Resolution and characterization of calcium/phospholipid-dependent protein kinase and H4 protease-activated protein kinase activities in lymphoid cells

Magnino, Peggy E.; Houssaye, Becky A. de la; Masaracchia, Ruthann A.

doi:10.1016/0006-291x(83)90578-8

Cited by 8 publications

(4 citation statements)

References 11 publications

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“…The activities of at least five other kinases can be increased following proteolysis: phosphorylase kinase (Hayakawa et al, 1973); myosin light chain kinase (Tanaka et al, 1980); proteaseactivated kinase I (Tahara & Traugh,198 1); protease-activated kinase I1 (Lubben & Traugh, 1983); protease-activated histone H4 kinase . However, with the exception of the latter two (Lubben & Traugh, 1983;Magnino et al, 1983), the others do not phosphorylate histone H1 (Chrisman et al, 1982;Adelstein & Klee, 1981;Tahara & Traugh, 1981).…”

Section: Resultsmentioning

confidence: 95%

“…Since protease-activated kinase II and protease-activated H4 kinase share somewhat similar DEAE and gel filtration chromatographic properties with PKC (Lubben & Traugh, 1983;Magnino et al, 1983), the contribution of these kinases toward the total trypsin-stimulated histone HI kinase activity in 3T3 cell extracts could not be readily discounted. However, as shown in the next section, in experiments with TPA, greater figure 1: DEAE-Sephacel chromatography of the trypsin-activated and Ca2+/phosphatidylserine/diolein-activated histone HI kinases in Swiss 3T3 cell cytosol.…”

Section: Resultsmentioning

confidence: 99%

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Rapid microassay for protein kinase C translocation in Swiss 3T3 cells

Pelech¹,

Meier²,

Krebs³

1986

Biochemistry

100

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The Ca2+/phosphatidylserine-stimulated protein kinase C (PKC) appears to exist as interconvertible inactive, soluble and active, membrane-bound forms. Changes in the bimodal distribution of PKC induced by diacylglycerol or tumor-promoting phorbol esters have been proposed to regulate the activity of this kinase [Nishizuka, Y. (1984) Nature (London) 308, 693-698]. A rapid microassay for assessment of protein kinase C translocation between cytosol and membranes was developed. This procedure, which relied on the selective digitonin-mediated release of cytoplasmic proteins, eliminated potential homogenization and fractionation artifacts. PKC activity toward histone H1 was determined after limited trypsinolysis, which abolished the Ca2+/phospholipid requirement of the enzyme and prevented interference by inhibitory proteins. Complete translocation of PKC to the membrane fraction and subsequent down-regulation of the kinase in response to 12-O-tetradecanoylphorbol-13-acetate treatment of Swiss 3T3 cells could be demonstrated by this method. Platelet-derived growth factor, insulin-like growth factor 1, vasopressin, and prostaglandin F2 alpha facilitated partial conversions of PKC to the membrane-bound form in quiescent 3T3 cells.

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Section: Resultsmentioning

confidence: 95%

Section: Resultsmentioning

confidence: 99%

Rapid microassay for protein kinase C translocation in Swiss 3T3 cells

Pelech¹,

Meier²,

Krebs³

1986

Biochemistry

100

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“…4A to D and 5A and B). For instance, Act induced phosphorylation of adducin and PKC, both of which could be mediated by calcium (32,38,69). Act also activated CREB (Fig.…”

Section: Discussionmentioning

confidence: 95%

Microarray and Proteomics Analyses of Human Intestinal Epithelial Cells Treated with theAeromonas hydrophilaCytotoxic Enterotoxin

et al. 2005

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We performed microarray analyses on RNA from human intestinal epithelial (HT-29) cells treated with the cytotoxic enterotoxin (Act) of Aeromonas hydrophila to examine global cellular transcriptional responses. Based on three independent experiments, Act upregulated the expression of 34 genes involved in cell growth, adhesion, signaling, immune responses (including interleukin-8 [IL-8] production), and apoptosis. We verified the upregulation of 14 genes by real-time reverse transcriptase-PCR and confirmed Act-induced production of IL-8 by enzyme-linked immunosorbent assay on supernatants from nonpolarized and polarized HT-29 cells. Maximal production of IL-8 in response to Act required the presence of intracellular calcium, since chelation of calcium with BAPTA-AM significantly reduced Act-induced IL-8 production in HT-29 cells. We also examined activation of mitogen-activated protein kinases and, as demonstrated by Western blot analysis of apical side-treated polarized HT-29 cells, Act induced phosphorylation of p38, c-Jun NH2-terminal kinase, and extracellular signal-regulated kinase 1/2. In addition, KinetWorks proteomics screening of whole-cell lysates revealed Act-induced phosphorylation of cyclic AMP-response element binding protein (CREB), c-Jun, adducin, protein kinase C, and signal transducer and activator of transcription 3 (STAT3) and decreased phosphorylation of protein kinase Bα, v-raf-1 murine leukemia viral oncogene homolog 1 (i.e., Raf1), and STAT1. We verified activation of CREB and activator protein 1 in polarized cells by gel shift assay. This is the first description of human intestinal epithelial cell transcriptional alterations, phosphorylation or activation of signaling molecules, cytokine production, and calcium mobilization in response to this toxin

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“…Another possible enzyme is the Ca*+-phospholipiddependent protein kinase that can be activated proteolytically [30], can phosphorylate S6 [ 171 and appears to be present in liver cells [3 11. However, this enzyme may have been eliminated by the CMSepharose step because of its low affinity for cation-exchange resins [32].…”

Section: Discussionmentioning

confidence: 99%

Phosphorylation of ribosomal protein S6 and a peptide analogue of S6 by a protease‐activated kinase isolated from rat liver

et al. 1984

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A trypsin-activated protein kinasc has been isolated from rat liver using a peptide analogue of ribosomal protein S6 as a substrate in kinase assays. The structure of the peptide, Arg-Arg-Leu-Ser-Ser-Leu-Arg-Ala, was based on a region of S6 containing both an insulin-and cyclic AMP-regulated phosphorylation site. The trypsin-activated protein kinase phosphorylated a corresponding site in the peptide analogue and ribosomal protein S6 that was distinct from the preferred site for cyclic AMP-dependent protein kinase. Ribosoma1 S6 contained at least one other major site for the trypsin-activated protein kinase. Ribosomal protein St5Synthetic peptide analogue

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Resolution and characterization of calcium/phospholipid-dependent protein kinase and H4 protease-activated protein kinase activities in lymphoid cells

Cited by 8 publications

References 11 publications

Rapid microassay for protein kinase C translocation in Swiss 3T3 cells

Rapid microassay for protein kinase C translocation in Swiss 3T3 cells

Microarray and Proteomics Analyses of Human Intestinal Epithelial Cells Treated with theAeromonas hydrophilaCytotoxic Enterotoxin

Phosphorylation of ribosomal protein S6 and a peptide analogue of S6 by a protease‐activated kinase isolated from rat liver

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