Stimulation of glucose oxidation in rat submandibular gland cells in vitro by analogues of cyclic AMP

1985 ◽  
Vol 30 (9) ◽  
pp. 701-703
Author(s):  
B.L. Kuyatt ◽  
G.S. Roth ◽  
B.J. Baum
Keyword(s):  
Cyclic Amp ◽  
Submandibular Gland ◽  
Glucose Oxidation ◽  
Gland Cells ◽  
Rat Submandibular Gland ◽  
Stimulation Of

Cytochemical Evidence for Presynatic β-Adrenergic Regulation of Secretion in the Developing Rat Submandibular Gland

1977 ◽  
Vol 35 ◽  
pp. 430-431
Author(s):  
L.S. Cutler
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Submandibular Gland ◽  
Neonatal Rat ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Parotid Glands ◽  
Adrenergic Agonist ◽  
Rat Submandibular Gland

Many studies previously have shown that the B-adrenergic agonist isoproterenol and the a-adrenergic agonist norepinephrine will stimulate secretion by the adult rat submandibular (SMG) and parotid glands. Recent data from several laboratories indicates that adrenergic agonists bind to specific receptors on the secretory cell surface and stimulate membrane associated adenylate cyclase activity which generates cyclic AMP. The production of cyclic AMP apparently initiates a cascade of events which culminates in exocytosis. During recent studies in our laboratory it was observed that the adenylate cyclase activity in plasma membrane fractions derived from the prenatal and early neonatal rat submandibular gland was retractile to stimulation by isoproterenol but was stimulated by norepinephrine. In addition, in vitro secretion studies indicated that these prenatal and neonatal glands would not secrete peroxidase in response to isoproterenol but would secrete in response to norepinephrine. In contrast to these in vitro observations, it has been shown that the injection of isoproterenol into the living newborn rat results in secretion of peroxidase by the SMG (1).

scholarly journals In vitro secretion of immunoreactive tonin from dispersed rat submandibular gland cells.

Hypertension ◽  
1986 ◽  
Vol 8 (10) ◽  
pp. 883-889 ◽  
Author(s):  
Y Hirata ◽  
M Tomita ◽  
T Fujita ◽  
M Ikeda
Keyword(s):  
Submandibular Gland ◽  
Gland Cells ◽  
Rat Submandibular Gland

scholarly journals Potassium (86Rb+) efflux from the rat submandibular gland under sodium-free conditions in vitro.

1989 ◽  
Vol 416 (1) ◽  
pp. 503-515 ◽  
Author(s):  
D L Bovell ◽  
H Y Elder ◽  
J D Pediani ◽  
S M Wilson
Keyword(s):  
Submandibular Gland ◽  
Rat Submandibular Gland

scholarly journals Interactions between adenylate cyclase and the yeast GTPase-activating protein IRA1.

1991 ◽  
Vol 11 (9) ◽  
pp. 4591-4598 ◽  
Author(s):  
M R Mitts ◽  
J Bradshaw-Rouse ◽  
W Heideman
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Adenylate Cyclase System ◽  
Gtpase Activating Protein ◽  
Yeast Saccharomyces Cerevisiae ◽  
Strong Candidate ◽  
Sepharose 4B ◽  
Stimulation Of ◽  
Cyclic Amp Synthesis

The adenylate cyclase system of the yeast Saccharomyces cerevisiae contains many proteins, including the CYR1 polypeptide, which is responsible for catalyzing the formation of cyclic AMP from ATP, RAS1 and RAS2 polypeptides, which mediate stimulation of cyclic AMP synthesis by guanine nucleotides, and the yeast GTPase-activating protein analog IRA1. We have previously reported that adenylate cyclase is only peripherally bound to the yeast membrane. We have concluded that IRA1 is a strong candidate for a protein involved in anchoring adenylate cyclase to the membrane. We base this conclusion on the following criteria: (i) a disruption of the IRA1 gene produced a mutant with very low membrane-associated levels of adenylate cyclase activity, (ii) membranes made from these mutants were incapable of binding adenylate cyclase in vitro, (iii) IRA1 antibodies inhibit binding of adenylate cyclase to the membrane, and (iv) IRA1 and adenylate cyclase comigrate on Sepharose 4B.

Intercellular contacts at the epithelial—mesenchymal interface of the developing rat submandibular gland in vitro

Development ◽  
1977 ◽  
Vol 39 (1) ◽  
pp. 71-77
Author(s):  
Leslie S. Cutler
Keyword(s):  
Electron Microscopy ◽  
Submandibular Gland ◽  
Functional Differentiation ◽  
Developmental Sequence ◽  
Millipore Filter ◽  
Intercellular Contacts ◽  
Rat Submandibular Gland ◽  
Developing Rat

An ultrastructural study of the development of the rat submandibular gland (SMG) anlage in vitro was undertaken to determine if epithelial-mesenchymal and epithelial-nerve contacts were integral events in the differentiation of the gland in vitro as they are in vivo. SMG rudiments were removed at the stalk-bulb stage (15 days in utero) and cultured for 6 days on a millipore filter in supplemented McCoy's 5A media. Rudiments were taken at daily intervals, fixed and processed for electron microscopy. The overall development of the explanted rudiments closely paralleled their maturation in vivo although cultured glands lagged 24–36 h behind their normal counterparts. Direct epithelial-mesenchymal contacts were seen after the morphogenetic patterning of the gland had been established but prior to functional differentiation of the rudiment. Epithelial-nerve contacts were not seen although healthy axons were seen in the stroma throughout the culture period. The study indicates that epithelial-nerve contacts are probably not required for morphogenesis of cytodifferentiation of the rat SMG. However, direct epithelial-mesenchymal contacts appear to be an integral part of the developmental sequence of the rat SMG.

Possible role of cyclic GMP in stimulus-secretion coupling by salt gland of the duck

1979 ◽  
Vol 237 (5) ◽  
pp. C200-C204 ◽  
Author(s):  
D. J. Stewart ◽  
J. Sax ◽  
R. Funk ◽  
A. K. Sen
Keyword(s):  
Cyclic Amp ◽  
Guanylate Cyclase ◽  
Cyclic Gmp ◽  
Salt Gland ◽  
Domestic Ducks ◽  
Stimulus Secretion Coupling ◽  
Stimulation Of

Stimulation of salt galnd secretion in domestic ducks in vivo increased the cyclic GMP concentration of the tissue, but had no effect on cyclic AMP levels. Methacholine, which is known to stimulate sodium transport by the glands both in vivo and in vitro, stimulated ouabain-sensitive respiration in salt gland slices. Cyclic GMP stimulated ouabain-sensitive respiration to the same extent as methacholine. Guanylate cyclase stimulators, hydroxylamine and sodium azide, also stimulated ouabain-sensitive respiration. The stimulation of ouabain-sensitive respiration by methacholine was blocked either by atropine or by removal of calcium from the incubation medium. The stimulation of ouabain-sensitive respiration by cyclic GMP still occurred in the absence of calcium. The above observations seem to indicate that cyclic GMP acts as a tertiary link in the process of stimulus-secretion coupling in the tissue.

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