PMID: 2122883Sep 15, 1990Paper

Endogenous phosphorylation of the lipoprotein-associated coagulation inhibitor at serine-2

The Biochemical Journal
T GirardG J Broze

Abstract

Lipoprotein-associated coagulation inhibitor (LACI) inhibits activated Factor X (Xa) directly and, in an Xa-dependent fashion, inhibits Factor VIIa-tissue factor (TF), presumably by forming a quaternary Xa-LACI-VIIa-TF complex. LACI isolated from the conditioned media of HepG2 cells grown in the presence of [32P]orthophosphate was observed to be covalently phosphorylated. Dephosphorylation of 32P-LACI with phosphatase resulted in an almost complete removal of the radiolabel. Phosphoamino acid analysis of the purified 32P-LACI established that the phosphorylation occurred on (a) serine residue(s). At its N-terminus, LACI contains a cluster of acidic residues C-terminal to the serine-2 residue. Such a site is characteristic of the sites phosphorylated by casein kinase II (CKII) in protein substrates. Edman degradation of endogenously labelled 32P-LACI revealed that the serine-2 residue was a major site of phosphorylation. Phosphorylation of purified LACI by bovine CKII was observed to occur in vitro; amino acid sequence analysis demonstrated that CKII phosphorylated LACI at the serine-2 residue. Recombinant LACI expressed from mouse C127 fibroblasts transfected using a bovine-papilloma-virus expression vector was found to be endo...Continue Reading

Citations

Nov 16, 2018·Blood Coagulation & Fibrinolysis : an International Journal in Haemostasis and Thrombosis·Saravanan SubramaniamCraig Fletcher
Jul 5, 2005·Expert Opinion on Investigational Drugs·B KaiserJ Fareed
Sep 12, 2018·Platelets·Emmanuel AmpofoMichael D Menger
Jun 17, 2000·Baillière's Best Practice & Research. Clinical Haematology·J H McVey
Mar 1, 1992·Trends in Cardiovascular Medicine·G J Broze
Sep 1, 1994·Baillière's Clinical Haematology·J H McVey

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