Ask about this productRelated genes to: GK3P antibody
- Gene:
- GK3P NIH gene
- Name:
- glycerol kinase 3 pseudogene
- Previous symbol:
- GKP3
- Synonyms:
- GKTB
- Chromosome:
- 4q32.3
- Locus Type:
- pseudogene
- Date approved:
- 1994-12-14
- Date modifiied:
- 2016-10-05
Related products to: GK3P antibody
Related articles to: GK3P antibody
- To address mechanisms for the differential sensitivity of voltage-gated Ca2+ channels (Cav) to agonists, channel activity was compared in Xenopus oocytes coexpressing muscarinic M(1) receptors and different Cav alpha1 subunits, all with beta1B,alpha2/delta subunits. Acetyl-beta-methylcholine (MCh) decreased Cav 1.2c currents, did not affect 2.1 or 2.2 currents, but potentiated Cav 2.3 currents. Phorbol 12-myristate 13-acetate (PMA) did not affect Cav 1.2c or 2.1 currents but potentiated 2.2 and 2.3 currents. Comparison of the amino acid sequences of the alpha1 subunits revealed a set of potential protein kinase C phosphorylation sites in common between the 2.2 and 2.3 channels that respond to PMA and a set of potential sites unique to the alpha1 2.3 subunits that respond to MCh. Quadruple Ser --> Ala mutation of the predicted MCh sites in the alpha1 2.3 subunit (Ser-888, Ser-892, and Ser-894 in the II-III linker and Ser-1987 in the C terminus) caused loss of the MCh response but not the PMA response. Triple Ser --> Ala mutation of just the II-III linker sites gave similar results. Ser-888 or Ser-892 was sufficient for the MCh responsiveness, whereas Ser-894 required the presence of Ser-1987. Ser --> Asp substitution of Ser-888, Ser-892, Ser-1987, and Ser-892/Ser-1987 increased the basal current and decreased the MCh response but did not alter the PMA response. These results reveal that sites unique to the II-III linker of alpha1 2.3 subunits mediate the responsiveness of Cav 2.3 channels to MCh. Because Cav 2.3 channels contribute to action potential-induced Ca2+ influx, these sites may account for M1 receptor-mediated regulation of neurotransmission at some synapses. - Source: PubMed
Publication date: 2003/11/18
Kamatchi Ganesan LFranke RuthieLynch CarlSando Julianne J - Protein kinase C (PKC)-dependent regulation of voltage-gated Ca (Ca(v); with alpha(1)beta1Balpha2/delta subunits) channel 2.3 was investigated using phorbol 12-myristate 13-acetate (PMA), or by M(1) muscarinic receptor activation in Xenopus oocytes. The inward Ca(2+)-current with Ba(2+) (I(Ba)) as the charge carrier was potentiated by PMA or acetyl-beta-methylcholine (MCh). The inactivating [I(inact)] and non-inactivating [I(noninact)] components of I(Ba) and the time constant of inactivation tau(inact) were all increased by MCh or PMA. This may be a PKC-dependent action since the effect of MCh and PMA was blocked by Ro-31-8425 or beta-pseudosubstrate. MCh effect was blocked by atropine, guanosine-5'-O-(2-thiodiphosphate) trilithium (GDPbetaS) or U-73122. The effect of MCh but not PMA was blocked by the inhibition of inositol-1,4,5-trisphosphate (IP3) receptors, intracellular Ca(2+) ([Ca(2+)](i)) or the translocation of conventional PKC (cPKC) with heparin, BAPTA and betaC2.4, respectively. While a lower concentration (25 nM) of Ro-31-8425 blocked MCh, a higher concentration (500 nM) of Ro-31-8425 was required to block PMA action. This differential susceptibility of MCh and PMA to heparin, BAPTA, betaC2.4 or Ro-31-8425 is suggestive of the involvement of Ca(2+)-dependent cPKC in MCh action, whereas cPKC and Ca(2+)-independent novel PKC (nPKC) in PMA action. PMA led to additional increase in I(Ba) that was already potentiated by preadministered MCh (1 or 10 microM), leading to the suggestion that differential phosphorylation sites for cPKC and nPKC may be present in the alpha(1)2.3 subunit of Ca(v) 2.3 channels. - Source: PubMed
