Effect of bitter compounds on amylase secretion in murine submandibular glands: Signaling pathway mechanisms

Background: Amylase is synthesized in submandibular glands (SMG) and released into the oral cavity to degrade carbohydrates in the mouth. Bitter taste receptors (T2R) belong to the G-protein coupled receptor (GPCR) family and are expressed in the taste cells and also in the digestive tract. Methods:...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autor principal: Dasso, M.
Otros Autores: Pagotto, R., Pignataro, O.P, Diez, R.A, Sales, M.E
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2011
Acceso en línea:Registro en Scopus
DOI
Handle
Registro en la Biblioteca Digital
Aporte de:Registro referencial: Solicitar el recurso aquí
LEADER 13590caa a22013937a 4500
001 PAPER-10129
003 AR-BaUEN
005 20230518204008.0
008 190411s2011 xx ||||fo|||| 00| 0 eng|d
024 7 |2 scopus  |a 2-s2.0-80054998442 
024 7 |2 cas  |a amylase, 9000-90-2, 9000-92-4, 9001-19-8; cyclic AMP, 60-92-4; cycloheximide, 642-81-9, 66-81-9; denatonium benzoate, 3734-33-6; inositol phosphate, 15421-51-9; theophylline, 58-55-9, 5967-84-0, 8055-07-0, 8061-56-1, 99007-19-9; Amylases, 3.2.1.-; Cyclic AMP, 60-92-4 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a BBGSB 
100 1 |a Dasso, M. 
245 1 0 |a Effect of bitter compounds on amylase secretion in murine submandibular glands: Signaling pathway mechanisms 
260 |c 2011 
270 1 0 |m Sales, M.E.; Centro de Estudios Farmacológicos y Botánicos (CEFYBO)-CONICET, Facultad de Medicina, Universidad de Buenos Aires, Paraguay 2155 piso 16 sector der. CP 1121, Buenos Aires, Argentina; email: msales@fmed.uba.ar 
506 |2 openaire  |e Política editorial 
504 |a Castle, D., Castle, A., Intracellular transport and secretion of salivary proteins (1998) Critical Reviews in Oral Biology and Medicine, 9 (1), pp. 4-22 
504 |a Barka, T., Biologically active polypeptides in submandibular glands (1980) Journal of Histochemistry and Cytochemistry, 28 (8), pp. 836-859 
504 |a Braum, B.J., Principles of saliva secretion (1993) Ann. N. Y. Acad. Sci., 694, pp. 17-23 
504 |a Butcher, F.R., Putney, Jr.J.W., Regulation of parotid gland function by cyclic nucleotides and calcium (1980) Adv. Cyclic Nucleotide Res., 13, pp. 215-249 
504 |a Chandrashekar, J., Mueller, K.L., Hoon, M.A., Adler, E., Feng, L., Guo, W., Zuker, C.S., Ryba, N.J.P., T2Rs function as bitter taste receptors (2000) Cell, 100, pp. 703-711 
504 |a Yan, W., Sunavala, G., Rosenzweig, S., Dasso, M., Brand, J.G., Spielman, A.I., Bitter taste transduced by PLCβ2-dependent rise in IP 3 and α-gustducin-dependent fall in cyclic nucleotides (2001) Am. J. Physiol. Cell Physiol., 280, pp. 742-C751 
504 |a Spielman, A.I., Nagai, H., Sunavala, G., Dasso, M., Breer, H., Boekhoff, I., Huque, T., Brand, J.G., Rapid kinetics of second messenger production in bitter taste (1996) Am. J. Physiol. Cell Physiol., 270, pp. 926-C931 
504 |a Rosenzweig, S., Yan, W., Dasso, M., Spielman, A.I., Possible novel mechanism for bitter taste mediated through cGMP (1999) Journal of Neurophysiology, 81 (4), pp. 1661-1665 
504 |a Wu, S.V., Rozengurt, N., Yang, M., Young, S.H., Sinnett-Smith, J., Rozengurt, E., Expression of bitter taste receptors of the T2R family in the gastrointestinal tract and enteroendocrine STC-1 cells (2002) Proceedings of the National Academy of Sciences of the United States of America, 99 (4), pp. 2392-2397. , DOI 10.1073/pnas.042617699 
504 |a Spielman, A.I., Huque, T., Whitney, G., Brand, J.G., The diversity of bitter taste signal transduction mechanisms (1992) Soc. Gen. Physiol. Ser., 47, pp. 307-324 
