Glucose, other secretagogues, and nerve growth factor stimulate mitogen-activated protein kinase in the insulin-secreting beta-cell line, INS-1.

M Frödin; N Sekine; E Roche; C Filloux; M Prentki; C B Wollheim; E Van Obberghen

Glucose, other secretagogues, and nerve growth factor stimulate mitogen-activated protein kinase in the insulin-secreting beta-cell line, INS-1.

M Frödin, N Sekine, E Roche, C Filloux, M Prentki, C B Wollheim, E Van Obberghen

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

203 Citationer (Scopus)

Abstract

Udgivelsesdato: 1995-Apr-7

Originalsprog	Engelsk
Tidsskrift	Journal of Biological Chemistry
Vol/bind	270
Udgave nummer	14
Sider (fra-til)	7882-9
Antal sider	7
ISSN	0021-9258
Status	Udgivet - 1995

Bibliografisk note

Keywords: Calcium; Camptothecin; Cell Line; Cytosol; DNA; Enzyme Activation; Gene Expression Regulation; Genes, Immediate-Early; Glucose; Insulin; Islets of Langerhans; Nerve Growth Factors; Potassium Chloride; Protein Kinases; Tetradecanoylphorbol Acetate

Citationsformater

Glucose, other secretagogues, and nerve growth factor stimulate mitogen-activated protein kinase in the insulin-secreting beta-cell line, INS-1. / Frödin, M; Sekine, N; Roche, E; Filloux, C; Prentki, M; Wollheim, C B; Van Obberghen, E.

I: Journal of Biological Chemistry, Bind 270, Nr. 14, 1995, s. 7882-9.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

@article{d2fc1d40524211dd8d9f000ea68e967b,

title = "Glucose, other secretagogues, and nerve growth factor stimulate mitogen-activated protein kinase in the insulin-secreting beta-cell line, INS-1.",

abstract = "The signaling pathways whereby glucose and hormonal secretagogues regulate insulin-secretory function, gene transcription, and proliferation of pancreatic beta-cells are not well defined. We show that in the glucose-responsive beta-cell line INS-1, major secretagogue-stimulated signaling pathways converge to activate 44-kDa mitogen-activated protein (MAP) kinase. Thus, glucose-induced insulin secretion was found to be associated with a small stimulatory effect on 44-kDa MAP kinase, which was synergistically enhanced by increased levels of intracellular cAMP and by the hormonal secretagogues glucagon-like peptide-1 and pituitary adenylate cyclase-activating polypeptide. Activation of 44-kDa MAP kinase by glucose was dependent on Ca2+ influx and may in part be mediated by MEK-1, a MAP kinase kinase. Stimulation of Ca2+ influx by KCl was in itself sufficient to activate 44-kDa MAP kinase and MEK-1. Phorbol ester, an activator of protein kinase C, stimulated 44-kDa MAP kinase by both Ca(2+)-dependent and -independent pathways. Nerve growth factor, independently of changes in cytosolic Ca2+, efficiently stimulated 44-kDa MAP kinase without causing insulin release, indicating that activation of this kinase is not sufficient for secretion. In the presence of glucose, however, nerve growth factor potentiated insulin secretion. In INS-1 cells, activation of 44-kDa MAP kinase was partially correlated with the induction of early response genes junB, nur77, and zif268 but not with stimulation of DNA synthesis. Our findings suggest a role of 44-kDa MAP kinase in mediating some of the pleiotropic actions of secretagogues on the pancreatic beta-cell.",

author = "M Fr{\"o}din and N Sekine and E Roche and C Filloux and M Prentki and Wollheim, {C B} and {Van Obberghen}, E",

note = "Keywords: Calcium; Camptothecin; Cell Line; Cytosol; DNA; Enzyme Activation; Gene Expression Regulation; Genes, Immediate-Early; Glucose; Insulin; Islets of Langerhans; Nerve Growth Factors; Potassium Chloride; Protein Kinases; Tetradecanoylphorbol Acetate",

year = "1995",

language = "English",

volume = "270",

pages = "7882--9",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology, Inc.",

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TY - JOUR

T1 - Glucose, other secretagogues, and nerve growth factor stimulate mitogen-activated protein kinase in the insulin-secreting beta-cell line, INS-1.

