Ca2+/Calmodulin-sensitive inositol 1,4,5-trisphosphate 3-kinase in rat and bovine brain tissues

Takazawa, Kazunaga; Passareiro, Heloísa; Dumont, Jacques Emile; Erneux, Christophé

doi:10.1016/s0006-291x(88)81142-2

Cited by 50 publications

(46 citation statements)

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“…In contrast, previous studies all suggested InsP 3 3-kinase A to be cytosolic. InsP 3 3-kinase A was initially purified from rat brain cytosolic fraction as a 50 -53-kDa protein (6,34,35,58,59). Antibodies to purified InsP 3 3-kinase recognized a 50 -53-kDa protein band in a soluble fraction of rat brain homogenates.…”

Section: Effect Of a Submaximal Atp Concentration On The [Ca 2ϩ ] I -mentioning

confidence: 99%

“…In rat AR4 -2J pancreatoma cells, InsP 3 3-kinase activity could only be seen in high speed supernatants of cellular homogenates, and these cells may actually overexpress InsP 3 5-phosphatase activity as compared with non-tumoral acinar cells (31). Finally, InsP 3 3-kinase activity is modulated by the Ca 2ϩ -calmodulin complex; the extent of this modulation varies between the various isoenzymes in different cell types (32)(33)(34)(35)(36)(37).…”

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confidence: 99%

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Isoprenylated Human Brain Type I Inositol 1,4,5-Trisphosphate 5-Phosphatase Controls Ca2+ Oscillations Induced by ATP in Chinese Hamster Ovary Cells

Smedt¹,

Missiaen²,

Parys³

et al. 1997

Journal of Biological Chemistry

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. In mouse exocrine pancreatic acinar cells, InsP 4 is effective in mobilizing Ca 2ϩ and promoting Ca 2ϩ influx in conditions where phospholipase A 2 activity, and thus arachidonic acid production, is inhibited (10). Recently, a high affinity InsP 4 -binding protein has been purified from pig platelets (11). The cDNA encoding this putative receptor encoded a GTPase-activating protein. In vitro, it shows GTPase-activating protein activity against Ras that is inhibited by phospholipids and specifically stimulated by InsP 4 (12).Both the InsP 3 3-kinase and the 5-phosphatase consist of a family of multiple isoenzymes. In particular, the various 5-phosphatases dephosphorylate InsP 3 , InsP 4 , phosphatidylinositol 4,5-bisphosphate, and phosphatidylinositol 3,4,5-trisphosphate with different specificities, K m , and V max (13)(14)(15). In vitro, type I InsP 3 5-phosphatase (also designated as the 43-kDa 5-phosphatase) can use either InsP 3 or InsP 4 as substrates but not the phosphoinositides (16 -20). Based upon kinetic analysis (K m for InsP 3 and V max values compared with other 5-phosphatases), this enzyme is generally considered as a signal-terminating enzyme for InsP 3 , analogous to the cyclic nucleotide phosphodiesterases for cyclic AMP (21).The type I 5-phosphatase has a higher affinity but lower

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Section: Effect Of a Submaximal Atp Concentration On The [Ca 2ϩ ] I -mentioning

confidence: 99%

mentioning

confidence: 99%

Isoprenylated Human Brain Type I Inositol 1,4,5-Trisphosphate 5-Phosphatase Controls Ca2+ Oscillations Induced by ATP in Chinese Hamster Ovary Cells

Smedt¹,

Missiaen²,

Parys³

et al. 1997

Journal of Biological Chemistry

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“…[3H]Ins(1,3,4)P3, the product of [3H]Ins(l,3,4,5)P4 5-phosphatase [15] was separated on 0.6-ml Dowex columns [16]. The specificity of dephosphorylation has been checked using a mixture of In~ (1,4,5)[5-~~P]P~ and [3H]Ins(1,4,5)P3 as substrate.…”

Section: Assay Ofmentioning

confidence: 99%

Soluble and particulate Ins(1,4,5)P₃/Ins(1,3,4,5)P₄ 5‐phosphatase in bovine brain

