The Primary Structure of High Molecular Mass Urokinase from Human Urine. The Complete Amino Arid Sequence of the A Chain

Günzler, Wolfgang A.; Steffens, Gerd; Ötting, Fritz; Kim, Sung-Man A.; Frankus, E; Flohé, Leopold

doi:10.1515/bchm2.1982.363.2.1155

Cited by 334 publications

(129 citation statements)

References 14 publications

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“…Limited proteolysis of -~ plasminogen with pancreatic elastase results in cleavage of kringle 1 -3, K( 1 + 2 + 3), and kringle 4, K4, fragments from plasminogen. Such kringle structures, which are also present in prothrombin [2], urokinase [3], tissue plasminogen activator [4] and fibronectin [5], are supposed to be involved in binding of ligands essential for the regulation of the biological function of these proteins. Purified K( 1 + 2 + 3) cleaved from plasminogen by elastase has been found to bind to fibrin [6], the plasminogen-binding form of a2-plasmin inhibitor [7] and histidine-rich glycoprotein [8].…”

mentioning

confidence: 99%

Purification and characterization of a novel, oligomeric, plasminogen kringle 4 binding protein from human plasma: tetranectin

Clemmensen

Petersen

Kluft³

1986

Eur J Biochem

193

139

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Purification of a2-plasmin inhibitor (a2PI) from human plasma by affinity chromatography on plasminogenSepharose resulted in copurification of a contaminating protein with MI 17000 as judged by sodium dodecyl sulphate/polyacrylamide gel electrophoresis. This contaminating protein could not be removed from the purified a2-PI preparation by several types of gel chromatography applied. The use of the kringle 1 -3 part of plasminogen, K(l + 2 + 3), bound to Sepharose for affinity chromatography, instead of plasminogen-Sepharose, resulted in an u2PI preparation without this contaminant. The contaminating protein was found to interact specifically with the kringle 4 part of plasminogen (K4) and not with K(1+2+3) or miniplasminogen.The KCbinding protein was purified by ammonium sulphate precipitation, affinity chromatography on K4-Sepharose, ion-exchange chromatography and gel filtration on AcA 34.The relative molecular mass of the protein (Mr 68 000) was estimated by gel filtration. This suggests a tetrameric protein composed of four subunits (MI 17000), that are dissociated by 1 YO sodium dodecyl sulphate. Dissociation into subunits was also demonstrated by gel filtration in the presence of 6 M guanidine hydrochloride. A specific antibody was raised in rabbits against the purified protein and this antibody was shown not to react with any known fibrinolytic components. The pl of the K4-binding protein was found to be 5.8. The first three N-terminal amino acids were determined to be Glu-Pro-Pro. The concentration of the protein in plasma was estimated to be 0.20 f 0.03 pM (15 +_ 2 mg/l). The electrophoretic mobility of the KCbinding protein was shown by crossed immunoelectrophoresis to be influenced by the presence of Ca2+, EDTA and heparin. The protein was found to enhance plasminogen activation catalyzed by tissue-type plasminogen activator (t-PA) in the presence of poly(Dlysine). The protein appeared to be a novel plasma protein tentatively called 'tetranectin'.

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mentioning

confidence: 99%

Purification and characterization of a novel, oligomeric, plasminogen kringle 4 binding protein from human plasma: tetranectin

Clemmensen

Petersen

Kluft³

1986

Eur J Biochem

193

139

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“…The amino acid sequence of human prothrombin was referred to Waltz et al (29) and Butkowki et al (1)1, and that of bovine one was to SottrupJensen et al (22). The amino acid seqeunce of human urokinase was from Steffens et al (23) and Giinzler et al (8), and that deduced from the nucleotide sequence of human urokinase was from Heyneker et al (9) and Verde et al (28). The complete amino acid sequence of human tissue-type plasminogen activator deduced from the nucleotide sequence was the work of Pennica et al (21).…”

Section: Methodsmentioning

confidence: 99%

“…Sottrup-Jensen et al (22) demonstrated a higher level of amino acid sequence homology of kringles in human and bovine prothrombin as well as those in human plasminogen. The homology of urokinase A-chain with murine EGF, the fifth kringle structure of human plasminogen, and bovine factor X was shown by Giinzler et al (8). The nucleotide sequence of urokinase was determined by Heyneker et al (9), who also showed the existence of a complete kringle arrangement in the A-chain.…”

mentioning

confidence: 98%

Homology of kringle structures in urokinase and tissue-type plasminogen activator: The phylogeny with the related serine proteases.

Takahashi

Gojobori

Naora

1985

Cell Struct. Funct.

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ABSTRACT. Twelve amino acid sequences of kringle-forming polypeptides were compiled from the known sequences of urokinase A-chain (human), a tissue-type plasminogen activator (human), prothrombin (human and bovine), and plasminogen (human). Their sequence homologies with maximum match were examined by a computer program. A homology alignment and graphic matrix analyses did show that they had a great degree of homology. All the cystein residues responsible for the kringle structures of urokinase and the tissue-type plasminogen activator were confidently preserved as well as other proteins.

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“…No secondary cleavage sites were detected. By comparison with the known sequence of scu-PA [27,28], this new N-terminal sequence resulted from cleavage of Lys 158-Ile t59, which is the same peptide bond cleaved when plasmin activates scu-PA [2]. I00 200 300 400 500 600 700 Time (s) Fig.…”

Section: Cleavage Of Seu-pa By Egf-bp Occurs Between Lys 15~ and Lie 159mentioning

confidence: 99%

Epidermal growth factor‐binding protein activates soluble and receptor‐bound single chain urokinase‐type plasminogen activator

Wolf¹,

Brown²

1995

FEBS Letters

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The Primary Structure of High Molecular Mass Urokinase from Human Urine. The Complete Amino Arid Sequence of the A Chain

Cited by 334 publications

References 14 publications

Purification and characterization of a novel, oligomeric, plasminogen kringle 4 binding protein from human plasma: tetranectin

Purification and characterization of a novel, oligomeric, plasminogen kringle 4 binding protein from human plasma: tetranectin

Homology of kringle structures in urokinase and tissue-type plasminogen activator: The phylogeny with the related serine proteases.

Epidermal growth factor‐binding protein activates soluble and receptor‐bound single chain urokinase‐type plasminogen activator

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