AU - Frödin, M

AU - Sekine, N

AU - Roche, E

AU - Filloux, C

AU - Prentki, M

AU - Wollheim, C B

AU - Van Obberghen, E

N1 - Keywords: Calcium; Camptothecin; Cell Line; Cytosol; DNA; Enzyme Activation; Gene Expression Regulation; Genes, Immediate-Early; Glucose; Insulin; Islets of Langerhans; Nerve Growth Factors; Potassium Chloride; Protein Kinases; Tetradecanoylphorbol Acetate

PY - 1995

Y1 - 1995

N2 - The signaling pathways whereby glucose and hormonal secretagogues regulate insulin-secretory function, gene transcription, and proliferation of pancreatic beta-cells are not well defined. We show that in the glucose-responsive beta-cell line INS-1, major secretagogue-stimulated signaling pathways converge to activate 44-kDa mitogen-activated protein (MAP) kinase. Thus, glucose-induced insulin secretion was found to be associated with a small stimulatory effect on 44-kDa MAP kinase, which was synergistically enhanced by increased levels of intracellular cAMP and by the hormonal secretagogues glucagon-like peptide-1 and pituitary adenylate cyclase-activating polypeptide. Activation of 44-kDa MAP kinase by glucose was dependent on Ca2+ influx and may in part be mediated by MEK-1, a MAP kinase kinase. Stimulation of Ca2+ influx by KCl was in itself sufficient to activate 44-kDa MAP kinase and MEK-1. Phorbol ester, an activator of protein kinase C, stimulated 44-kDa MAP kinase by both Ca(2+)-dependent and -independent pathways. Nerve growth factor, independently of changes in cytosolic Ca2+, efficiently stimulated 44-kDa MAP kinase without causing insulin release, indicating that activation of this kinase is not sufficient for secretion. In the presence of glucose, however, nerve growth factor potentiated insulin secretion. In INS-1 cells, activation of 44-kDa MAP kinase was partially correlated with the induction of early response genes junB, nur77, and zif268 but not with stimulation of DNA synthesis. Our findings suggest a role of 44-kDa MAP kinase in mediating some of the pleiotropic actions of secretagogues on the pancreatic beta-cell.

AB - The signaling pathways whereby glucose and hormonal secretagogues regulate insulin-secretory function, gene transcription, and proliferation of pancreatic beta-cells are not well defined. We show that in the glucose-responsive beta-cell line INS-1, major secretagogue-stimulated signaling pathways converge to activate 44-kDa mitogen-activated protein (MAP) kinase. Thus, glucose-induced insulin secretion was found to be associated with a small stimulatory effect on 44-kDa MAP kinase, which was synergistically enhanced by increased levels of intracellular cAMP and by the hormonal secretagogues glucagon-like peptide-1 and pituitary adenylate cyclase-activating polypeptide. Activation of 44-kDa MAP kinase by glucose was dependent on Ca2+ influx and may in part be mediated by MEK-1, a MAP kinase kinase. Stimulation of Ca2+ influx by KCl was in itself sufficient to activate 44-kDa MAP kinase and MEK-1. Phorbol ester, an activator of protein kinase C, stimulated 44-kDa MAP kinase by both Ca(2+)-dependent and -independent pathways. Nerve growth factor, independently of changes in cytosolic Ca2+, efficiently stimulated 44-kDa MAP kinase without causing insulin release, indicating that activation of this kinase is not sufficient for secretion. In the presence of glucose, however, nerve growth factor potentiated insulin secretion. In INS-1 cells, activation of 44-kDa MAP kinase was partially correlated with the induction of early response genes junB, nur77, and zif268 but not with stimulation of DNA synthesis. Our findings suggest a role of 44-kDa MAP kinase in mediating some of the pleiotropic actions of secretagogues on the pancreatic beta-cell.

M3 - Journal article

C2 - 7713882

VL - 270

SP - 7882

EP - 7889

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 14

ER -