Abstract
Binding activity of [3H]inositol 1,3,4,5-tetrakisphosphate (InsP4) was characterized with rat cerebellar membranes. Two types of InsP4 analog with either the aminobenzoyl or the aminocyclohexanecarbonyl group on the 2nd position of InsP4 have been synthesized and their effects on the binding activity were also examined. [3H]InsP4 binding was gradually displaced by increasing amounts of unlabeled InsP4, with an IC50 of 60-170 nM, depending on the pH values. The binding was sharply increased at acidic pH and millimolar concentrations of Ca2+, this being in clear contrast with [3H]InsP3 binding noted in the same species of tissue. Heparin inhibited the binding, with an IC50 of 1.7, 3 or 20 μg/ml at pH 8.3, 7.2 or 5.0, respectively. Adenine nucleotide inhibited the binding more potently than did [3H]InsP3 binding. InsP4 analogs were as effective as InsP4 in displacing [3H]InsP4 from rat cerebellar membranes, thereby indicating that the 2nd hydroxl group may not be involved in recognition of InsP4 by its binding sites.
| Original language | English |
|---|---|
| Pages (from-to) | 218-222 |
| Number of pages | 5 |
| Journal | BBA - Biomembranes |
| Volume | 1069 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Nov 4 1991 |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Cell Biology
Cite this
Synthetic inositol 1,3,4,5-tetrakisphosphate analogs and their effect on the binding to microsomal fraction of rat cerebellum. / Kimura, Yuichi; Kanematsu, Takashi; Watanabe, Yutaka; Ozaki, Shoichiro; Koga, Toshitaka; Hirata, Masato.
In: BBA - Biomembranes, Vol. 1069, No. 2, 04.11.1991, p. 218-222.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Synthetic inositol 1,3,4,5-tetrakisphosphate analogs and their effect on the binding to microsomal fraction of rat cerebellum
AU - Kimura, Yuichi
AU - Kanematsu, Takashi
AU - Watanabe, Yutaka
AU - Ozaki, Shoichiro
AU - Koga, Toshitaka
AU - Hirata, Masato
PY - 1991/11/4
Y1 - 1991/11/4
N2 - Binding activity of [3H]inositol 1,3,4,5-tetrakisphosphate (InsP4) was characterized with rat cerebellar membranes. Two types of InsP4 analog with either the aminobenzoyl or the aminocyclohexanecarbonyl group on the 2nd position of InsP4 have been synthesized and their effects on the binding activity were also examined. [3H]InsP4 binding was gradually displaced by increasing amounts of unlabeled InsP4, with an IC50 of 60-170 nM, depending on the pH values. The binding was sharply increased at acidic pH and millimolar concentrations of Ca2+, this being in clear contrast with [3H]InsP3 binding noted in the same species of tissue. Heparin inhibited the binding, with an IC50 of 1.7, 3 or 20 μg/ml at pH 8.3, 7.2 or 5.0, respectively. Adenine nucleotide inhibited the binding more potently than did [3H]InsP3 binding. InsP4 analogs were as effective as InsP4 in displacing [3H]InsP4 from rat cerebellar membranes, thereby indicating that the 2nd hydroxl group may not be involved in recognition of InsP4 by its binding sites.
AB - Binding activity of [3H]inositol 1,3,4,5-tetrakisphosphate (InsP4) was characterized with rat cerebellar membranes. Two types of InsP4 analog with either the aminobenzoyl or the aminocyclohexanecarbonyl group on the 2nd position of InsP4 have been synthesized and their effects on the binding activity were also examined. [3H]InsP4 binding was gradually displaced by increasing amounts of unlabeled InsP4, with an IC50 of 60-170 nM, depending on the pH values. The binding was sharply increased at acidic pH and millimolar concentrations of Ca2+, this being in clear contrast with [3H]InsP3 binding noted in the same species of tissue. Heparin inhibited the binding, with an IC50 of 1.7, 3 or 20 μg/ml at pH 8.3, 7.2 or 5.0, respectively. Adenine nucleotide inhibited the binding more potently than did [3H]InsP3 binding. InsP4 analogs were as effective as InsP4 in displacing [3H]InsP4 from rat cerebellar membranes, thereby indicating that the 2nd hydroxl group may not be involved in recognition of InsP4 by its binding sites.
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UR - http://www.scopus.com/inward/citedby.url?scp=0025993927&partnerID=8YFLogxK
U2 - 10.1016/0005-2736(91)90127-T
DO - 10.1016/0005-2736(91)90127-T
M3 - Article
C2 - 1657168
AN - SCOPUS:0025993927
VL - 1069
SP - 218
EP - 222
JO - Biochimica et Biophysica Acta - Biomembranes
JF - Biochimica et Biophysica Acta - Biomembranes
SN - 0005-2736
IS - 2
ER -