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Title: Free sphingosine in control and stimulated human neutrophils

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6150476

Exogenous long-chain (sphingoid) bases are potent inhibitors of protein kinase C in vitro and the oxidative burst of human neutrophils. To assess their involvement in neutrophil function, high-performance liquid chromatography was used to quantitate free long-chain bases in neutrophils incubated with and without N-formyl-methionyl-leucyl-phenylalanine (fMLP) and phorbol 12-myristate 13-acetate (PMA). Sphingosine was present in freshly isolated neutrophils at 6.1 +/- 1.1 pmol/10W cells. During incubation at 37, the level increased several fold; further increases were obtained with fMLP whereas PMA decreased free sphingosine. This sphingosine was apparently derived from hydrolysis of complex sphingolipids. Since endogenous levels are comparable to those of diacylglycerols in neutrophils and, hence, within the range expected to affect the activity of protein kinase C, long-chain bases may serve a role in modulating neutrophil functions related to the action of this enzyme.

Research Organization:
Emory Univ., Atlanta, GA
OSTI ID:
6150476
Report Number(s):
CONF-870644-
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 46:6; Conference: 78. annual meeting of the American Society of Biological Chemists conference, Philadelphia, PA, USA, 7 Jun 1987
Country of Publication:
United States
Language:
English