Electron microscopic localization of type I protein kinase C in rat Purkinje cells

Kose, Akiko; Saito, Naoaki; Itô, Hiroshi; Kikkawa, Ushio; Nishizuka, Yasutomi; Tanaka, Chikako

doi:10.1523/jneurosci.08-11-04262.1988

Cited by 115 publications

(50 citation statements)

References 16 publications

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“…Among various tissues, the enzyme is most concentrated in the CNS (Minakuchi et al,198 1). Immunocytochemical and biochemical studies in this and other laboratories have revealed a differential regional and cellular localization of each PKC subspecies in the brain (Kitano et al, 1987;Hidaka et al, 1988;Huang et al, 1988;Kose et al, 1988;Saito et al, 1988Saito et al, , 1989Hosoda et al, 1989;Ito et al, 1990). Particularly, the r-PKC subspecies is found only in the CNS (Ohno et al, 1987).…”

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confidence: 68%

Differential localization of four subspecies of protein kinase C in the rat striatum and substantia nigra

et al. 1991

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The distribution of protein kinase C (PKC) subspecies and their colocalization with neurotransmitters were examined in the rat striatum and substantia nigra (SN), using immunocytochemistry. The alpha- and beta I-PKC immunoreactivies were seen predominantly in the perikarya of the neurons in the striatum and SN. In contrast, the beta II- and gamma- PKC immunoreactivities were abundant in both the perikarya and the neuropils in the striatum and only in the neuropils in the SN. From electron microscopic studies, the alpha- and beta I-PKC immunoreactivities were seen adjacent to the plasma membrane, while the beta II-PKC immunoreactivity was observed in the cytoplasm around the Golgi complex. The gamma-PKC immunoreaction was dense throughout the cytoplasm. The double-staining and lesion studies revealed that the alpha-PKC-immunopositive neurons in the striatum were intrinsic cholinergic neurons, and that most of the alpha-PKC-immunoreactive neurons in the SN were dopaminergic neurons. The beta I-PKC- immunoreactive neurons were intrinsic GABAergic neurons in the striatum. Moreover, most of the beta II- and gamma-PKC-immunoreactive neurons were medium-sized neurons projecting to the SN, and over 90% of GABAergic neurons in the caudate-putamen contained beta II-PKC. The beta II-PKC-immunoreactive neurons showed no gamma-PKC immunoreactivity, and the gamma-PKC-immunoreactive neurons were not beta II-PKC immunoreactive. These findings suggest that alpha-PKC is related to the function of the nigral dopaminergic and the striatal cholinergic neurons, and that the beta I-PKC is involved in the function of the striatal intrinsic GABAergic neurons. The beta II- and gamma-PKC may also modulate a specific neuronal function in the striatonigral system.

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confidence: 68%

Differential localization of four subspecies of protein kinase C in the rat striatum and substantia nigra

et al. 1991

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“…It has been shown that both PKC␥ and DGK␥ are abundantly expressed in Purkinje cells (12,30) and possess not only cysteine-rich regions but also calcium-sensitive domains (2). These findings suggest a functional correlation between this DG-dependent kinase and DG-catalyzing kinase.…”

Section: Discussionmentioning

confidence: 90%

Subtype-specific Translocation of Diacylglycerol Kinase α and γ and Its Correlation with Protein Kinase C

