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Epidermal growth factor inhibits bombesin-induced activation of phospholipase C-beta1 in rat pancreatic acinar cells. 1997

A Piiper, and D Stryjek-Kaminska, and R Klengel, and S Zeuzem
II Medical Department, University of Frankfurt, Germany.

OBJECTIVE Epidermal growth factor (EGF) inhibits bombesin-induced activation of phosphoinositide-specific phospholipase C (PLC) in pancreatic acini. The aim of this study was to investigate the mechanism by which EGF inhibits bombesin-induced activation of PLC. METHODS Intact pancreatic acini were pretreated with pertussis toxin to study the role of Gi/o-type heterotrimeric guanosine triphosphate-binding regulatory proteins (G proteins) in EGF-induced modulation of PLC activity. To identify the PLC isoenzyme(s) and Gi/o protein subtype(s) involved in EGF-induced signaling, PLC activity was measured in isolated pancreatic acinar membranes that had been preincubated with immunoneutralizing antibodies raised against various PLC-beta isoenzymes or G protein alpha-subunits. The association of PLC-beta1 and Gi/o-type G proteins was studied by pertussis toxin-catalyzed [32P]adenosine diphosphate ribosylation of PLC-beta1 immunoprecipitates. RESULTS Pertussis toxin pretreatment of pancreatic acini abolished the inhibitory effect of EGF on bombesin-induced PLC activation and amylase release. Anti-PLC-beta1, -beta3, and Gq/11alpha antibodies inhibited bombesin-induced PLC activity by 50%, 35%, and 65%, respectively. Anti-Gi1-2alpha, but not a Gi3alpha-specific antibody, abolished the inhibitory effect of EGF on bombesin-induced PLC activity. Pertussis toxin-sensitive G proteins coimmunoprecipitated with PLC-beta1 in an EGF-dependent fashion. CONCLUSIONS EGF inhibits bombesin-induced activation of PLC-beta1 by a mechanism involving activation of Gi1-2 proteins in pancreatic acinar membranes.

UI MeSH Term Description Entries
D008245 Lysophospholipase An enzyme that catalyzes the hydrolysis of a single fatty acid ester bond in lysoglycerophosphatidates with the formation of glyceryl phosphatidates and a fatty acid. EC 3.1.1.5. Lecithinase B,Lysolecithinase,Phospholipase B,Lysolecithin-Lysolecithin Acyltransferase,Lysophospholipase A,Lysophospholipase A1,Lysophospholipase C,Lysophospholipase L2,Acyltransferase, Lysolecithin-Lysolecithin,L2, Lysophospholipase,Lysolecithin Lysolecithin Acyltransferase
D008297 Male Males
D010179 Pancreas A nodular organ in the ABDOMEN that contains a mixture of ENDOCRINE GLANDS and EXOCRINE GLANDS. The small endocrine portion consists of the ISLETS OF LANGERHANS secreting a number of hormones into the blood stream. The large exocrine portion (EXOCRINE PANCREAS) is a compound acinar gland that secretes several digestive enzymes into the pancreatic ductal system that empties into the DUODENUM.
D010566 Virulence Factors, Bordetella A set of BACTERIAL ADHESINS and TOXINS, BIOLOGICAL produced by BORDETELLA organisms that determine the pathogenesis of BORDETELLA INFECTIONS, such as WHOOPING COUGH. They include filamentous hemagglutinin; FIMBRIAE PROTEINS; pertactin; PERTUSSIS TOXIN; ADENYLATE CYCLASE TOXIN; dermonecrotic toxin; tracheal cytotoxin; Bordetella LIPOPOLYSACCHARIDES; and tracheal colonization factor. Bordetella Virulence Factors,Agglutinogen 2, Bordetella Pertussis,Bordetella Virulence Determinant,LFP-Hemagglutinin,LP-HA,Leukocytosis-Promoting Factor Hemagglutinin,Lymphocytosis-Promoting Factor-Hemagglutinin,Pertussis Agglutinins,Agglutinins, Pertussis,Determinant, Bordetella Virulence,Factor Hemagglutinin, Leukocytosis-Promoting,Factor-Hemagglutinin, Lymphocytosis-Promoting,Factors, Bordetella Virulence,Hemagglutinin, Leukocytosis-Promoting Factor,LFP Hemagglutinin,LP HA,Leukocytosis Promoting Factor Hemagglutinin,Lymphocytosis Promoting Factor Hemagglutinin,Virulence Determinant, Bordetella
D010738 Type C Phospholipases A subclass of phospholipases that hydrolyze the phosphoester bond found in the third position of GLYCEROPHOSPHOLIPIDS. Although the singular term phospholipase C specifically refers to an enzyme that catalyzes the hydrolysis of PHOSPHATIDYLCHOLINE (EC 3.1.4.3), it is commonly used in the literature to refer to broad variety of enzymes that specifically catalyze the hydrolysis of PHOSPHATIDYLINOSITOLS. Lecithinase C,Phospholipase C,Phospholipases, Type C,Phospholipases C
D001839 Bombesin A tetradecapeptide originally obtained from the skins of toads Bombina bombina and B. variegata. It is also an endogenous neurotransmitter in many animals including mammals. Bombesin affects vascular and other smooth muscle, gastric secretion, and renal circulation and function. Bombesin 14,Bombesin Dihydrochloride,Dihydrochloride, Bombesin
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D004815 Epidermal Growth Factor A 6-kDa polypeptide growth factor initially discovered in mouse submaxillary glands. Human epidermal growth factor was originally isolated from urine based on its ability to inhibit gastric secretion and called urogastrone. Epidermal growth factor exerts a wide variety of biological effects including the promotion of proliferation and differentiation of mesenchymal and EPITHELIAL CELLS. It is synthesized as a transmembrane protein which can be cleaved to release a soluble active form. EGF,Epidermal Growth Factor-Urogastrone,Urogastrone,Human Urinary Gastric Inhibitor,beta-Urogastrone,Growth Factor, Epidermal,Growth Factor-Urogastrone, Epidermal,beta Urogastrone
D000681 Amylases A group of amylolytic enzymes that cleave starch, glycogen, and related alpha-1,4-glucans. (Stedman, 25th ed) EC 3.2.1.-. Diastase,Amylase
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

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