Three distinct forms of rat brain protein kinase C: Differential response to unsaturated fatty acids

Sekiguchi, Koichi; Tsukuda, Masanori; Ogita, Kouji; Kikkawa, Ushio; Nishizuka, Yasutomi

doi:10.1016/0006-291x(87)91035-7

Cited by 236 publications

(84 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Rabbit thymus also contained some subspecies of PKC which did not seem to be identical with type II or type III PKC. In the extract of human granulocytes a dominant type III fraction was shown, in good agreement with the data available [16]. The isoenzyme profile obtained from pig granulocytes was in principle similar ( fig.2C).…”

supporting

confidence: 88%

“…In the brain three major types of protein kinase C isoenzymes have been resolved by hydroxyapatite chromatography [10][11][12] and the correspondence of type I, II and III isoenzymes to the cDNA clones designated 7, 13x+/~ II and a, respectively, has been determined [13]. Protein kinase C isoenzymes are differentially distributed in various tissues [6,9,11,14,15] and the subspecies show a slightly different mode of activation, kinetic properties and substrate specificities [9,12,16,17], suggesting different functional roles.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Isoenzyme patterns of protein kinase C and a phospholipid‐dependent but Ca²⁺‐inhibited enzyme fraction in the crude extracts of different tissues

et al. 1989

View full text Add to dashboard Cite

We compared the protein kinase C isoenzyme patterns of crude extracts of rabbit brain, cerebellum, spleen, thymus and human and pig granulocytes. The isoenzymes were fractionated by hydroxyapatite chromatography and the protein kinase C activity was determined with a synthetic oligopeptide substrate. In the extracts of several tissues we also observed an enzyme fraction which was activated by phosphatidylserine + diacylglycerol but inhibited by Ca z÷.Protein kinase C; Synthetic ofigopeptide substrate; Isoenzyme; Ca2+-inhibited enzyme fraction

show abstract

supporting

confidence: 88%

Section: Introductionmentioning

confidence: 99%

Isoenzyme patterns of protein kinase C and a phospholipid‐dependent but Ca²⁺‐inhibited enzyme fraction in the crude extracts of different tissues

et al. 1989

View full text Add to dashboard Cite

show abstract

“…In the brain, three major distinct types of protein kinase C can be resolved upon chromatography on a hydroxyapatite column [12- with the respective cDNA-containing plasmids [13,14]. The subspecies of protein kinase C thus identified appear to show a slightly different mode of activation, kinetic properties and substrate specificities [16,17]. In the present study an additional three subspecies of the protein kinase C family will be described.…”

Section: Introductionmentioning

confidence: 96%

Identification of three additional members of rat protein kinase C family: gd‐, ϵ‐ and ξ‐subspecies

et al. 1987

Self Cite

View full text Add to dashboard Cite

Three types of cDNA clone of the protein kinase C family termed 6, Eand < were newly identified by molecular cloning and sequence analysis. These members have a common structure that is closely related to, but clearly different from the other four known members of the family which have LX-, PI-, PII-and y-sequences, although the I-cDNA available at present does not contain a complete reading frame for a protein kinase C molecule. The diverse heterogeneity of the enzyme seems to be an important factor in determining the mode of response of many tissues and cell types to a variety of external stimuli.Protein kinase C; cDNA; (Rat brain)

show abstract

“…Moreover, Wang et al (2001) found no evidence for lindane activation of PLC or a calciumdependent PLA 2 as a mechanism for lindane-induced myometrial release of arachidonic acid. Nonetheless, lindane stimulation of arachidonic acid release may be involved in inhibition of myometrial gap junctions and uterine contractions (Criswell and Loch-Caruso, 1999) by an unidentified pathway, perhaps through actions on PKC, as observed in neural tissue (Sekiguchi et al, 1987;Shearman et al, 1989) and macrophages (Huang et al, 1997). The mechanistic correlation between myometrial PLC activation and arachidonic acid release by lindane is under further investigation.…”

Section: Discussionmentioning

confidence: 97%

Phospholipase-Mediated Inhibition of Spontaneous Oscillatory Uterine Contractions by Lindane in Vitro,

