa; Abiko, Yasushi

doi:10.1016/0049-3848(80)90183-8

Cited by 60 publications

(25 citation statements)

References 20 publications

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“…Data were represented mean ± SD (n = 5). Fibrinolytic activity of the LK inclusion bodies (IB) was evaluated using a rat model of venous thrombosis (Kumada et al, 1980). The inclusion bodies suspended in a 0.5% carboxylmethyl cellulose (CMC) solution was administered orally for 5 days.…”

Section: Resultsmentioning

confidence: 99%

“…At this point, 1.0 mM of IPTG (isopropyl-α-thio-galactopyranoside) (Stratagene, Heidelbergh, Germany) was added, and the cells were re-incubated for 4 hrs at 37 o C, and centrifuged at 12,000 × g for 30 min at 4 o C. The insoluble protein pellets and supernatants were then separated, and the supernatants were concentrated with 1.0% of trichloroacetic acid and freeze-dried. The insoluble protein pellets were sonicated and centrifuged at 12,000 × g for 30 min at 4 o C. The insoluble protein pellets (LK inclusion bodies) were washed twice with 1% Triton X-100, resuspended in 150 µl of 1.0 mM Tris · HCl buffer (pH 7.6), and used for SDS-PAGE (Laemmli, 1970) and to determine fibrinolytic activity (Kumada et al, 1980;Cho et al, 2004).…”

Section: Sequencing and Computer Analysis Of Lk6 Gene Cdnasmentioning

confidence: 99%

“…In vivo fibrinolytic activity of the protease from E. coli The fibrinolytic activity of the lumbrokinase (LK) inclusion bodies produced by the E. coli system, was evaluated using a rat model of venous thrombosis (Kumada et al, 1980) with some modification. Briefly, the inclusion bodies were resuspended in 50 mM phosphate buffer (pH 7.4), washed twice with 1.0% Triton X-100, rewashed with phosphate buffer, and freeze-dried.…”

Section: Sequencing and Computer Analysis Of Lk6 Gene Cdnasmentioning

confidence: 99%

See 2 more Smart Citations

Molecular Cloning, Sequencing, and Expression of a Fibrinolytic Serine-protease Gene from the Earthworm Lumbricus rubellus

Cho

Choi²,

Lee³

2004

BMB Reports

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The full-length cDNA of the lumbrokinase fraction 6 (F6) protease gene of Lumbricus rubellus was amplified using an mRNA template, sequenced and expressed in E. coli cells. The F6 protease gene consisted of pro-and mature sequences by gene sequence analysis, and the protease was translated and modified into active mature polypeptide by N-terminal amino acid sequence analysis of the F6 protease. The pro-region of F6 protease consisted of the 44 residues from methionine-1 to lysine-44, and the mature polypeptide sequence (239 amino acid residues and one stop codon; 720 bp) started from isoleucine-45 and continued to the terminal residue. F6 protease gene clones having pro-mature sequence and mature sequence produced inclusion bodies in E. coli cells. When inclusion bodies were orally administrated rats, generated thrombus weight in the rat's venous was reduced by approximately 60% versus controls. When the inclusion bodies were solubilized in pepsin and/or trypsin solutions, the solubilized enzymes showed hemolytic activity in vitro. It was concluded the F6 protease has hemolytic activity, and that it is composed of pro-and mature regions.

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Section: Resultsmentioning

confidence: 99%

Section: Sequencing and Computer Analysis Of Lk6 Gene Cdnasmentioning

confidence: 99%

Section: Sequencing and Computer Analysis Of Lk6 Gene Cdnasmentioning

confidence: 99%

See 1 more Smart Citation

Molecular Cloning, Sequencing, and Expression of a Fibrinolytic Serine-protease Gene from the Earthworm Lumbricus rubellus

Cho

Choi²,

Lee³

2004

BMB Reports

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“…Numerous methods are available to produce experimental thrombosis in vivo (Philp, 1979), however, the specific physiological mechanisms involved in thrombus formation in individual models are not always clear, with many models exhibiting a typical red (venous) as opposed to white (arterial) thrombi. Recently, models have been described by Ashida, Sakuma & Abiko (1980) who used a vascular shunt in rats to produce occlusive thrombi, and Kumada, Ishihara, Ogawa & Abiko (1980) who induced thrombus formation in rats by the insertion of a steel wire into the vena cava. Seuter, Busse, Meng, Hoffmeister, Moller & Horstmann (1979) has described a model in which the vessels of rats were chilled to cause occlusive thrombi.…”

Section: Introduction Methodsmentioning

confidence: 99%

Fibrin, Red Cell and Platelet Interactions in an Experimental Model of Thrombosis

Smith

White

1982

British J Pharmacology

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Insertion of a cotton thread into an arteriovenous shunt of an anaesthetized rat causes an increase in the weight of the thread due to deposition of thrombus. The thrombus formed was of the venous (red) type, being sensitive to heparin, yet possessed important characteristics of an arterial thrombus, in that it was dependent on platelets and on rate of blood flow. Thromboxane synthetase inhibitors had no effect on thrombus deposition. Cyclo‐oxygenase inhibitors did not significantly depress thrombus formation at doses which inhibited platelet function ex vivo. Compounds which can modify the release or action of adenosine 5′‐diphosphate partly inhibited thrombus formation. A depression in clotting factor levels induced by sodium warfarin led to a highly significant reduction in thrombus formation at doses which caused a prolongation of prothrombin clotting time.

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“…In another model, a metallic spiral placed in the inferior vena cava of the rat produces a well-organised fibrin thrombus within 48 h [100]. Unlike aspirin.…”

Section: Coagulation-dependent Modelsmentioning

confidence: 99%

Ticlopidine: A Promise for the Prevention and Treatment of Thrombosis and Its Complications

Panak¹,

Maffrand²,

Picard-Fraire³

et al. 1983

Pathophysiol Haemos Thromb

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Experimental model of venous thrombosis in rats and effect of some agents

Cited by 60 publications

References 20 publications

Molecular Cloning, Sequencing, and Expression of a Fibrinolytic Serine-protease Gene from the Earthworm Lumbricus rubellus

Molecular Cloning, Sequencing, and Expression of a Fibrinolytic Serine-protease Gene from the Earthworm Lumbricus rubellus

Fibrin, Red Cell and Platelet Interactions in an Experimental Model of Thrombosis

Ticlopidine: A Promise for the Prevention and Treatment of Thrombosis and Its Complications

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