caa a22 4500 397558120 CHVBK 20180308164809.0 cr unu---uuuuu 161202e199610 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021466 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021466 Ca2+ Signaling and Intracellular Ca2+ Binding Proteins [Elektronische Daten] [Ichiro Niki, Hisayuki Yokokura, Toshiki Sudo, Masumi Kato, Hiroyoshi Hidaka] Changes in cytosolic Ca2+ concentrations evoke a wide range of cellular responses and intracellular Ca2+-binding proteins are the key molecules to transduce Ca2+ signaling via enzymatic reactions or modulation of protein/protein interations (Fig. 1). The EF hand proteins, like calmodulin and S100 proteins, are considered to exert Ca2+-dependent actions in the nucleus or the cytoplasm. The Ca2+/phospholipid binding proteins are classified into two groups, the annexins and the C2 region proteins. These proteins, distributed mainly in the cytoplasm, translocate to the plasma membrane in response to an increase in cytosolic Ca2+ and function in the vicinity of the membrane. Ca2+ storage proteins in the endoplasmic or sarcoplasmic reticulum provide the high Ca2+ capacity of the Ca2+ store sites, which regulate intracellular Ca2+ distribution. The variety and complexity of Ca2+ signaling result from the cooperative actions of specific Ca2+-binding proteins. This review describes biochemical properties of intracellular Ca2+-binding proteins and their proposed roles in mediating Ca2+ signaling. © 1996 BY THE JOURNAL OF BIOCHEMISTRY JB Review nationallicence annexins nationallicence C2 region proteins nationallicence Ca2+ storage proteins nationallicence Ca2+ signaling nationallicence EF-hand proteins nationallicence Niki Ichiro Department of Pharmacology, Nagoya University School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466 aut Yokokura Hisayuki Department of Pharmacology, Nagoya University School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466 aut Sudo Toshiki Department of Pharmacology, Nagoya University School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466 aut Kato Masumi Department of Pharmacology, Nagoya University School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466 aut Hidaka Hiroyoshi Department of Pharmacology, Nagoya University School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466 aut The Journal of Biochemistry Oxford University Press 120/4(1996-10), 685-698 0021-924X 120:4<685 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021466 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021466 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Niki Ichiro Department of Pharmacology, Nagoya University School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466 aut NATIONALLICENCE 700 1- Yokokura Hisayuki Department of Pharmacology, Nagoya University School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466 aut NATIONALLICENCE 700 1- Sudo Toshiki Department of Pharmacology, Nagoya University School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466 aut NATIONALLICENCE 700 1- Kato Masumi Department of Pharmacology, Nagoya University School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466 aut NATIONALLICENCE 700 1- Hidaka Hiroyoshi Department of Pharmacology, Nagoya University School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/4(1996-10), 685-698 0021-924X 120:4<685 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