| First Author | Hascakova-Bartova R | Year | 2004 |
| Journal | Biochem Biophys Res Commun | Volume | 323 |
| Issue | 3 | Pages | 920-5 |
| PubMed ID | 15381088 | Mgi Jnum | J:92854 |
| Mgi Id | MGI:3054613 | Doi | 10.1016/j.bbrc.2004.08.152 |
| Citation | Hascakova-Bartova R, et al. (2004) Identification and subcellular distribution of endogenous Ins(1,4,5)P(3) 3-kinase B in mouse tissues. Biochem Biophys Res Commun 323(3):920-5 |
| abstractText | Inositol 1,4,5-trisphosphate 3-kinase (IP(3)-3K) catalyses the phosphorylation of inositol 1,4,5-trisphosphate to inositol 1,3,4,5-tetrakisphosphate. cDNAs encoding three mammalian isoforms have been reported and referred to as IP(3)-3KA, IP(3)-3KB, and IP(3)-3KC. IP(3)-3KB is particularly sensitive to proteolysis at the N-terminus, a mechanism known to generate active fragments of lower molecular mass. Endogenous IP(3)-3KB has therefore not been formally identified in tissues. We have probed a series of murine tissues with an antibody directed against the C-terminus of IP(3)-3KB and used IP(3)-3KB deficient mouse tissues as negative controls. IP(3)-3KB was shown to be particularly well expressed in brain, lung, and thymus with molecular masses of 110-120kDa. The identification of the native IP(3)-3KB by Western blotting for the first time will facilitate further studies of regulation of its activity by specific proteases and/or phosphorylation. |
