Urokinase

Duckert, F

doi:10.1007/978-3-642-66863-0_8

Cited by 9 publications

(4 citation statements)

References 102 publications

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“…2) and the degradation of the fibrinogen in the plasma (Fig. 3) are caused by urokinase nonspecifically (5,25).…”

Section: Discussionmentioning

confidence: 94%

“…Urokinase, an isolate from human urine that consists of two polypeptide chains linked by one disulfide bond (molecular weight 50,000), has been used clinically in thrombolytic therapy. Thrombolysis by urokinase is associated with systemic plasminogen activation, the degradation of fibrinogen and the coagulation proteins in circulating blood (5,25). In contrast, the t-PA produced by a human melanoma cell line has been shown to be a more specific and effective thrombolytic agent than urokinase because of its high affinity for fibrin and its thrombus-localized stimulation of plasminogen activator activity without the activation of systemic plasminogen or the degradation of plasma proteins (9,16,20).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Thrombolytic properties of an inactive proenzyme form of human urokinase secreted from human kidney cells.

Kasai

Arimura

Nishida

et al. 1985

Cell Struct. Funct.

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“…2) and the degradation of the fibrinogen in the plasma (Fig. 3) are caused by urokinase nonspecifically (5,25).…”

Section: Discussionmentioning

confidence: 94%

Section: Introductionmentioning

confidence: 99%

Thrombolytic properties of an inactive proenzyme form of human urokinase secreted from human kidney cells.

Kasai

Arimura

Nishida

et al. 1985

Cell Struct. Funct.

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“…Urokinase is a plasminogen activator isolated from human urine (1) and used in therapy as a physiological thrombolytic agent in deep-vein thromboses, coronary obstructions, etc. (2).…”

mentioning

confidence: 99%

Identification and primary sequence of an unspliced human urokinase poly(A)+ RNA.

Verde¹,

Stoppelli²,

Galeffi³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

209

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Human urokinase cDNA clones have been identified from a cDNA library prepared from total RNA of human fibroblasts transformed by simian virus 40 [Okayama, H. & Berg, P. (1983) Mol. Cell. Biol. 3,[280][281][282][283][284][285][286][287][288][289]. Synthetic oligonucleotides, corresponding to urokinase protein sequence, were used as probes. The cloned cDNA covers most of the coding sequence and the entire 3' untranslated region. The nucleotide sequence of one of the clones identifies this as a copy of a partially spliced polyadenylylated precursor to urokinase mRNA. The introns separate functionally different domains of the enzyme. Human urokinase mRNA has been identified by RNA blot and its size was estimated at 2500 nucleotides.Urokinase is a plasminogen activator isolated from human urine (1) and used in therapy as a physiological thrombolytic agent in deep-vein thromboses, coronary obstructions, etc. (2). Plasminogen activators convert the inactive zymogen plasminogen to the active serine protease, plasmin, thus initiating and finely controlling extracellular proteolysis (for review, see ref.3). Besides and beyond its interest as a therapeutic tool, urokinase appears to play an important role in tissue formation and degradation (3) and in the metastatic activity of human tumors (4). The level of urokinase mRNA appears to be controlled by a variety of physiological and experimental effectors, including hormones (5), neoplastic transformation (6, 7), growth factors (8, 9), and tumor promoters (10).Two different active forms of urinary urokinase have been isolated: a high-and a low-molecular-weight form (Mr, 54,000 and 33,000, respectively). High-molecular-weight urokinase is split by reduction into the A and B chains of Mr 20,000 and Mr 30,000, respectively (11). The low-molecularweight form is made up by the same B chain and by a 21 amino acid long Al chain (12). The A, Al, and B chains have been sequenced (11-13) and the Al chain has been shown to be the COOH terminus of the A chain. The sequence data suggest that the A chain is the NH2-and the B chain is the COOH-terminal portion of a single chain pro-urokinase precursor (12 Fig. 1) was synthesized according to a published technique (15) and was purified through a Partisyl Sax 25 x 0.8 cm HPLC column, with a linear gradient (1-300 mM) of potassium phosphate (pH 6.5) in 30% ethanol. Oligonucleotides 1, 2, and 4 (see Fig. 1) (22); 4 x 106 clones were obtained and screened by the high-density screening procedure (24). Duplicate filters (20,000-30,000 colonies each) were hybridized to 32P end-labeled oligonucleotides in 5x standard saline citrate (NaCl/Cit)/lOx Denhardt's solution/250 ,ug of E. coli transfer RNA carrier per ml/0.5% sodium dodecyl sulfate (lx NaCl/Cit = 0.15 M NaCl/0.015 M Na citrate; lx Denhardt's solution = 0.02% bovine serum albumin/0.02% Ficoll/0.02% polyvinylpyrrolidone) (25). Filters were incubated at 550C and the temperature was allowed to drop to 320C (oligonucleotides 1 and 2) or to 370C (oligonucleotides 3 and 4) in 2 hr. The hy...

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“…The adsorption of urokinase to non-siliconized glass as described by Toki and Sumi (1) is to be regarded as the cause of this phenomenon. A higher prolonged activity of urokinase could be achieved by stabilization with human albumin (3,4). But according to our data this stabilization is not likely to prevent absolutely the adsorption of urokinase to non-siliconized glass surfaces.…”

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confidence: 99%