Wang

Loch‐Caruso

2002

Toxicology and Applied Pharmacology

View full text Add to dashboard Cite

Although regulation of uterine contractility is fundamental for parturition, mechanisms by which toxicants modify uterine muscle contractions remain poorly understood. In a previous cumulative concentration-response study, 10 μM lindane (γ-hexachlorocyclohexane) reduced contraction force and 30 μM lindane abolished contractions in Gestation Day 10 rat uterine strips when lindane was added to muscle baths at 10-min intervals. Other studies showed that brief (<10 min) exposures to 10-100 μM lindane inhibit gap junctions and activate phospholipase pathways in rat myometrial cells in culture. Consequently, lindane was used as a prototype toxicant with known uterine activity to investigate the hypothesis that activation of a specific phospholipase pathway provides a mechanistic link between inhibition of uterine contraction and inhibition of myometrial gap junctions. Uterine tissue and cells were pretreated with phospholipase pathway inhibitors to evaluate the role of phospholipase pathways in lindane's actions in the uterus. Concentrations of inhibitors were selected based on previous reports of effective concentrations for the enzyme activity and on pilot toxicity studies of the inhibitors on uterine contraction and gap junction communication. To monitor uterine contractions, longitudinal uterine strips were excised from Gestation Day 10 rats and suspended in isometric muscle baths, consistent with previous experiments. Exposure in vitro for 60 min to 10-50 μM lindane, an effective concentration range for the uterine responses of interest, revealed that 30 μM lindane rapidly abolished contractions. Subsequently, uterine strips were pretreated with phospholipase pathway inhibitors and then challenged with 30 μM lindane, the lindane concentration that elicited maximal inhibition of uterine contraction. Pretreatment with 20-50 μM of the phosphatidylinositol-specific phospholipase C inhibitor 1-O-octadecyl-2-O-methyl-sn -glycerol-3-phosphorylcholine (ET-18-OCH 3 ) reversed lindane-induced inhibition of spontaneous uterine contractions. Gap junction intercellular communication was monitored by injecting the fluorescent dye Lucifer yellow into rat myometrial cells grown in culture and assessing dye transfer to adjacent cells using epifluorescence microscopy. Similar to uterine contraction, pretreatment of cell cultures with phospholipase C inhibitors (30 μM ET-18-OCH 3 , 50 μM tricyclodecan-p-yl-xanthogenate · K [D609] or 50 μM tricyclodecan-p-yl-xanthogenate · K or 2-nitro-4-carboxyphenyl-N,Ndophenylcarbamate [NCDC]) partially reversed inhibition of dye transfer by 100 μM lindane, a 4To whom correspondence and reprint requests should be addressed at 1420 Washington Heights, Department of Environmental Health Sciences, School of Public Health, University of Michigan, Ann Arbor, MI 48109-2029. Fax: (734) lindane concentration previously shown to abolish myometrial Lucifer yellow dye transfer under similar culture conditions. In contrast, pretreatment with 20 μM of bromoenol lactone (BEL) to inhibit the calcium-i...

show abstract

Three distinct forms of rat brain protein kinase C: Differential response to unsaturated fatty acids

Cited by 236 publications

References 15 publications

Isoenzyme patterns of protein kinase C and a phospholipid‐dependent but Ca²⁺‐inhibited enzyme fraction in the crude extracts of different tissues

Isoenzyme patterns of protein kinase C and a phospholipid‐dependent but Ca²⁺‐inhibited enzyme fraction in the crude extracts of different tissues

Identification of three additional members of rat protein kinase C family: gd‐, ϵ‐ and ξ‐subspecies

Phospholipase-Mediated Inhibition of Spontaneous Oscillatory Uterine Contractions by Lindane in Vitro,

Contact Info

Product

Resources

About

Three distinct forms of rat brain protein kinase C: Differential response to unsaturated fatty acids

Cited by 236 publications

References 15 publications

Isoenzyme patterns of protein kinase C and a phospholipid‐dependent but Ca2+‐inhibited enzyme fraction in the crude extracts of different tissues

Isoenzyme patterns of protein kinase C and a phospholipid‐dependent but Ca2+‐inhibited enzyme fraction in the crude extracts of different tissues

Identification of three additional members of rat protein kinase C family: gd‐, ϵ‐ and ξ‐subspecies

Phospholipase-Mediated Inhibition of Spontaneous Oscillatory Uterine Contractions by Lindane in Vitro,

Contact Info

Product

Resources

About

Isoenzyme patterns of protein kinase C and a phospholipid‐dependent but Ca²⁺‐inhibited enzyme fraction in the crude extracts of different tissues

Isoenzyme patterns of protein kinase C and a phospholipid‐dependent but Ca²⁺‐inhibited enzyme fraction in the crude extracts of different tissues