Erneux

Lemos

Verjans

et al. 1989

European Journal of Biochemistry

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Ins(1 ,4,5)P3 5-phosphatase catalyses the dephosphorylation of Ins(1,4,5)P3 in the 5 position. At 1 pM Ins(1,4,5)P3, 10-15% of total activity of a bovine brain homogenate was measured in the soluble fraction, whereas 85 -90% was in the particulate fraction. Particulate activity could be solubilized by cholate or, to a lower extent, by 2 M KCI. Two soluble enzymes (type I and type 11) could be fractionated by DEAE-Sephacel chromatography. Soluble activities have been further purified by blue-Sepharose, Sephacryl S-200 and phosphocellulose chromatography. Specific activities reached 10-30 pmol . min-' mg protein-' for type I and were 10-20 times lower for type 11. Type I and type 11 Ins(1,4,5)P3 5-phosphatase displayed different K,,, values and molecular masses, as estimated by gel filtration. Type I dephosphorylated both Ins(1,4,5)P3 and Ins(1 ,3,4,5)P4; in contrast, type I1 specifically dephosphorylated Ins(1 ,4,5)P3 but not Ins(1,3,4,5)P4. Type 1 lns(1,4,5)P3 5-phosphatase eluted as a single peak of activity with an apparent molecular mass of 51 kDa when gel filtration was performed in the presence of cholate. This molecular mass is identical to the molecular mass estimated for the particulate Ins(1 ,4,5)P3 5-phosphatase that was solubilized by cholate. K , values for Ins(1,4,5)P3 and Ins(1 ,3,4,5)P4 obtained with type I Ins(1,4,5)P3 5-phosphatase were 11 pM and 1 pM, respectively. Similar values were obtained with particulate Ins(1 ,4,5)P3 5-phosphatase. In conclusion, the catalytic domains of type I and particulate Ins(1 ,4,5)P3 5-phosphatase activity may be very similar, if not identical, but different from type I1 phosphatase.Agonist-stimulated hydrolysis of phosphatidylinositol 4,s-bisphosphate produces two signal molecules, Ins(1 ,4,5)P3 and diacylglycerol. Ins( 1 ,4,5)P3, a second messenger for mobilizing intracellular calcium [l, 21, has been shown to be metabolized to Ins(1,4)P2 or phosphorylated to Ins(1,3,4,5)P4 [3]. These reactions are catalyzed by an Ins(1,4,5)P3 5-phosphomonoesterase or phosphatase and an Ins(1 ,4,5)P3 3-kinase, respectively. These two enzymes represent potential control points at which both Ins(1 ,4,5)P3 and Ins(1,3,4,5)P4 concentrations could be regulated.Ins(1,4,5)P3 5-phosphatase was originally described in human erythrocyte membranes, where its activity is M g Z fdependent and inhibited by 2,3-bisphosphoglycerate [4]. The product of dephosphorylation is Ins(1 ,4)P2. The same enzyme specifically removes the 5 phosphate from Ins( 1,3,4,5)P4 to form lns(1,3,4)P3, the most abundant InsP3 isomer in many cells [S]. The Ins(1,4,5)P3 5-phosphatase is found in the soluble fractions of most tissues, although the membrane-bound activity is often quantitatively more important 16-91. A single enzyme form was purified from the soluble fraction of human platelets by the group of Majerus [lo]. Its apparent molecular mass was 38 kDa as determined by gel filtration. Both Ins(1,4,5)P3 and Ins(1,3,4,5)P4 appeared to be substrates for the platelet Ins(1 ,4,5)P3 5-phosphatase [I I]. In platelets, ...

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“…In human brain, at least two isozymes, referred to as Ins(1,4,5)P3 3-kinase A and Ins(1,4,5)P3 3-kinase B, have been isolated (Takazawa et al, 1991 b). The complex formed by Caz+ and calmodulin appears to be the activator of native and recombinant Ins(1,4,5)P3 3-kinase (Biden et al, 1987 1987; Ryu et al, 1987;Yamaguchi et al, 1988;Takazawa et al, 1988Takazawa et al, , 1990a. As calmodulin often recognizes basic amphiphilic a-helices (O'Neil and De Grado, 1990), amino acids stretching from Ser156 to Leu189 of rat brain 3-kinase may contain the calmodulin-binding domain (Takazawa and Emeux, 1991a).…”

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Interaction of calmodulin with a putative calmodulin‐binding domain of inositol 1,4,5‐triphosphate 3‐kinase.

Erneux

Moreau

Vandermeers

et al. 1993

European Journal of Biochemistry

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Recombinant rat brain inositol 1,4,5‐triphosphate [Ins(1,4,5)P3] 3‐kinase was expressed in Escherichia coli as a β‐galactosidase fusion product. It could be adsorbed onto calmodulin‐Sepharose and eluted in Ca2+‐free medium as a 48‐kDa protein. Purification could be achieved in a single step. Molecular evidence for a calmodulin‐binding domain on Ins(1,4,5)P3 3‐kinase can be shown by the following approaches. (a) Inhibition of Ca2+/calmodulin stimulation by a synthetic peptide based on a candidate calmodulin‐binding domain. The inhibition was mimicked by a well‐characterized peptide derived from the sequence of smooth muscle myosin light‐chain kinase calmodulin‐binding site. (b) The construction of two mutants by site‐directed mutagenesis of Trp165 to Gly or Arg. Both mutants displayed kinase activity but were no longer Ca2+/calmodulin sensitive, supporting, therefore, the role of Trp165 in calmodulin binding.

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Ca2+/Calmodulin-sensitive inositol 1,4,5-trisphosphate 3-kinase in rat and bovine brain tissues

Cited by 50 publications

References 23 publications

Isoprenylated Human Brain Type I Inositol 1,4,5-Trisphosphate 5-Phosphatase Controls Ca2+ Oscillations Induced by ATP in Chinese Hamster Ovary Cells

Isoprenylated Human Brain Type I Inositol 1,4,5-Trisphosphate 5-Phosphatase Controls Ca2+ Oscillations Induced by ATP in Chinese Hamster Ovary Cells

Soluble and particulate Ins(1,4,5)P₃/Ins(1,3,4,5)P₄ 5‐phosphatase in bovine brain

Interaction of calmodulin with a putative calmodulin‐binding domain of inositol 1,4,5‐triphosphate 3‐kinase.

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Ca2+/Calmodulin-sensitive inositol 1,4,5-trisphosphate 3-kinase in rat and bovine brain tissues

Cited by 50 publications

References 23 publications

Isoprenylated Human Brain Type I Inositol 1,4,5-Trisphosphate 5-Phosphatase Controls Ca2+ Oscillations Induced by ATP in Chinese Hamster Ovary Cells

Isoprenylated Human Brain Type I Inositol 1,4,5-Trisphosphate 5-Phosphatase Controls Ca2+ Oscillations Induced by ATP in Chinese Hamster Ovary Cells

Soluble and particulate Ins(1,4,5)P3/Ins(1,3,4,5)P4 5‐phosphatase in bovine brain

Interaction of calmodulin with a putative calmodulin‐binding domain of inositol 1,4,5‐triphosphate 3‐kinase.

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Soluble and particulate Ins(1,4,5)P₃/Ins(1,3,4,5)P₄ 5‐phosphatase in bovine brain