TY - JOUR
T1 - Ca2+/calmodulin independent inositol 1,4,5-trisphosphate 3-kinase activity in guinea pig peritoneal macrophages
AU - Kimura, Yuichi
AU - Watanabe, Yutaka
AU - Ozaki, Shoichiro
AU - Koga, Toshitaka
AU - Hirata, Masato
N1 - Funding Information:
Acknowledgements--This work was supported by Uehara Memorial Foundation and Grants-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan. We thank M. Ohara for helpful comments and K. Higuchi for secretarial services.
PY - 1990
Y1 - 1990
N2 - 1. 1. The Ca2+/calmodulin (CaM) independent activity of inositol 1,4,5-trisphosphate (InsP3) 3-kinase in macrophages could be separated from the dependent activity by serial column chromatography, gel filtration, Orange A and DEAE-5PW. 2. 2. An InsP3 analog which has an aminobenzoyl group on the 2nd carbon of the inositol ring inhibited the conversion of [3H]InsP3 to [3H]InsP4 (inositol 1,3,4,5-tetrakisphosphate) in a dose-dependent manner. The concentration required for half-maximal inhibition (IC50) with the Ca2+/CaM independent enzyme activity was also dependent on the free Ca2+ concentration, as with the dependent activity. 3. 3. These results suggest that a conformational change in the enzyme occurs in response to a change in free Ca2+ concentration, and thus the potency to recognize the InsP3 analog would change, even when the Ca2+ CaM independent enzyme activity was used.
AB - 1. 1. The Ca2+/calmodulin (CaM) independent activity of inositol 1,4,5-trisphosphate (InsP3) 3-kinase in macrophages could be separated from the dependent activity by serial column chromatography, gel filtration, Orange A and DEAE-5PW. 2. 2. An InsP3 analog which has an aminobenzoyl group on the 2nd carbon of the inositol ring inhibited the conversion of [3H]InsP3 to [3H]InsP4 (inositol 1,3,4,5-tetrakisphosphate) in a dose-dependent manner. The concentration required for half-maximal inhibition (IC50) with the Ca2+/CaM independent enzyme activity was also dependent on the free Ca2+ concentration, as with the dependent activity. 3. 3. These results suggest that a conformational change in the enzyme occurs in response to a change in free Ca2+ concentration, and thus the potency to recognize the InsP3 analog would change, even when the Ca2+ CaM independent enzyme activity was used.
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U2 - 10.1016/0305-0491(90)90154-L
DO - 10.1016/0305-0491(90)90154-L
M3 - Article
C2 - 1962745
AN - SCOPUS:0025226059
SN - 0305-0491
VL - 97
SP - 527
EP - 533
JO - Comparative Biochemistry and Physiology -- Part B: Biochemistry and
JF - Comparative Biochemistry and Physiology -- Part B: Biochemistry and
IS - 3
ER -