Abstract
The regulation of protein secretion in exocrine tissues such as the lacrimal gland involves coupling of cell surface receptor activation by neurotransmitters and neuropeptides to the generation of intracellular messengers.1,2 In lacrimal gland, components of the cyclic adenosine 3’, 5’- monophosphate (cAMP) pathway include seven transmembrane receptors whose activation leads to stimulation or inhibition of the effector enzyme adenylyl cyclase and alterations in the intracellular levels of cAMP, as well as alterations in the release of proteins into the tears.2 In virtually all tissues, heterotrimeric G proteins that reversibly bind guanine nucleotides link cell surface receptor activation to adenylyl cyclase and thus are critical components of signal transduction events in the cAMP pathway. In lacrimal gland, experimental evidence for G protein-dependent regulation of adenylyl cyclase includes stimulation of the enzyme by NaF, a direct activator of Gsα, and by guanine 5’-0–3’-thiosphosphate (GTPyS), a non-hydrolyzable analog of GTP.3,4 Vasoactive intestinal peptide (VIP) stimulation of the enzyme is also dependent upon GTP.5 In the work presented here, we have used toxin-catalyzed ADP-ribosylation and immunoreaction with antisera directed against peptide sequences of the a subunits of specific G proteins to identify and characterize the G proteins present in the mammalian lacrimal gland and that mediate lacrimal secretion through transduction of extracellular signals and alterations in adenylyl cyclase activity.
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References
Harper JE Stimulus-secretion coupling: Second messenger-regulated exocytosis. In: Greengard P, Robison GA, eds. Advances in Second Messenger and Phosphoprotein Research. New York: Raven Press; 1988: 193–231.
Dartt DA. Regulation of tear secretion. Adv Exp Med Biol. 1994; 350: 115–119.
Mircheff AK, Conteas CN, Lu CC, Santiago G, Gray M, Lipson LG. Basal-lateral and intra-cellular membrane populations of rat exorbital lacrimal gland. Am JPhysiol. 1983; 245: G133.
Cripps MM, Bennett DJ. Guanine nucleotide binding proteins in the dual regulation of lacrimal function. Invest Ophthalmol Vis Sci. 1992; 33: 3592–3600.
Cripps MM, Bennett DJ. Peptidergic stimulation and inhibition of lacrimal gland adenylate cyclase. Invest Ophthalmol Vis Sci. 1990; 31: 2145–2150.
Meneray MA, Fields TY, Bromberg BB, Moses RL. Morphology and physiologic responsiveness of cultured rabbit lacrimal acini. Invest Ophthalmol Vis Sci. 1994; 35: 4144–4158.
Meneray MA, Bennett DJ. Identification of GTP-binding proteins in lacrimal gland. Invest Ophthalmol Vis Sci. 1995; 36: 1173–1180.
Brown BL, Albano JDM, Ekins RP, Sgherzi AM. A simple and sensitive saturation assay method for the measurement of adenosine 3’,5 -cyclic monophosphate. Biochem J. 1971; 121: 561–562.
Masters SB, Sullivan K, Miller RT, et al. Carboxyl terminal domain of Gsα specifies coupling of receptors to stimulation of adenylyl cyclase. Science. 1988; 241: 448–451.
Bouhelal R, Guillon G, Hornburger V, Bockaert J. Forskolin-induced change of the size of adenylate cyclase. J Biol Chem. 1985; 260: 10901–10904.
Morris D, McHugh-Sutkowski E, Moos M, Simonds WF, Spiegel AM, Seamon KB. Immunoprecipitation of adenylate cyclase with an antibody to a carboxyl-terminal peptide from Gssα. Biochemistry. 1990; 29: 9079–9084.
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Meneray, M.A., Bennett, D.J. (1998). Identification and Characterization of G Proteins in the Mammalian Lacrimal Gland. In: Sullivan, D.A., Dartt, D.A., Meneray, M.A. (eds) Lacrimal Gland, Tear Film, and Dry Eye Syndromes 2. Advances in Experimental Medicine and Biology, vol 438. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5359-5_29
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DOI: https://doi.org/10.1007/978-1-4615-5359-5_29
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