Blood coagulation factor Xa interacts with a linear sequence of the kringle 2 domain of prothrombin.

Blood coagulation factor Xa interacts with a linear sequence of the kringle 2 domain of prothrombin. Research Abstract Details 

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Blood coagulation factor Xa interacts with a linear sequence of the kringle 2 domain of prothrombin. Abstract Text:

H Taneda,K Andoh,J Nishioka,H Takeya,K Suzuki,

Prothrombin is a vitamin K-dependent plasma protein composed of several functional domains, which is proteolytically activated into thrombin by factor Xa in the presence of factor Va, Ca2+, and phospholipids. During the activation, prothrombin is cleaved into three fragments: fragment 1, containing a domain rich in gamma-carboxyglutamic acid residues and kringle 1 domain; fragment 2, containing the kringle 2 domain; and a protease catalytic domain, thrombin. Here we studied the interaction site for factor Xa in human prothrombin during the activation. The isolated fragment 2 inhibited the activation of prothrombin by either prothrombinase complex or factor Xa alone in a dose-dependent manner, whereas fragment 1 and diisopropylphosphate (DIP)-thrombin did not. Factor Xa directly bound to fragment 2 immobilized to microwell plates with a Kd of 9.0 x 10(-8) M, but not to fragment 1 or DIP-thrombin. Factor Xa also bound to immobilized prothrombin and prethrombin 1 with Kds of 2.0 x 10(-7) and 1.5 x 10(-7) M, respectively, suggesting that factor Xa interacts with the kringle 2 domain in these molecules. The binding of factor Xa to immobilized fragment 2 was Ca(2+)-dependent with an optimal concentration at 6 mM. In the presence of Ca2+, the interaction was enhanced by phospholipids in a concentration-dependent manner. To localize the factor Xa-binding site in the kringle 2 domain, fragment 2 was digested with lysyl endopeptidase and then trypsin after reduction and S-carboxymethylation. The resulting peptides were immobilized to microwell plates and assayed for factor Xa binding ability. The amino acid sequence of the peptide positive in the assay was determined to be residues His205 to Arg220. Factor Xa bound to a synthetic peptide corresponding to the residues His205 to Arg220 immobilized to microwell plates. The peptide inhibited factor Xa-catalyzed activation of prothrombin, but a peptide with the reversed sequence of His205 to Arg220 did not. These findings indicate that factor Xa interacts with at least a linear sequence, His205 to Arg220, in the kringle 2 domain of prothrombin during its activation into thrombin.

Blood coagulation factor Xa interacts with a linear sequence of the kringle 2 domain of prothrombin. Publishing Authors By Initials

H Taneda,K Andoh,J Nishioka,H Takeya,K Suzuki,

For similar enzymes and coenzymes: enzyme precursors: prothrombin research abstracts see: enzymes and coenzymes: enzyme precursors: prothrombin research

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Blood coagulation factor Xa interacts with a linear sequence of the kringle 2 domain of prothrombin. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 116

Page Numbers: 589-97

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Sep

YEAR: 1994

Blood coagulation factor Xa interacts with a linear sequence of the kringle 2 domain of prothrombin. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Blood coagulation factor Xa interacts with a linear sequence of the kringle 2 domain of prothrombin. Keywords Mesh Terms:

KEYWORDS: Prothrombin

MESH TERMS: metabolism

Chemical & Substance for Abstract: Blood coagulation factor Xa interacts with a linear sequence of the kringle 2 domain of prothrombin. Information

Substance Name: Factor Xa

Registry Number: EC 3.4.21.6

Grant and Affiliation Information for Blood coagulation factor Xa interacts with a linear sequence of the kringle 2 domain of prothrombin.

AFFILIATION: Department of Molecular Biology on Genetic Disease, Mie University School of Medicine.

Country: JAPAN

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MEDLINETA: J Biochem

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