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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1990-12-6
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pubmed:abstractText |
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 endogenously phosphorylated. By using site-directed mutagenesis, an altered form of LACI was produced in which the serine-2 residue had been changed to alanine. This altered LACI, although expressed in similar quantity to the wild-type LACI, was not detectably phosphorylated. Using the altered LACI in functional studies demonstrated that a serine residue at position 2, and thus the phosphorylation of this site, was not essential for LACI's inhibition of Xa and VIIa-TF activities.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-115877,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-2424499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-2448300,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-2452157,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-271951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-2781520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-2827342,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-2927510,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-2987912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-3024756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-3031657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-3143429,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-3239755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-3422166,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-3474230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-3617011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-3657866,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-3873968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-5940945,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-6090457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-6196603,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-6225933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-6286303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-6293815,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-6316096,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-6795061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-6814825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-6937462,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-7354023,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-7380833,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2122883-925006
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
621-5
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:2122883-Blotting, Western,
pubmed-meshheading:2122883-Casein Kinases,
pubmed-meshheading:2122883-Factor VII,
pubmed-meshheading:2122883-Factor VIIa,
pubmed-meshheading:2122883-Factor Xa,
pubmed-meshheading:2122883-Humans,
pubmed-meshheading:2122883-Lipoproteins,
pubmed-meshheading:2122883-Phosphorylation,
pubmed-meshheading:2122883-Phosphoserine,
pubmed-meshheading:2122883-Protein Kinases,
pubmed-meshheading:2122883-Serine,
pubmed-meshheading:2122883-Structure-Activity Relationship,
pubmed-meshheading:2122883-Thromboplastin,
pubmed-meshheading:2122883-Tumor Cells, Cultured
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pubmed:year |
1990
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pubmed:articleTitle |
Endogenous phosphorylation of the lipoprotein-associated coagulation inhibitor at serine-2.
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pubmed:affiliation |
Division of Hematology/Oncology, Washington University School of Medicine, Jewish Hospital, St. Louis, MO 63110.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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