Kamatchi Ganesan LTiwari Shveta NChan Carrie KChen DaguangDo Sang-HwanDurieux Marcel ELynch Carl - Since volatile anesthetics inhibited high voltage-gated calcium channels and G-protein-coupled M(1) muscarinic signaling, their effects upon M(1) receptor-induced modulation of L-type (alpha1C) calcium channel was investigated. Voltage-clamped Ba(2+) currents (I(Ba)) were measured in Xenopus oocytes coexpressed with L-type channels and M(1) muscarinic receptors. M(1) receptor agonist, acetyl-beta-methylcholine (MCh) inhibited the peak and late components of I(Ba) in a dose-dependent manner. Analysis of I(Ba) after the treatment with MCh or volatile anesthetics revealed that the inactivating component, its time constant, and the noninactivating current were all decreased by these agents. MCh-induced inhibition followed a second messenger pathway that included G-proteins, phospholipase C, inositol-1,4,5-trisphosphate, and intracellular calcium [Ca(2+)](i). Although halothane or isoflurane inhibited I(Ba,) their effect was not mediated through these intracellular second messengers. By using volatile anesthetics and MCh sequentially, and in various combinations, the susceptibility of L-type currents and their modulation by M(1) receptors to volatile anesthetics were investigated. When MCh and volatile anesthetics were administered together simultaneously, a pronounced inhibition that was approximately equal to the sum of their individual effects was seen. Halothane or isoflurane further inhibited the I(Ba) when either volatile anesthetic was administered following the inhibition produced by prior administration of MCh. However, when MCh was administered following either volatile anesthetic, its effect was significantly reduced. Thus, whereas volatile anesthetics appear to directly inhibit L-type channels, they also interfere with channel modulation by G-protein-coupled receptors, which may have functional implications for both neuronal and cardiovascular tissues. - Source: PubMed
Kamatchi G LDurieux M ELynch C - The effect of the volatile anesthetics (VAs) halothane (0.59 mM) and isoflurane (0.70 mM) on protein kinase C (PKC)-mediated modulation of alpha1E type of high-voltage-gated Ca(2+) channels was examined in Xenopus oocytes coexpressing m1 muscarinic acetylcholine receptors. Phorbol-12-myristate-13-acetate (PMA) or 1, 2-dioctanoyl-sn-glycerol (DOG) was used to activate PKC directly, whereas indirect activation was induced with acetyl-beta-methylcholine (MCh). The interaction between PKC activators and VAs was examined by perfusing either VA before, during, or after the administration of PMA, DOG, or MCh. In addition, the effect of VAs was studied after the down-regulation of PKC. The application of VAs inhibited Ba(2+) current (I(Ba)), whereas PMA (500 nM), DOG (100 microM), or MCh (1 and 10 microM) markedly potentiated I(Ba). VAs inhibited PMA- or DOG-enhanced I(Ba) to the same extent as seen in controls. The inhibition of I(Ba) induced by VAs was not reversed by PMA or DOG. The administration of VAs in combination with PMA, DOG, or MCh (1 microM) led to the inhibition of I(Ba). MCh (10 microM) counteracted the inhibitory effect of VAs when administered together and reversed the inhibition of I(Ba) produced by VAs. These differences in the responses between PMA and MCh (10 microM) may be based on the involvement of various pools of PKC. It is suggested that VAs act directly at the membrane, because they blocked the membrane-based action of PMA, whereas the receptor-based action of MCh was only partially blocked. It is possible that some PKC isoforms may not be a direct target of VAs. - Source: PubMed
Kamatchi G LTiwari S NDurieux M ELynch C