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Biochemistry

R.G. Knowles, M. Palacios, R.M.J. Palmer, S. Moncada, "Formation of nitric oxide from L-arginine in the central nervous system: a transduction mechanism for stimulation of the soluble guanylate cyclase," Proceedings of the National Academy of Sciences, 86, 5159-62, July 1989. Richard Knowles (Wellcome Research Laboratories, Beckenham, Kent, U.K.): "We started our studies looking for the arginine:nitric oxide (NO) pathway in the brain because of the discovery that vascular endothelial cells syn

November 26, 1990

R.G. Knowles, M. Palacios, R.M.J. Palmer, S. Moncada, "Formation of nitric oxide from L-arginine in the central nervous system: a transduction mechanism for stimulation of the soluble guanylate cyclase," Proceedings of the National Academy of Sciences, 86, 5159-62, July 1989.

Richard Knowles (Wellcome Research Laboratories, Beckenham, Kent, U.K.): "We started our studies looking for the arginine:nitric oxide (NO) pathway in the brain because of the discovery that vascular endothelial cells synthesize NO from arginine. This finding suggested to us that the effects of arginine on crude brain guanylate cyclase, described by Takeo Deguchi [Tokyo Metropolitan University] and colleagues (Journal of Biological Chemistry, 252:7617-9, 1977; and 257:10147-51, 1982), were likely to be caused by NO formation. While we were completing these studies, a paper appeared by John Garthwaite [University of Liverpool] and colleagues (Nature, 336:385-8, 1988) on the production of an endothelium-derived relaxing factor (EDRF)(NO)-like material by cere- bellar cells stimulated with N-methyl-D-aspartate (NMDA). Important elements of both our and Garthwaite's findings were quickly confirmed, and the appearance of these papers in rapid succession has provided a convincing body of evidence for the hypothesis that Ca2+-stimulated NO formation con- stitutes a novel transduction mech- anism to the brain. This is important to many other researchers because it links research on brain function with the large and rapidly growing literature on NO synthesis and function in blood vessels, in activated macrophages, and, more recently, in several other cell types and tissues."

B. Margolis, S.G. Rhee, S. Felder, M. Mervic, et al., "EGF induces tyrosine phosphorylation of phospholipase C-II: a potential mechanism for EGF receptor signaling," Cell, 57, 1101-7, 30 June 1989.

Ben Margolis (New York University Medical Center, N.Y.): "When it was realized that many growth factor receptors had intrinsic tyrosine kinase activity, it was hypothesized that there must be substrates of these receptor kinases that are important in transducing the mitogenic signal. This paper reports the finding that one isozyme of phospholipase C, now called phospholipase Cg, was tyrosine phosphorylated in living cells after epidermal growth factor (EGF) treatment. This marked the first substrate of the EGF-receptor kinase that had a known physiological function. The finding also supported the concept that phosphorylation of substrates by growth factor receptors might be critical in mitogenic signaling.

"The work was widely quoted because it marked the coming together of two highly studied fields, namely, inositol phosphates and growth factor signaling. Our paper extended and complemented the work of Matthew Wahl and Graham Carpenter [Vanderbilt University, Nashville, Tenn.] (PNAS, 86:1568-72, 1989) and Jill Meisenhelder and Tony Hunter [Salk Institute] (Cell, 57:1109-22, 1989), and represented collaborations with the laboratory of Sue Goo Rhee [National Heart, Lung, and Blood Institute], where several phospho- lipase C isozymes were purified and cloned."


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