caa a22 4500 397557280 CHVBK 20180308164806.0 cr unu---uuuuu 161202e199607 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021395 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021395 Interaction of Ganglioside with Specific Peptide Sequences as a Mechanism for the Modulation of Calmodulin-Dependent Enzymes [Elektronische Daten] [Hideyoshi Higashi, Sachiyo Yoshida, Kazuki Sato, Tatsuya Yamagata] We examined the interaction between gangliosides and synthetic peptides of calmodulin (CaM)-dependent enzymes to confirm the hypothesis that interaction between gangliosides and the CaM-like site (CLS) of the enzyme is a mechanism for the modulation of the enzyme activity by gangliosides. Gangliosides, GD1b, GT1b, and GD1a, inhibited the activity of CaM-independently activated cAMP-phosphodiesterase and their inhibition was cancelled by a peptide consisting of 17 amino acid residues of a plasma membrane Ca2+-pump CLS, suggesting the involvement of the interaction between the peptide and the gangliosides. The peptide of an assumed CLS of phosphodiesterase also cancelled the inhibition. On the other hand, the gangliosides interacted with synthetic CaM-binding site (CBS) peptides of phosphodiesterase, calcineurin, Ca2+-pump, and Ca2+/calmodulin-dependent protein kinase II. Moreover, gangliosides GM3 and LM1, that activate but do not inhibit phosphodiesterase, interacted with the CBS peptides, whereas they did not bind to CLS peptides. On the basis of these new findings, we propose a revised model for the ganglioside-mediated modulation of CaM-dependent enzymes, i.e. without CaM, gangliosides bind to CBS and thus stimulate the enzyme activity, acting like CaM. At higher concentrations, they bind to CLS of the enzymes as well and inhibit the activity, acting like the CBS of the enzyme. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence calcineurin nationallicence calcium pump nationallicence calmodulin nationallicence ganglioside nationallicence phosphodiesterase nationallicence Higashi Hideyoshi Mitsubishi Kasei Institute of Life Sciences 11 Minamiooya, Machida, Tokyo 194 aut Yoshida Sachiyo Mitsubishi Kasei Institute of Life Sciences 11 Minamiooya, Machida, Tokyo 194 aut Sato Kazuki Mitsubishi Kasei Institute of Life Sciences 11 Minamiooya, Machida, Tokyo 194 aut Yamagata Tatsuya Department of Biomolecular Engineering, Tokyo Institute of Technology 4259 Nagatsuta, Midori-ku, Yokohama 227 aut The Journal of Biochemistry Oxford University Press 120/1(1996-07), 66-73 0021-924X 120:1<66 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021395 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021395 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Higashi Hideyoshi Mitsubishi Kasei Institute of Life Sciences 11 Minamiooya, Machida, Tokyo 194 aut NATIONALLICENCE 700 1- Yoshida Sachiyo Mitsubishi Kasei Institute of Life Sciences 11 Minamiooya, Machida, Tokyo 194 aut NATIONALLICENCE 700 1- Sato Kazuki Mitsubishi Kasei Institute of Life Sciences 11 Minamiooya, Machida, Tokyo 194 aut NATIONALLICENCE 700 1- Yamagata Tatsuya Department of Biomolecular Engineering, Tokyo Institute of Technology 4259 Nagatsuta, Midori-ku, Yokohama 227 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/1(1996-07), 66-73 0021-924X 120:1<66 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford