The effect of prolactin on casein kinase II, MAP kinase and PKC in rabbit mammary cells and Nb2 rat lymphoid cells

Mitev, Vanio; Bayat-Sarmadi, Mahasti; Lemnaouar, Mustapha; Puissant, C.; Houdebiné, Louis‐Marie

doi:10.1016/s0006-2952(96)00523-0

Cited by 19 publications

(9 citation statements)

References 37 publications

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“…It has recently been shown that purified endogenous casein kinase II effectively phosphorylated serine 32 of I B␣ and that when associated with p90 rsk , this kinase complex is capable of phosphorylating both degradation-relevant serines in I B␣ and also exists as a preassembled kinase-substrate complex containing all known I B isoforms and most Rel family members (51). These last data together with many other reports, such as in U937, Chinese ovary, and rat lymphoid cells treated with bufalin (52), insulin (53), and prolactin (54), demonstrate the inducibility of casein kinase II. It is thus clear that casein kinase II activity may be stimulated by various stimuli, and oxidative stress is probably one of them.…”

Section: Discussionsupporting

confidence: 67%

Crucial Role of the Amino-Terminal Tyrosine Residue 42 and the Carboxyl-Terminal PEST Domain of IκBα in NF-κB Activation by an Oxidative Stress

Schoonbroodt

Ferreira²,

Best‐Belpomme

et al. 2000

The Journal of Immunology

233

172

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Activation of transcription factor NF-κB involves the signal-dependent degradation of basally phosphorylated inhibitors such as IκBα. In response to proinflammatory cytokines or mitogens, the transduction machinery has recently been characterized, but the activation mechanism upon oxidative stress remains unknown. In the present work, we provide several lines of evidence that NF-κB activation in a T lymphocytic cell line (EL4) by hydrogen peroxide (H2O2) did not involve phosphorylation of the serine residues 32 and 36 in the amino-terminal part of IκBα. Indeed, mutation of Ser32 and Ser36 blocked IL-1β- or PMA-induced NF-κB activation, but had no effect on its activation by H2O2. Although IκBα was phosphorylated upon exposure to H2O2, tyrosine residue 42 and the C-terminal PEST (proline-glutamic acid-serine-threonine) domain played an important role. Indeed, mutation of tyrosine 42 or serine/threonine residues of the PEST domain abolished NF-κB activation by H2O2, while it had no effect on activation by IL-1β or PMA-ionomycin. This H2O2-inducible phosphorylation was not dependent on IκB kinase activation, but could involve casein kinase II, because an inhibitor of this enzyme (5,6-dichloro-1-β-d-ribofuranosyl-benzimidazole) blocks NF-κB activation. H2O2-induced IκBα phosphorylation was followed by its degradation by calpain proteases or through the proteasome. Taken together, our findings suggest that NF-κB activation by H2O2 involves a new mechanism that is totally distinct from those triggered by proinflammatory cytokines or mitogens.

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Section: Discussionsupporting

confidence: 67%

Crucial Role of the Amino-Terminal Tyrosine Residue 42 and the Carboxyl-Terminal PEST Domain of IκBα in NF-κB Activation by an Oxidative Stress

Schoonbroodt

Ferreira²,

Best‐Belpomme

et al. 2000

The Journal of Immunology

233

172

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“…oocytes treated with thimerosal in the presence of the inhibitor of protein kinase C Ro 31-8220 agree with the above mentioned data. Our results suggesting that the effects of prolactin on pig oocytes are related to the protein kinase C activation also agree with the data obtained on cells of other animals: rat lymphoid cells, rabbit mammary gland cells, and pig theca cells (Mitev et al, 1996;Ciereszko et al, 2003). Phorbol ester 12-tetradecanoylphorbol-13-acetate activates protein kinase C in various cells (Downs et al, 2001).…”

Section: Discussionsupporting

confidence: 91%

Effects of Guanine Nucleotides and Protein Kinase C on Prolactin-Stimulated Release of Ca2+ from Intracellular Stores of Pig Oocytes

