A battery of monoclonal antibodies that induce unique conformations to evolve cryptic but constitutive functions of plasminogen.

A battery of monoclonal antibodies that induce unique conformations to evolve cryptic but constitutive functions of plasminogen. Research Abstract Details 

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A battery of monoclonal antibodies that induce unique conformations to evolve cryptic but constitutive functions of plasminogen. Abstract Text:

S Madoiwa,K Arai,Y Ueda,M Ishizuka,J Mimuro,S Asakura,M Matsuda,Y Sakata,

Two groups of anti-plasminogen monoclonal antibodies, whose epitope was either in the kringle 1 + 2 + 3 domain (F3P2, F11P5, F11P6, and F12P18) or the kringle 5 domain (F1P6 and F12P16), were isolated and their effects on the conformation of plasminogen were explored. All antibodies except F1P6 had 3- to 10-fold higher affinity toward Lys-plasminogen than Glu-plasminogen. F1P6 exhibited a comparable affinity to Glu- and Lys-plasminogen. Among these, only F11P5 binding was inhibited by epsilon-amino-nu-caproic acid (EACA) in a concentration-dependent manner, with half maximal inhibition at 3 mM. From a competition assay, we concluded that the epitopes of F11P5, F11P6, and F12P18 should be very close, and located at or near the low affinity lysine binding site on the kringle 2 + 3. These three antibodies dramatically enhanced the binding of Glu-plasminogen to the other antibodies, except to F1P6. Interestingly, F3P2, whose non-overlapping epitope was in the kringle 2 + 3 domain, also augmented the binding of Glu-plasminogen to the other antibodies. In contrast, we did not observe enhanced binding of Lys-plasminogen to one antibody in the presence of the other antibodies, and the binding of Glu-plasminogen to these antibodies did not increase in the presence of 10 mM EACA. In the presence of these antibodies, including F1P6, Glu-plasminogen bound more efficiently to immobilized degraded fibrin, with a binding profile similar to Lys-plasminogen. All antibodies except F1P6 enhanced the conversion rate of plasminogen to plasmin remarkably. Taken together, we propose that these two groups of monoclonal antibodies can dissociate the intramolecular interactions of Glu-plasminogen and induce the conformational transition of Glu-plasminogen to Lys-plasminogen. In addition, the kringle 2 + 3 and kringle 5 structures of Glu-plasminogen liganded with EACA are distinct from the Lys-plasminogen structure.

A battery of monoclonal antibodies that induce unique conformations to evolve cryptic but constitutive functions of plasminogen. Publishing Authors By Initials

S Madoiwa,K Arai,Y Ueda,M Ishizuka,J Mimuro,S Asakura,M Matsuda,Y Sakata,

For similar enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: urinary plasminogen activator research abstracts see: enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: urinary plasminogen activator research

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A battery of monoclonal antibodies that induce unique conformations to evolve cryptic but constitutive functions of plasminogen. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 121

Page Numbers: 278-87

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Feb

YEAR: 1997

A battery of monoclonal antibodies that induce unique conformations to evolve cryptic but constitutive functions of plasminogen. Information

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LANGUAGE: eng

NlmUniqueID: 376600

A battery of monoclonal antibodies that induce unique conformations to evolve cryptic but constitutive functions of plasminogen. Keywords Mesh Terms:

KEYWORDS: Urinary Plasminogen Activator

MESH TERMS: metabolism

Chemical & Substance for Abstract: A battery of monoclonal antibodies that induce unique conformations to evolve cryptic but constitutive functions of plasminogen. Information

Substance Name: Urinary Plasminogen Activator

Registry Number: EC 3.4.21.73

Grant and Affiliation Information for A battery of monoclonal antibodies that induce unique conformations to evolve cryptic but constitutive functions of plasminogen.

AFFILIATION: Division of Hemostasis and Thrombosis, Jichi Medical School, Tochigi.

Country: JAPAN

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MEDLINETA: J Biochem

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