Characterization of <i>γ</i>- and <i>δ</i>-subunits of Ca2+/calmodulin-dependent protein kinase II in rat gastric mucosal cell populations

Mayer, Péter; Möhlig, Matthias; Seidler, Ursula; Rochlitz, H.; Fährmann, Michael; Schatz, H.; Hidaka, Hiroyoshi; Pfeiffer, Andreas F. H.

doi:10.1042/bj2970157

Cited by 19 publications

(15 citation statements)

References 36 publications

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“…Kinase was detected with an anti‐β‐CaM kinase II antibody (left panel), an anti‐γ antibody which crossreacts with β isoforms (middle) and an anti‐δ antibody (right). Note that δ D ‐CaM kinase II (also termed δ 4 ) is the only known δ isoform with a molecular mass significantly higher then δ B but lower than δ A thus facilitating its identification (Mayer et al ., 1993; Edman and Schulman, 1994). ( B ) Structure and peptide sequence of the novel β M ‐CaM kinase II.…”

Section: Resultsmentioning

confidence: 99%

“…In mammals, numerous alternative spliced isoforms are generated from the four closely related α, β, γ and δ CaM kinase II genes (Tobimatsu and Fujisawa, 1989; Karls et al ., 1992; Mayer et al ., 1993; Nghiem et al ., 1993; Edman and Schulman, 1994; Brocke et al ., 1995; Uriquidi and Ashcroft, 1995; Bayer et al ., 1996). These isoforms have distinct but overlapping spatial and temporal expression patterns (Tobimatsu and Fujisawa, 1989; Burgin et al ., 1990; Sakagami and Kondo, 1993), suggesting different specific functions.…”

Section: Introductionmentioning

confidence: 99%

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alpha KAP is an anchoring protein for a novel CaM kinase II isoform in skeletal muscle

1998

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Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) is present in a membrane-bound form that phosphorylates synapsin I on neuronal synaptic vesicles and the ryanodine receptor at skeletal muscle sarcoplasmic reticulum (SR), but it is unclear how this soluble enzyme is targeted to membranes. We demonstrate that alphaKAP, a non-kinase protein encoded by a gene within the gene of alpha-CaM kinase II, can target the CaM kinase II holoenzyme to the SR membrane. Our results indicate that alphaKAP (i) is anchored to the membrane via its N-terminal hydrophobic domain, (ii) can co-assemble with catalytically competent CaM kinase II isoforms and target them to the membrane regardless of their state of activation, and (iii) is co-localized and associated with rat skeletal muscle CaM kinase II in vivo. alphaKAP is therefore the first demonstrated anchoring protein for CaM kinase II. CaM kinase II assembled with alphaKAP retains normal enzymatic activity and the ability to become Ca2+-independent following autophosphorylation. A new variant of beta-CaM kinase II, termed betaM-CaM kinase II, is one of the predominant CaM kinase II isoforms associated with alphaKAP in skeletal muscle SR.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

alpha KAP is an anchoring protein for a novel CaM kinase II isoform in skeletal muscle

1998

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“…CaMK-II diversity in all species is achieved through alternative promoter and/or exon usage (Griffith and Greenspan, 1993;Mayer et al, 1993Mayer et al, , 1994Mayer et al, , 1995Schworer et al, 1993;Edman and Schulman, 1994;Ramirez et al, 1997;Tombes and Krystal, 1997;Bayer et al, 1998Bayer et al, , 1999Hoch et al, 1998Hoch et al, , 2000Takeuchi and Fujisawa, 1998;Donai et al, 2000b;Mima et al, 2001;Hudmon and Schulman, 2002a). As many as seven alternative variable domain exons are used in different combinations to yield over three dozen unique isozymes (Tombes and Krystal, 1997;Bayer et al, 1998;Takeuchi et al, 2000a).…”

Section: Introductionmentioning

confidence: 98%

Organization and evolution of multifunctional Ca2+/CaM-dependent protein kinase genes

Tombes

Faison

Turbeville

2003

Gene

198

192

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“…The key signalling protein kinase in cholinergic stimulation of H + secretion is CaMKII (Tsunoda et al ., 1992; Mayer et al ., 1994; Fährmann et al ., 1998; 1999; 2002; Fährmann & Pfeiffer, 1999; 2000). Carbachol‐stimulation causes a doubling of CaMKII activity (Figure 4a), as well as a strong increase of autoactivated CaMKII in the secretory apical membrane of rabbit gastric mucosal cells (Figure 4b).…”

Section: Resultsmentioning

confidence: 99%

Different actions of protein kinase C isoforms α and ε on gastric acid secretion

Fährmann

Kaufhold

Rieg

et al. 2002

British J Pharmacology

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1. The phorbol ester TPA, an activator of protein kinase C (PKC), inhibits cholinergic stimulation of gastric acid secretion but increases basal H(+) secretion. 2. Since these contradictory findings suggest the action of different PKC isozymes we analysed the role of calcium-dependent PKC-alpha, and calcium-independent PKC-epsilon in gastric acid secretion. 3. Inhibition of PKC-alpha by the indolocarbazole Gö 6976 revealed that about 28% of carbachol-induced acid secretion was inhibited by PKC-alpha. In the presence of Gö 6976 approximately 64% of the carbachol-induced signal transduction is mediated by Ca(2+)/calmodulin-dependent protein kinase II (CaMKII), and 14% is conveyed by PKC-epsilon as deduced from the inhibition with the bisindolylmaleimide Ro 31-8220. 4. Inhibition of carbachol-induced acid secretion by TPA was accompanied by a decrease in CaMKII activity. 5. The stimulation of basal acid secretion by TPA was biphasic with a peak at a very low concentration (10 pM), resulting in an activation of the calcium-sensor CaMKII. The activation was determined with a phosphospecific polyclonal antibody against active CaMKII. The TPA-induced increase of H(+) secretion was sensitive to the cell-permeable Ca(2+)-chelator BAPTA/AM, Ro 31-8220, and the CaMKII-inhibitor KN-62, but not to Gö 6976. 6. Since TPA induced the translocation of PKC-epsilon but not of PKC-alpha in resting parietal cells, PKC-epsilon seems to be at least responsible for an initial elevation of free intracellular calcium to initiate TPA-induced acid secretion. 7. Our data indicate the different roles of two PKC isoforms: PKC-epsilon activation appears to facilitate cholinergic stimulation of H(+)-secretion likely by increasing intracellular calcium. In contrast, PKC-alpha activation attenuates acid secretion accompanied by a down-regulation of CaMKII activity.

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Characterization of γ- and δ-subunits of Ca2+/calmodulin-dependent protein kinase II in rat gastric mucosal cell populations

Cited by 19 publications

References 36 publications

alpha KAP is an anchoring protein for a novel CaM kinase II isoform in skeletal muscle

alpha KAP is an anchoring protein for a novel CaM kinase II isoform in skeletal muscle

Organization and evolution of multifunctional Ca2+/CaM-dependent protein kinase genes

Different actions of protein kinase C isoforms α and ε on gastric acid secretion

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