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Protein tyrosine kinase activation is required for LPS and PMA induction of tissue factor mRNA in human blood monocytes.
Thromb Haemost. 1995 Mar; 73(3):413-20.TH

Abstract

Tissue factor (TF) is a transmembrane glycoprotein which assembles with factor VIIa on cell surfaces to form a proteolytically active cofactor-enzyme complex; the TF/VIIa complex initiates the coagulation protease cascade. In response to bacterial lipopolysaccharide (LPS) and phorbol-12 myristate 13-acetate (PMA), monocytes synthesize and express TF on their surface. However, the mechanisms by which LPS and PMA activate TF synthesis by human blood monocytes are not fully understood. As it has been established that LPS and PMA activate protein tyrosine kinase (PTK) in monocytes, we studied the role of PTK in LPS and PMA induction of TF by human blood monocytes. Both LPS- and PMA-induced TF activity was inhibited in a concentration-dependent manner by the protein tyrosine kinase-specific inhibitors herbimycin A and genistein. TF antigen determination confirmed that LPS- and PMA-induced cell surface TF protein levels decreased in parallel to TF functional activity under herbimycin A and genistein treatment. Northern blot analysis of total RNA from LPS- and PMA-stimulated monocytes showed a concentration-dependent decrease in TF mRNA levels in response to herbimycin A and genistein. The rate of decay of LPS-induced TF mRNA, evaluated after the arrest of transcription by actinomycin D was not affected by genistein and herbimycin A, suggesting that the inhibitory effects occur at least partly at the transcriptional level. We conclude that LPS- and PMA-induced TF production by human monocytes is dependent on tyrosine kinase activation.

Authors+Show Affiliations

Service of Hematology and Immunology, CHU Xavier Bichat, Paris, France.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

7545319

Citation

Ternisien, C, et al. "Protein Tyrosine Kinase Activation Is Required for LPS and PMA Induction of Tissue Factor mRNA in Human Blood Monocytes." Thrombosis and Haemostasis, vol. 73, no. 3, 1995, pp. 413-20.
Ternisien C, Ollivier V, Khechai F, et al. Protein tyrosine kinase activation is required for LPS and PMA induction of tissue factor mRNA in human blood monocytes. Thromb Haemost. 1995;73(3):413-20.
Ternisien, C., Ollivier, V., Khechai, F., Ramani, M., Hakim, J., & de Prost, D. (1995). Protein tyrosine kinase activation is required for LPS and PMA induction of tissue factor mRNA in human blood monocytes. Thrombosis and Haemostasis, 73(3), 413-20.
Ternisien C, et al. Protein Tyrosine Kinase Activation Is Required for LPS and PMA Induction of Tissue Factor mRNA in Human Blood Monocytes. Thromb Haemost. 1995;73(3):413-20. PubMed PMID: 7545319.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Protein tyrosine kinase activation is required for LPS and PMA induction of tissue factor mRNA in human blood monocytes. AU - Ternisien,C, AU - Ollivier,V, AU - Khechai,F, AU - Ramani,M, AU - Hakim,J, AU - de Prost,D, PY - 1995/3/1/pubmed PY - 1995/3/1/medline PY - 1995/3/1/entrez SP - 413 EP - 20 JF - Thrombosis and haemostasis JO - Thromb Haemost VL - 73 IS - 3 N2 - Tissue factor (TF) is a transmembrane glycoprotein which assembles with factor VIIa on cell surfaces to form a proteolytically active cofactor-enzyme complex; the TF/VIIa complex initiates the coagulation protease cascade. In response to bacterial lipopolysaccharide (LPS) and phorbol-12 myristate 13-acetate (PMA), monocytes synthesize and express TF on their surface. However, the mechanisms by which LPS and PMA activate TF synthesis by human blood monocytes are not fully understood. As it has been established that LPS and PMA activate protein tyrosine kinase (PTK) in monocytes, we studied the role of PTK in LPS and PMA induction of TF by human blood monocytes. Both LPS- and PMA-induced TF activity was inhibited in a concentration-dependent manner by the protein tyrosine kinase-specific inhibitors herbimycin A and genistein. TF antigen determination confirmed that LPS- and PMA-induced cell surface TF protein levels decreased in parallel to TF functional activity under herbimycin A and genistein treatment. Northern blot analysis of total RNA from LPS- and PMA-stimulated monocytes showed a concentration-dependent decrease in TF mRNA levels in response to herbimycin A and genistein. The rate of decay of LPS-induced TF mRNA, evaluated after the arrest of transcription by actinomycin D was not affected by genistein and herbimycin A, suggesting that the inhibitory effects occur at least partly at the transcriptional level. We conclude that LPS- and PMA-induced TF production by human monocytes is dependent on tyrosine kinase activation. SN - 0340-6245 UR - https://www.unboundmedicine.com/medline/citation/7545319/Protein_tyrosine_kinase_activation_is_required_for_LPS_and_PMA_induction_of_tissue_factor_mRNA_in_human_blood_monocytes_ DB - PRIME DP - Unbound Medicine ER -