Identification of normal human peripheral blood monocytes and liver as sites of synthesis of coagulation factor XIII a-chain.

Abstract:

:Factor XIII is the fibrin-stabilizing factor that covalently cross-links fibrin monomers to form a highly organized, stable fibrin clot. The plasma form of factor XIII is a heterodimer, a2b2, consisting of two a-chains and two b-chains; the intracellular form, such as in platelets and placenta, is a dimer, a2, consisting of a-chains only. The catalytic function of factor XIII, a transglutaminase, resides in the a-chain. To address questions regarding sites of synthesis of factor XIII a-chain, an EcoRI restriction fragment from the protein-coding region of the factor XIII a-chain cDNA was used as a probe for Northern blot analysis. The cDNA probe showed hybridization with a single approximately 4.0-kilobase (kb) message in poly (A)+ mRNA prepared from normal human peripheral blood monocytes and normal human liver. The results demonstrate conclusively that factor XIII a-chains are actively synthesized in circulating monocytes and in liver. To our knowledge, these data represent the first demonstration of synthesis of any blood coagulation factor in primary uncultured and unstimulated monocytes or macrophage cells.

journal_name

Blood

journal_title

Blood

authors

Weisberg LJ,Shiu DT,Conkling PR,Shuman MA

subject

Has Abstract

pub_date

1987-08-01 00:00:00

pages

579-82

issue

2

eissn

0006-4971

issn

1528-0020

journal_volume

70

pub_type

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