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Cytoplasm calcium-binding proteins of germ cells and embryos of the sea urchin
Institution:1. Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China;2. Function Laboratory for Marine Fisheries Science and Food Production Processes, Qingdao National Laboratory for Marine Science and Technology, Qingdao 266200, China;3. Changdao Enhancement and Experiment Station, Chinese Academy of Fishery Sciences, Changdao, China;1. Centro de Investigación Científica y Educación Superior de Ensenada, Laboratorio de Genómica Marina, Carretera Ensenada-Tijuana, C.P. 22860 Ensenada, B. C., Mexico;2. Universidad Autónoma de Baja California, Facultad de Ciencias Marinas, Laboratorio de Patología Experimental Acuícola, Carretera Ensenada-Tijuana No. 3917, C.P. 22860 Ensenada, B. C., Mexico;3. Universidad Autónoma de Baja California, Instituto de Investigaciones Oceanológicas, Carretera Ensenada-Tijuana No. 3917, C.P. 22860 Ensenada, B. C., Mexico
Abstract:Synchronous, demonstrative, easily reproducible fertilization with the following embryonic development makes the process in the sea urchin extremely attractive for studying many biological enigmas. In particular, germ and embryonic cells of the sea urchin present a wide opportunity for investigating different associated phenomena launched by an increase in concentration of Ca2+ in cells (Ca2+]i).Ca2+ ions participate in the activation of diverse processes of respiration and sperm motility (Shapiro et al., 1990; Brokaw, 1991), chemotaxis of spermatozoa to components of the egg jelly (Ward et al., 1985), acrosomal reaction (Trimmer et al., 1986; Shapiro et al., 1990), cortical reaction, formation of the fertilization membrane (Sasaki, 1984; Sardet and Chang, 1987), cellular division in the embryo (Poenie et al., 1985; Silver, 1986; Whitaker and Patel, 1990), their adhesion (McClay and Matranga, 1986), differentiation and formation of spicules (Mitsunaga et al., 1988) and metamorphosis (Carpenter et al., 1984).The present review combines information on the function of calcium-binding proteins and their targets, calmodulin regulation of NAD-kinase, exocytosis of cortical granules, Ca2+- and calmodulin-dependent protein phosphatase, Ca2+-dependent protein phosphorylation, regulation of ion-exchanger in the germ and embryonic cells as well as Ca2+- and calmodulin control of sperm motility in sea urchins.
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