Detail of "205368-58-7"

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Identification of novel target proteins of cyclic GMP signaling pathways using chemical proteomics

Identification of novel target proteins of cyclic GMP signaling pathways using chemical proteomics. Kim, Euikyung; Park, Ji Man (Department of Life Science, Division of Molecular and Life Science, Pohang University of Science and Technology, Kyungbuk 790-784, S. Korea). Journal of Biochemistry and Molecular Biology, 36(3), 299-304 (English) 2003 Biochemical Society of the Republic of Korea. 205368-58-7 and 9023-47-6 are also occured in this study. CODEN: JBMBE5. ISSN: 1225-8687. DOCUMENT TYPE: Journal CA Section: 9 (Biochemical Methods) Section cross-reference(s): 13 For deciphering the cyclic guanosine monophosphate (cGMP) signaling pathway, we employed chem. proteomics to identify the novel target mols. of cGMP. We used cGMP that was immobilized onto agarose beads with linkers directed at three different positions of cGMP. We performed a pull-down assay using the beads as baits on tissue lysates and identified 9 proteins by MALDI-TOF (Matrix-Assisted Laser Desorption/Ionization Time-of-Flight) mass spectrometry. Some of the identified proteins were previously known cGMP targets, including cGMP-dependent protein kinase and cGMP-stimulated phosphodiesterase. Surprisingly, some of the co-pptd. proteins were never formerly reported to assoc. with the cGMP signaling pathway. The competition binding assays showed that the interactions are not by nonspecific binding to either the linker or bead itself, but by specific binding to cGMP. Furthermore, we obsd. that the interactions are highly specific to cGMP against other nucleotides, such as cyclic adenosine monophosphate (cAMP) and 5'-GMP, which are structurally similar to cGMP. As one of the identified targets, MAPK1 was confirmed by immunoblotting with an anti-MAPK1 antibody. For further proof, we obsd. that the membrane-permeable cGMP (8-bromo cyclic GMP) stimulated mitogen-activated protein kinase 1 signaling in the treated cells. Our present study suggests that chem. proteomics can be a very useful and powerful technique for identifying the target proteins of small bioactive mols. .