Title |
Signal transduction through the sphingomyelin pathway
|
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Published in |
Journal of Molecular Neuroscience, February 1994
|
DOI | 10.1007/bf02815356 |
Pubmed ID | |
Authors |
Richard Kolesnick |
Abstract |
The sphingomyelin pathway is a new signal transduction system initiated by hydrolysis of plasma membrane sphingomyelin to ceramide by the actin of a neutral sphingomyelinase. Ceramide serine/threonine protein kinase termed ceramide-activated protein kinase. This kinase belongs to a family of proline-directed protein kinases that recognize substrates containing the minimal motif, X-Thr/Ser-Pro-X, where the phosphoacceptor site is followed on the carboxyl terminus by a proline residue and X may be any amino acid. Three lines of evidence, rapid kinetics of activation of the sphingomyelin pathway by tumor necrosis factor (TNF) alpha, the ability of cell-permeable ceramide analogs to bypass receptor activation and mimic the effect of TNF alpha, and reconstitution of this cascade in a cell-free system, support the concept that the sphingomyelin pathway serves to signal TNF alpha-induced monocytic differentiation. Hence, the sphingomyelin pathway may represent a signaling system analogous to more well-defined systems such as the cyclic adenosine monophosphate and phosphoinositide pathways. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Germany | 2 | 6% |
Canada | 1 | 3% |
Unknown | 29 | 91% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 6 | 19% |
Student > Ph. D. Student | 6 | 19% |
Student > Doctoral Student | 5 | 16% |
Student > Bachelor | 5 | 16% |
Student > Master | 4 | 13% |
Other | 3 | 9% |
Unknown | 3 | 9% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 9 | 28% |
Biochemistry, Genetics and Molecular Biology | 8 | 25% |
Physics and Astronomy | 2 | 6% |
Chemistry | 2 | 6% |
Medicine and Dentistry | 2 | 6% |
Other | 4 | 13% |
Unknown | 5 | 16% |