title: Sphingomyelinase increases 2-deoxyglucose uptake and glucose metabolism of human platelets.
abstract: Recent studies have shown that the sphingomyelinase (SMase) catalyzed hydrolysis of sphingomyelin (SM) represents an important cell signalling pathway. Control of SMase activity appears to be crucial for the regulation of multiple biological events in different cell systems; in particular, SMase activity appears to be involved in the control of vascular functions and in atherogenic events. Here we report that SMase treatment of human platelets significantly increases 2-deoxyglucose uptake by decreasing K(m) value of sugar transport and increasing sugar diffusion. In addition SMase treatment enhances basal glycolytic flux of platelets as well as the stimulation of the flux induced by suboptimal concentration of thrombin. The present study demonstrates that exposure of platelets to SMase, which may take place in vivo in physiological and/or in pathological conditions, modifies biochemical parameters of resting and stimulated platelets which are essential for cell physiological role.
authors.affiliation: Department of Biochemical Sciences, University of Firenze, Italy. biocell@scibio.unifi.it
authors.forename: V
authors.initials: V
authors.lastname: Vasta
authors.forename: E
authors.initials: E
authors.lastname: Meacci
authors.forename: E
authors.initials: E
authors.lastname: Romiti
authors.forename: M
authors.initials: M
authors.lastname: Farnararo
authors.forename: P
authors.initials: P
authors.lastname: Bruni
mesh_terms: D001692:Biological Transport; D001792:Blood Platelets / Q000187:drug effects / Q000378:metabolism*; D003847:Deoxyglucose / Q000097:blood*; D004058:Diffusion; D006019:Glycolysis; D006801:Humans; D007700:Kinetics; D019344:Lactic Acid / Q000097:blood; D013108:Sphingomyelin Phosphodiesterase / Q000378:metabolism*; D013917:Thrombin / Q000494:pharmacology
chemical_list: D019344:Lactic Acid; D003847:Deoxyglucose; D013108:Sphingomyelin Phosphodiesterase; D013917:Thrombin