504 |a Espanol, A.J., Sales, M.E., Parasympathetic modulation of amylase secretion by IFNγ in murine submandibular glands (2001) International Immunopharmacology, 1 (5), pp. 903-910. , DOI 10.1016/S1567-5769(01)00026-1, PII S1567576901000261 
504 |a Bradford, M.M., A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254 
504 |a Mondillo, C., Pagotto, R.M., Piotrkowski, B., Reche, C.G., Patrignani, Z.J., Cymeryng, C.B., Pignataro, O.P., Involvement of nitric oxide synthase in the mechanism of histamine-induced inhibition of Leydig cell steroidogenesis via histamine receptor subtypes in Sprague-Dawley rats (2009) Biol. Reprod., 80, pp. 144-152 
504 |a Turner, R.J., Sugiya, H., Understanding salivary fluid and protein secretion (2002) Oral Diseases, 8 (1), pp. 3-11. , DOI 10.1034/j.1601-0825.2002.10815.x 
504 |a Tandler, B., Gresik, E.W., Nagato, T., Phillips, C.J., Secretion by striated ducts of mammalian major salivary glands: Review from an ultrastructural, functional, and evolutionary perspective (2001) Anatomical Record, 264 (2), pp. 121-145. , DOI 10.1002/ar.1108 
504 |a Quissell, D.O., Stimulus-exocytosis coupling mechanism in salivary gland cells (1993) Biology of the Salivary Glands, pp. 181-200. , K. Dobrosielski-Vergona, CRC Press Florida 
504 |a Chrétien, M., Zajdela, F., Histochemical demonstration of amylase secretion in the submaxillary, retrolingual and subparotid salivary glands in mice (1965) C. R. Acad. Sci. Hebd. Seances Acad. Sci. D, 260, pp. 4263-4266 
504 |a Barka, T., Gresik, E.W., Van Der Noen, H., Stimulation of secretion of epidermal growth factor and amylase by cyclocytidine (1978) Cell and Tissue Research, 186 (2), pp. 269-278 
504 |a Ozek, M., Brust, P., Xu, H., Servant, G., Receptors for bitter, sweet and umami taste couple to inhibitory G protein signaling pathways (2003) Eur. J. Pharmacol., 489, pp. 130-149 
504 |a Laska, M., Rivas Bautista, R.M., Hernandez Salazar, L.T., Gustatory responsiveness to six bitter tastants in three species of nonhuman primates (2009) J. Chem. Ecol., 35, pp. 560-571 
504 |a Mueller, K.L., Hoon, M.A., Erlenbach, I., Chandrashekar, J., Zuker, C.S., Ryba, N.J.P., The receptors and coding logic for bitter taste (2005) Nature, 434 (7030), pp. 225-229. , DOI 10.1038/nature03352 
504 |a Margolskee, R.F., Molecular mechanisms of bitter and sweet taste transduction (2002) Journal of Biological Chemistry, 277 (1), pp. 1-4. , DOI 10.1074/jbc.R100054200 
504 |a Clapp, T.R., Trubey, K.R., Vandenbeuch, A., Stone, L.M., Margolskee, R.F., Chaudari, N., Kinnamon, S.C., Tonic activity of Gα-gustducin regulates taste cell responsivity (2008) FEBS Lett., 582, pp. 3783-3787 
504 |a Ueda, T., Ugawa, S., Yamamura, H., Imaizumi, Y., Shimada, S., Functional interaction between T2R taste receptors and G-protein α subunits expressed in taste receptor cells (2003) J. Neurosci., 23, pp. 7376-7379 
504 |a Caicedo, A., Pereira, E., Margolskee, R.F., Roper, S.D., Role of the G-Protein Subunit α-Gustducin in Taste Cell Responses to Bitter Stimuli (2003) Journal of Neuroscience, 23 (30), pp. 9947-9952 
504 |a Socorro, L., Alexander, R.W., Griendling, K.K., Cholera toxin modulation of angiotensin II-stimulated inositol phosphate production in cultured vascular smooth muscle cells (1990) Biochemical Journal, 265 (3), pp. 799-807 
504 |a Keularts, I.M.L.W., Van Gorp, R.M.A., Feijge, M.A.H., Vuist, W.M.J., Heemskerk, J.W.M., α(2A)-Adrenergic receptor stimulation potentiates calcium release in platelets by modulating cAMP levels (2000) Journal of Biological Chemistry, 275 (3), pp. 1763-1772. , DOI 10.1074/jbc.275.3.1763 
504 |a Campos-Toimil, M., Keravis, T., Orallo, F., Takeda, K., Lugnier, C., Short-term or long-term treatments with a phosphodiesterase-4 (PDE4) inhibitor result in opposing agonist-induced Ca 2+ responses in endothelial cells (2008) British Journal of Pharmacology, 154 (1), pp. 82-92. , DOI 10.1038/bjp.2008.56, PII BJP200856 
504 |a Ito, K., Lim, S., Caramori, G., Cosio, B., Chung, K.F., Adcock, I.M., Barnes, P.J., A molecular mechanism of action of theophylline: Induction of histone deacetylase activity to decrease inflammatory gene expression (2002) Proceedings of the National Academy of Sciences of the United States of America, 99 (13), pp. 8921-8926. , DOI 10.1073/pnas.132556899 
504 |a Dotson, C.D., Vigues, S., Steinle, N.I., Munger, S.D., T1R and T2R receptors: The modulation of incretin hormone and potential targets for the treatment of type 2 diabetes mellitus (2010) Curr. Opin. Investig. Drugs, 11, pp. 447-454 
520 3 |a Background: Amylase is synthesized in submandibular glands (SMG) and released into the oral cavity to degrade carbohydrates in the mouth. Bitter taste receptors (T2R) belong to the G-protein coupled receptor (GPCR) family and are expressed in the taste cells and also in the digestive tract. Methods: The activity of amylase secreted by murine SMG was measured, detecting maltose by Bernfeld's method. Amylase and T2R6 were detected by imunohistochemistry and Western blot. The expression of Ggustducin, Gi, and phospholipase Cβ2 was also studied by Western blot. cAMP levels were measured by radioimmunoassay and inositol monophosphate production was quantified by ELISA. Results: Theophylline, denatonium and cycloheximide exerted a dose-dependent inhibition on amylase secretion. This effect was reverted by preincubating SMG with an anti-Gαi antibody. cAMP production was increased by the same compounds, an effect that was also abrogated by an anti-Gαi antibody. Bitter compounds reduced inositol monophosphate formation in SMG and H-89, a protein kinase A inhibitor, reverted this action, revealing that this protein kinase down regulates phospholipase C activity. General significance: We demonstrated that theophylline, denatonium and cycloheximide inhibit salivary amylase secretion, activating an intracellular signaling pathway that involves cAMP and phospholipase C, that cross talks via protein kinase A. © 2011 Elsevier B.V.  |l eng 
536 |a Detalles de la financiación: National Science and Technology Development Agency 
536 |a Detalles de la financiación: Universidad de Buenos Aires, UBACyT M064 
536 |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica, PICT 2006–485 
536 |a Detalles de la financiación: The authors wish to thank Drs. Maria P. Cecchini, Flavia Merigo and Andrea Sbarbati from the Dipartimento di Scienze Morfologico-Biomediche, Sezione di Anatomia e Istologia, Universitá degli Studi di Verona, Italy, where the immunohistochemistry slides were developed. Also our special thanks to Mrs. María Esther Castro for her skillful technical assistance in mice surgical procedures and Drs. Eulalia de la Torre, Alejandro Español and Ganna Dmytrenko for their help and observations on the different experimental techniques employed. This research was funded in part by Fundación Conamed; University of Buenos Aires grant UBACyT M064 and the National Agency for the Promotion of Science and Technology (ANPCyT) grant PICT 2006–485 . 