Shirai¹,

Segawa²,

Kuriyama³

et al. 2000

Journal of Biological Chemistry

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We examined the translocation of diacylglycerol kinase (DGK) ␣ and ␥ fused with green fluorescent protein in living Chinese hamster ovary K1 cells (CHO-K1) and investigated temporal and spatial correlations between DGK and protein kinase C (PKC) when both kinases are overexpressed. DGK␣ and ␥ were present throughout the cytoplasm of CHO-K1 cells. Tetradecanoylphorbol 13-acetate (TPA) induced irreversible translocation of DGK␥, but not DGK␣, from the cytoplasm to the plasma membrane. The (TPA)-induced translocation of DGK␥ was inhibited by the mutation of C1A but not C1B domain of DGK␥ and was not inhibited by staurosporine. Arachidonic acid induced reversible translocation of DGK␥ from the cytoplasm to the plasma membrane, whereas DGK␣ showed irreversible translocation to the plasma membrane and the Golgi network. Purinergic stimulation induced reversible translocation of both DGK␥ and ␣ to the plasma membrane. The timing of the ATP-induced translocation of DGK␥ roughly coincided with that of PKC␥ re-translocation from the membrane to the cytoplasm. Furthermore, re-translocation of PKC␥ was obviously hastened by co-expression with DGK␥ and was blocked by an inhibitor of DGK (R59022). These results indicate that DGK shows subtype-specific translocation depending on extracellular signals and suggest that PKC and DGK are orchestrated temporally and spatially in the signal transduction. Diacylglycerol (DG)1 is a second messenger regulating various cellular responses (1, 2). One of the important roles of DG is the activation of protein kinase C (PKC) (1, 3, 4). Thus, DG is very important for regulation of PKC activity and cellular response. DG is produced physiologically as a result of the signal-induced hydrolysis of phosphatidylinositol by phospholipase C and also from phosphatidylcholine by phospholipase D. Generated DG is phosphorylated to phosphatidic acid by diacylglycerol kinase (DGK) or cleavage by DG lipase (2, 5, 6). DGK is an important enzyme for inactivating PKC by attenuation of the DG level, contributing to regulation of the cellular response. In addition, phosphatidic acid itself activates PKC and PLC␥1 (7, 8) and modulates Ras GTPase-activating protein (9). DGKs have additional important functions for various cellular responses.To date at least nine subtypes of mammalian DGKs have been cloned and divided into five groups based on structure (2). Generally, all DGKs have cysteine-rich regions homologous to the C1A and C1B motifs of PKCs in the regulatory domain at the N terminus of the protein and possess a conserved catalytic domain in the C terminus of the protein. Type I DGKs, including DGK␣, -␤, and -␥, have EF-hand motifs and two cysteinerich regions in the regulatory domain (10 -12). Type II DGKs such as DGK␦ and -, have a pleckstrin homology domain instead of the EF-hand motif in addition to two cysteine-rich regions (13,14). Interestingly, the catalytic domains of DGK␦ and -are separated. Type III, consisting of DGK⑀, has only two cysteine-rich regions in the regulatory domain. Type IV, DGK and ...

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“…DAG also functions as an activator for PKC. Like DAGL␣, PKC␥ is particularly abundant in Purkinje cells and activated downstream to the mGluR1 cascade (Kose et al, 1988;Nishizuka, 1992). The major mGluR1 signaling cascade in Purkinje cells, i.e., mGluR1-G␣q/11-PLC␤4 -PKC␥, is crucial for climbing fiber synapse elimination and motor coordination (Kano et al, 1995(Kano et al, , 1998Offermanns et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

Localization of Diacylglycerol Lipase-α around Postsynaptic Spine Suggests Close Proximity between Production Site of an Endocannabinoid, 2-Arachidonoyl-glycerol, and Presynaptic Cannabinoid CB1 Receptor

Yoshida

Fukaya²,

Uchigashima³

et al. 2006

J. Neurosci.

311

294

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2-Arachidonoyl-glycerol (2-AG) is an endocannabinoid that is released from postsynaptic neurons, acts retrogradely on presynaptic cannabinoid receptor CB1, and induces short-and long-term suppression of transmitter release. To understand the mechanisms of the 2-AG-mediated retrograde modulation, we investigated subcellular localization of a major 2-AG biosynthetic enzyme, diacylglycerol lipase-␣ (DAGL␣), by using immunofluorescence and immunoelectron microscopy in the mouse brain. In the cerebellum, DAGL␣ was predominantly expressed in Purkinje cells. DAGL␣ was detected on the dendritic surface and occasionally on the somatic surface, with a distal-to-proximal gradient from spiny branchlets toward somata. DAGL␣ was highly concentrated at the base of spine neck and also accumulated with much lower density on somatodendritic membrane around the spine neck. However, DAGL␣ was excluded from the main body of spine neck and head. In hippocampal pyramidal cells, DAGL␣ was also accumulated in spines. In contrast to the distribution in Purkinje cells, DAGL␣ was distributed in the spine head, neck, or both, whereas somatodendritic membrane was labeled very weakly. These results indicate that DAGL␣ is essentially targeted to postsynaptic spines in cerebellar and hippocampal neurons, but its fine distribution within and around spines is differently regulated between the two neurons. The preferential spine targeting should enable efficient 2-AG production on excitatory synaptic activity and its swift retrograde modulation onto nearby presynaptic terminals expressing CB1. Furthermore, different fine localization within and around spines suggests that the distance between postsynaptic 2-AG production site and presynaptic CB1 is differentially controlled depending on neuron types.

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Electron microscopic localization of type I protein kinase C in rat Purkinje cells

Cited by 115 publications

References 16 publications

Differential localization of four subspecies of protein kinase C in the rat striatum and substantia nigra

Differential localization of four subspecies of protein kinase C in the rat striatum and substantia nigra

Subtype-specific Translocation of Diacylglycerol Kinase α and γ and Its Correlation with Protein Kinase C

Localization of Diacylglycerol Lipase-α around Postsynaptic Spine Suggests Close Proximity between Production Site of an Endocannabinoid, 2-Arachidonoyl-glycerol, and Presynaptic Cannabinoid CB1 Receptor

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