TY - JOUR
T1 - Tissue and subcellular distributions of an inhibitory GDP GTP exchange protein (GDI) for smg p25A by use of its antibody
AU - Nonaka, Hidetaro
AU - Kaibuchi, Kozo
AU - Shimizu, Kazuya
AU - Yamamoto, Juro
AU - Takai, Yoshimi
N1 - Funding Information:
1 This investigation was supported by grants-in-aid Scientific Research and Cancer Research from the Ministry Education, Science, and Culture, Japan (1990), a grant-in-aid for Abnormalities in Hormone Receptor Mechanisms from the Ministry Of Health and Welfare, Japan (19901, and by grants from the Yamanouchi Foundation for Research on Metabolic Disease (1990), and the Research Program on Cell Calcium Signal in the Cardiovascular System (1990). 2To whom correspondence should The abbreviations used are: tein: GDI. GDP dissociation inhibitor; sulfate-polyacrylamide electrophoresis; saline; BSA, bovine albumin.
PY - 1991/1/31
Y1 - 1991/1/31
N2 - We have recently purified from bovine brain cytosol to near homogeneity a GDP GTP exchange protein for smg p25A, named smg p25A GDI, that inhibits the dissociation of GDP from and the subsequent binding of GTP to smg p25A. In the present study, we made an antiserum against smg p25A GDI and studied its tissue distribution in rat and its subcellular distribution in rat cerebrum by use of this antiserum. smg p25A GDI was found in secretory cells with both regulated and constitutive secretion types. Since smg p25A was previously found in only secretory cells with a regulated secretion type, this result suggests that small GTP-binding proteins different from smg p25A but recognized by smg p25A GDI are present in secretory cells with a constitutive secretion type, and that smg p25A GDI is involved in both regulated and constitutive secretory processes. In subcellular fractionation analysis of rat cerebrum, smg p25A GDI was mostly found in the cytosol fraction of neuron body and synaptosome. In synaptosome, it was mainly found in the synaptic cytosol.
AB - We have recently purified from bovine brain cytosol to near homogeneity a GDP GTP exchange protein for smg p25A, named smg p25A GDI, that inhibits the dissociation of GDP from and the subsequent binding of GTP to smg p25A. In the present study, we made an antiserum against smg p25A GDI and studied its tissue distribution in rat and its subcellular distribution in rat cerebrum by use of this antiserum. smg p25A GDI was found in secretory cells with both regulated and constitutive secretion types. Since smg p25A was previously found in only secretory cells with a regulated secretion type, this result suggests that small GTP-binding proteins different from smg p25A but recognized by smg p25A GDI are present in secretory cells with a constitutive secretion type, and that smg p25A GDI is involved in both regulated and constitutive secretory processes. In subcellular fractionation analysis of rat cerebrum, smg p25A GDI was mostly found in the cytosol fraction of neuron body and synaptosome. In synaptosome, it was mainly found in the synaptic cytosol.
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U2 - 10.1016/0006-291X(91)91453-J
DO - 10.1016/0006-291X(91)91453-J
M3 - Article
C2 - 1899568
AN - SCOPUS:0025972058
SN - 0006-291X
VL - 174
SP - 556
EP - 563
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -