Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease.

Kishimoto, Akira; Kajikawa, Norio; Shiota, Makoto; Nishizuka, Yasutomi

doi:10.1016/s0021-9258(18)33173-9

Cited by 571 publications

(26 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In order for the proteins' movement to be visible by monitoring the fluorescence of GFP fused to the protein, the fusion proteins must have the same properties as native PKCs. Furthermore, because PKCs are reported to be proteolysed by proteases such as calpain (Kishimoto et al, 1983), we examined the enzymological and immunochemical properties of ␥and ⑀-PKC-GFP. Because ␥-PKC-GFP is reported to have the same properties as native ␥-PKC (Sakai et al, 1997), we analyzed the properties of ⑀-PKC-GFP by a kinase assay, immunostaining, and Western blotting and found that (a) the activity of ⑀-PKC-GFP was dependent on PS and DO (Fig.…”

Section: Discussionmentioning

confidence: 99%

Distinct Effects of Fatty Acids on Translocation of γ- and ε-Subspecies of Protein Kinase C

Shirai

Kashiwagi

Yagi

et al. 1998

The Journal of Cell Biology

131

107

View full text Add to dashboard Cite

Effects of fatty acids on translocation of the γ- and ε-subspecies of protein kinase C (PKC) in living cells were investigated using their proteins fused with green fluorescent protein (GFP). γ-PKC–GFP and ε-PKC–GFP predominated in the cytoplasm, but only a small amount of γ-PKC–GFP was found in the nucleus. Except at a high concentration of linoleic acid, all the fatty acids examined induced the translocation of γ-PKC–GFP from the cytoplasm to the plasma membrane within 30 s with a return to the cytoplasm in 3 min, but they had no effect on γ-PKC–GFP in the nucleus. Arachidonic and linoleic acids induced slow translocation of ε-PKC–GFP from the cytoplasm to the perinuclear region, whereas the other fatty acids (except for palmitic acid) induced rapid translocation to the plasma membrane. The target site of the slower translocation of ε-PKC–GFP by arachidonic acid was identified as the Golgi network. The critical concentration of fatty acid that induced translocation varied among the 11 fatty acids tested. In general, a higher concentration was required to induce the translocation of ε-PKC–GFP than that of γ-PKC–GFP, the exceptions being tridecanoic acid, linoleic acid, and arachidonic acid. Furthermore, arachidonic acid and the diacylglycerol analogue (DiC8) had synergistic effects on the translocation of γ-PKC–GFP. Simultaneous application of arachidonic acid (25 μM) and DiC8 (10 μM) elicited a slow, irreversible translocation of γ-PKC– GFP from the cytoplasm to the plasma membrane after rapid, reversible translocation, but a single application of arachidonic acid or DiC8 at the same concentration induced no translocation.These findings confirm the involvement of fatty acids in the translocation of γ- and ε-PKC, and they also indicate that each subspecies has a specific targeting mechanism that depends on the extracellular signals and that a combination of intracellular activators alters the target site of PKCs.

show abstract

Section: Discussionmentioning

confidence: 99%

Distinct Effects of Fatty Acids on Translocation of γ- and ε-Subspecies of Protein Kinase C

Shirai

Kashiwagi

Yagi

et al. 1998

The Journal of Cell Biology

131

107

View full text Add to dashboard Cite

show abstract

“…The data represent the means ± standard deviations of three independent experiments. generation (16,21,25,30,31). It is likely that the chemiluminescence response and leukotriene generation are mediated predominantly by only one or two of the abovedescribed active species of PKC.…”

Section: Discussionmentioning

confidence: 99%

Roles of human peripheral blood leukocyte protein kinase C and G proteins in inflammatory mediator release by isogenic Escherichia coli strains

König

1991

Infect Immun

View full text Add to dashboard Cite

The signal transduction pathway (protein kinase C [PKC], calcium influx, and G protein involvement) was studied with isogenic Escherichia coli strains expressing different types of adhesins (MSH+/- MS-Fim+/-, P-MRH+/- P-Fim+/-, and S-MRH+/- S-Fim+/-) or varying only in the expression of E. coli alpha-hemolysin. As target cells, human polymorphonuclear granulocytes (PMN) and a lymphocyte-monocyte-basophil (LMB) cell suspension were used. The alpha-hemolysin-producing (Hly+) strain E. coli K-12(pANN5211) induced calcium influx in a dose-dependent manner in both cell types. No calcium influx was detected after stimulation with the hemolysin-negative (Hly-) E. coli bacteria independent of the type of fimbriae. With Hly+ bacteria, a dose-dependent activation of PKC was observed in both cell types. The Hly- E. coli K-12 induced PKC to a lesser degree, expressing kinetics different from those of E. coli K-12(pANN5211) (Hly+). E. coli MSH+ MS-Fim+ was the most potent activator for PKC. Membrane preparations from leukocytes stimulated with Hly+ E. coli K-12(pANN5211) showed increased binding of [3H]guanylylimidodiphosphate, a nonhydrolyzable GTP analog, and increased GTPase activity compared with leukocytes stimulated with Hly- E. coli K-12. The amounts of GTPase activation and [3H]guanylylimidodiphosphate binding were similar for all Hly- E. coli bacteria in human PMN as well as in human LMB; no activation was obtained for E. coli bacteria without any type of fimbriae. GTP-gamma-S, a nonhydrolyzable GTP analog, inhibited the leukotriene B4 (LTB4) generation from human PMN by Hly- bacteria, unlike E. coli K-12(pANN5211). However, in the presence of NaF, a predominant activator of Gi, LTB4 generation by Hly+ and by Hly- bacteria was significantly enhanced. For LMBs only LTB4 generation by Hly+ bacteria was increased in the presence of GTP-gamma-S. NaF decreased the chemiluminescence induced by all E. coli strains. Our results thus indicate that (i) Hly+ and Hly- bacteria induce the activation of distinct G proteins, e.g., Gi, to different degrees, (ii) LTB4 generation and chemiluminescence response are differently regulated, and (iii) in comparison with PMN, a different signal transduction pathway is activated by E. coli bacteria in LMBs.

show abstract

“…In support of this finding is the recent report (22) suggesting that the T200 glycoprotein may be an enzyme with Ca++-dependent autoproteolytic activity. The authors (22) discussed the similarities of the T200-associated protease and the protease that activates protein kinase C (48) and is the endogenous enzyme that cleaves the epidermal growth factor (EGF) receptor (49). Like the EGF receptor, the T200 molecule has an unusually large intracytoplasmic domain (Mr 80 K) with several possible phosphorylation sites, although little sequence homology between T200 and the EGF receptor was noted (50).…”

Section: Discussionmentioning

confidence: 99%

Acquisition of cytotoxic T lymphocyte-specific carbohydrate differentiation antigens.

Lefrançois

Puddington

Machamer

et al. 1985

The Journal of Experimental Medicine

View full text Add to dashboard Cite

The mechanism by which cytotoxic T lymphocytes (CTL) j recognize and subsequently destroy target cells remains obscure. This process occurs in three discrete steps: (a) recognition and binding of the CTL to the target cell, (b) programming for lysis, and (c) target cell destruction. One requirement for proper recognition by CTL is the simultaneous expression on the target cell plasma membrane of a specific foreign antigen and a particular histocompatibility molecule. At the CTL level, not only is the T cell receptor for antigen necessary for target cell recognition (1, 2) but a number of other molecules have been implicated in CTL-induced lysis. These include T3, which is noncovalently associated with the T cell antigen receptor (3, 4); Lyt-2 (5, 6) and L3T4 (7), which may confer specificity for a particular class of histocompatibility molecule; and the leukocyte function-associated antigens (8). In each of these cases the binding of antibodies specific for these proteins to the CTL cell surface results in the inhibition of CTL-mediated lysis. However, since all of these molecules are present on naive, noncytolytic CTL precursors, activational processes must occur after a primary encounter with antigen which allow the subsequent expression of cytolytic capability by CTL in an antigen-specific manner.Recently (9, 10), we have described activation antigens that are associated with CTL (termed CT determinants). Monoclonal antibodies (mAb) specific for these antigens inhibit the function of CTL expressing high levels of CT antigen on their surface. Biochemical analyses revealed that the CT determinants are present on the T200 molecules of murine CTL and on two other unidentified cell surface proteins. Although forms of T200 are found on all T cells and hematopoietic cells except cells of erythroid lineage (11), the CT antigens are expressed only on the T200 glycoprotein of activated CTL. T200 has been previously implicated in natural killer (NK) cell-mediated lysis (12, 13) but its role in the lytic mechanism of CTL remains controversial. The Ly-5 alloantigenic determinants

show abstract

Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease.

Cited by 571 publications

References 34 publications

Distinct Effects of Fatty Acids on Translocation of γ- and ε-Subspecies of Protein Kinase C

Distinct Effects of Fatty Acids on Translocation of γ- and ε-Subspecies of Protein Kinase C

Roles of human peripheral blood leukocyte protein kinase C and G proteins in inflammatory mediator release by isogenic Escherichia coli strains

Acquisition of cytotoxic T lymphocyte-specific carbohydrate differentiation antigens.

Contact Info

Product

Resources

About