Denisenko

Kuzmina

2005

Russ J Dev Biol

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Prolactin is involved in the regulation of growth and differentiation, as well as of reproductive function in mammals. However, the mechanisms underlying the action of the hormone at the cellular level are not yet fully clear. It was shown that ë ‡ 2+ cam mediate the effect of prolactin, since it stimulates the mobilization of Ca 2+ from intracellular stores, as well as supply of Ca 2+ from outside (Villalba et al. , 1991;Szafranska et al. , 1999). The fluorescent dye chlorotetracycline is used to detect the presence of Ca 2+ and measure its level in the intracellular compartments (Dixon et al. , 1984;Engelmann et al. , 1990).There are data on interrelations between the effect of prolactin and protein kinase C activity in the cell: prolactin induces protein kinase C in the mouse mammary gland cells (Banerjee and Vonderhaar, 1992). In the liver cells, GTP stimulates the inositol triphosphateinduced Ca 2+ release from intracellular stores but inhibits the GTP-stimulated release (Wolf et al. , 1987;Kobayashi et al. , 1988).The aim of this work was to study the effects of guanine nucleotides and protein kinase C on prolactinstimulated Ca 2+ release from intracellular stores of pig oocytes. MATERIALS AND METHODSStudies were carried out on oocytes of Landras pigs killed at the meat cutting plant. Ovaries at the stage of follicular growth without visible signs of pathology were used in the experiments. The ovaries were washed by saline three times and oocytes were isolated from the follicles, 3 to 6 mm in diameter. Circular oocytes with fine-granulated ooplasm and equally wide zona pellucida were taken. The oocytes were isolated in saline in Petri dishes by dissecting the follicles with a safety blade. The oocytes with tissue fragments were then washed three times by saline and transferred in Dulbecco medium consisting of (mM): NaCl 136, KCl 2.7, CaCl 2 (anhydrous) 0.9, MgCl 2 · 6H 2 O-0.49, NaHPO 4 · H 2 O 8.9, and KH 2 PO 4 1.5. The medium was complemented with 36 mg/l pyruvate and 1 g/l glucose and the oocytes were cleaned from cumulus cells by a preparation needle before incubation. The oocytes were incubated in Dulbecco medium with pyruvate and glucose in the presence or absence of 0.9 mM CaCl 2 .Ca concentration in intracellular stores was measured using the fluorescent dye chlorotetracycline (CTC). Prior to measurements, the oocytes were cleaned from cumulus cells and incubated in an incubation medium containing 40 µ m CTC at 37°C for 5 min. The cells were then washed three times by the incubation medium and transferred onto a special quartz glass Abstract -The effects of guanine nucleotides and protein kinase C on prolactin-stimulated ë ‡ 2+ release from intracellular stores of pig oocytes were studied using the fluorescent dye chlorotetracycline. The effect of prolactin was related to the protein kinase C activation. Inhibition of protein kinase C stimulated ë ‡ 2+ release from intracellular stores of the pig oocytes treated with 5 ng/ml prolactin in the presence of extracellular ë ‡ 2+ and inhibited ë ‡ 2+ rel...

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“…40 The activity of CKII in rat lymphoid Nb2 cells was 2-fold higher than in the control 24 h later following prolactin treatment. 48 The slow stimulation of CKII by prolactin in Nb2 cells suggests that this kinase is not specifically induced and is not responsible for inducing ODC activity in prolactin action. Our results demonstrate that prolactin rapidly induces ODC activity but doesn't affect ODC mRNA and protein expression.…”

Section: Discussionmentioning

confidence: 99%

Increasing ornithine decarboxylase activity is another way of prolactin preventing methotrexate-induced apoptosis: Crosstalk between ODC and BCL-2

et al. 2006

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Prolactin has more than 300 separate functions including affecting mammary growth, differentiation, secretion and anti-apoptosis. In the previous studies, prolactin induced Bcl-2 expression to prevent apoptosis and also provoked the activity of ornithine decarboxylase (ODC). Our previous data showed that ODC overexpression upregulates Bcl-2 and prevents tumor necrosis factor alpha (TNF-alpha)- and methotrexate (MTX)-induced apoptosis. Here, we further investigate whether prolactin prevents MTX-induced apoptosis through inducing ODC activity and the relationship between ODC and Bcl-2 upon prolactin stimulation. Prolactin prevented MTX-induced apoptosis in a dose-dependent manner in HL-60 cells. Following prolactin stimulation, ODC enzyme activity also shows an increase in a dose-dependent manner, expressing its maximum level at 3 h, and rapidly declining thereafter. Prolactin-induced ODC activity is completely blocked by a protein kinase C delta (PKCdelta) inhibitor, rottlerin. However, there are no changes in the expressions of ODC mRNA and protein level after prolactin stimulus. It indicates that prolactin may induce ODC activity through the PCKdelta pathway. Besides, Bcl-2 expresses within 1 h of prolactin treatment and this initiating effect of prolactin is not inhibited by alpha-difluoromethylornithine (DFMO). However, Bcl-2 is further enhanced following prolactin stimulation for 4 h and this enhancement is blocked by DFMO. Bcl-2 has no effect on ODC activity and protein levels, but ODC upregulates Bcl-2, which is inhibited by DFMO. Overall, there are two different forms of prolactin effect, it induces Bcl-2 primarily, and following this it stimulates ODC activity. Consequently induced ODC activity further enhances the expression of Bcl-2. The anti-apoptotic effect of prolactin is diminished by DFMO and recovered by putrescine. Obviously, ODC activity is one basis for the anti-apoptotic mechanisms of prolactin. A Bcl-2 inhibitor, HA14-1, together with DFMO, completely blocks the anti-apoptotic effects of prolactin. These results suggest that increasing ODC activity is another way of prolactin preventing MTX-induced apoptosis and that this induction of ODC activity enhances the expression of Bcl-2 strongly enough to bring about the anti-apoptotic function.

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The effect of prolactin on casein kinase II, MAP kinase and PKC in rabbit mammary cells and Nb2 rat lymphoid cells

Cited by 19 publications

References 37 publications

Crucial Role of the Amino-Terminal Tyrosine Residue 42 and the Carboxyl-Terminal PEST Domain of IκBα in NF-κB Activation by an Oxidative Stress

Crucial Role of the Amino-Terminal Tyrosine Residue 42 and the Carboxyl-Terminal PEST Domain of IκBα in NF-κB Activation by an Oxidative Stress

Effects of Guanine Nucleotides and Protein Kinase C on Prolactin-Stimulated Release of Ca2+ from Intracellular Stores of Pig Oocytes

Increasing ornithine decarboxylase activity is another way of prolactin preventing methotrexate-induced apoptosis: Crosstalk between ODC and BCL-2

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