The effects of activators of G-proteins,mastoparan and compound 48/80, on the G-protein/adenylate cyclase system in cultured melanophores of the black-moor goldfish,Carassius auratus |
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Authors: | F. Morishita A. Shimada Y. Takeda M. Fujimoto H. Katayama K. Yamada |
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Affiliation: | (1) Department of Biological Science, Faculty of Science, Hiroshima University, Kagamiyama, Higashi-Hiroshima 724, Japan, JP;(2) Mukaishima Biological Laboratory, Faculty of Science, Hiroshima University, Mukaishima, Mitsugi-gun, 722, Japan, JP |
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Abstract: | To investigate the functions of GTP-binding protein(s) in the melanosome-aggregating response in fish melanophores, the effects of activators of G-proteins, namely, mastoparan and compound 48/80, were examined in cultured melanophores of the balck-moor goldfish, Carassius auratus. Both mastoparan and compound 48/80 induced an approximately 40% increase in the GTP-hydrolyzing activity in the melanophore membranes compared to the basal level. In intact melanophores, these compounds inhibited the effect of 3-isobutyl-1-methylxanthine, which induced the accumulation of intracellular cAMP. Pretreatment of melanophores with pertussis toxin at 1 μg ⋅ ml-1 for 15 h attenuated the inhibitory effect of mastoparan on the accumulation of cAMP. However, pretreatment with the toxin only slightly attenuated the inhibitory effect of compound 48/80 on the accumulation of cAMP. In addition, compound 48/80 at 1 mg ⋅ ml-1 induced full aggregation of the melanosomes in melanophores, though mastoparan at 5 μmol ⋅ l-1 induced only 10–20% aggregation of melanophores. These results suggest that mastoparan and compound 48/80 can each activate the inhibitory G-protein in goldfish melanophores, which results in inhibition of adenylate cyclase activity. This signal-transduction pathway is involved in the aggregation of melanosomes in these cells. Accepted: 3 June 1996 |
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Keywords: | Melanophore Mastoparan Compound 48/80 GTP-binding protein Goldfish Carassius auratus |
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