593 |a Centro de Estudios Farmacológicos y Botánicos (CEFYBO)-CONICET, Facultad de Medicina, Universidad de Buenos Aires, Paraguay 2155 piso 16 sector der. CP 1121, Buenos Aires, Argentina 
593 |a Instituto de Biología y Medicina Experimental (IBYME)-CONICET, Buenos Aires, Argentina 
593 |a Dpto. de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina 
593 |a Cátedra de Farmacología, Facultad de Medicina, Universidad de Buenos Aires, Buenos Aires, Argentina 
690 1 0 |a AMYLASE 
690 1 0 |a BITTER AGONIST 
690 1 0 |a CAMP 
690 1 0 |a GI PROTEIN 
690 1 0 |a INOSITOL MONOPHOSPHATE 
690 1 0 |a PROTEIN KINASE A 
690 1 0 |a AMYLASE 
690 1 0 |a CYCLIC AMP 
690 1 0 |a CYCLIC AMP DEPENDENT PROTEIN KINASE 
690 1 0 |a CYCLOHEXIMIDE 
690 1 0 |a DENATONIUM BENZOATE 
690 1 0 |a GUANINE NUCLEOTIDE BINDING PROTEIN 
690 1 0 |a GUSTDUCIN 
690 1 0 |a INHIBITORY GUANINE NUCLEOTIDE BINDING PROTEIN 
690 1 0 |a INOSITOL PHOSPHATE 
690 1 0 |a PHOSPHOLIPASE C BETA2 
690 1 0 |a THEOPHYLLINE 
690 1 0 |a UNCLASSIFIED DRUG 
690 1 0 |a ANIMAL TISSUE 
690 1 0 |a ARTICLE 
690 1 0 |a BITTER TASTE 
690 1 0 |a CONTROLLED STUDY 
690 1 0 |a ENZYME ACTIVITY 
690 1 0 |a ENZYME INHIBITION 
690 1 0 |a ENZYME LINKED IMMUNOSORBENT ASSAY 
690 1 0 |a ENZYME LOCALIZATION 
690 1 0 |a ENZYME RELEASE 
690 1 0 |a IMMUNOHISTOCHEMISTRY 
690 1 0 |a MOUSE 
690 1 0 |a NONHUMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROTEIN EXPRESSION 
690 1 0 |a PROTEIN FUNCTION 
690 1 0 |a QUANTITATIVE ANALYSIS 
690 1 0 |a RADIOIMMUNOASSAY 
690 1 0 |a SIGNAL TRANSDUCTION 
690 1 0 |a SUBMANDIBULAR GLAND 
690 1 0 |a TASTE BUD 
690 1 0 |a WESTERN BLOTTING 
690 1 0 |a AMYLASES 
690 1 0 |a ANIMALS 
690 1 0 |a BLOTTING, WESTERN 
690 1 0 |a CYCLIC AMP 
690 1 0 |a IMMUNOHISTOCHEMISTRY 
690 1 0 |a MICE 
690 1 0 |a MICE, INBRED BALB C 
690 1 0 |a SIGNAL TRANSDUCTION 
690 1 0 |a SUBMANDIBULAR GLAND 
690 1 0 |a MURINAE 
700 1 |a Pagotto, R. 
700 1 |a Pignataro, O.P. 
700 1 |a Diez, R.A. 
700 1 |a Sales, M.E. 
773 0 |d 2011  |g v. 1810  |h pp. 1212-1219  |k n. 12  |p Biochim. Biophys. Acta Gen. Subj.  |x 03044165  |w (AR-BaUEN)CENRE-2260  |t Biochimica et Biophysica Acta - General Subjects 
856 4 1 |u https://www.scopus.com/inward/record.uri?eid=2-s2.0-80054998442&doi=10.1016%2fj.bbagen.2011.08.009&partnerID=40&md5=d256402dea0ae057ccf7f16b102f1503  |y Registro en Scopus 
856 4 0 |u https://doi.org/10.1016/j.bbagen.2011.08.009  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_03044165_v1810_n12_p1212_Dasso  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03044165_v1810_n12_p1212_Dasso  |y Registro en la Biblioteca Digital 
961 |a paper_03044165_v1810_n12_p1212_Dasso  |b paper  |c PE 
962 |a info:eu-repo/semantics/article  |a info:ar-repo/semantics/artículo  |b info:eu-repo/semantics/publishedVersion 
963 |a VARI 
999 |c 71082