In vitro activation of adenylate cyclase by parathyroid hormone and calcitonin during normal and hydrocortisoneinduced cleft palate development in the golden hamster

1977 ◽  
Vol 188 (4) ◽  
pp. 431-443 ◽  
Author(s):  
Robert Earle Waterman ◽  
Gene C. Palmer ◽  
S. Jo Palmer ◽  
Susan M. Palmer
Keyword(s):  
Parathyroid Hormone ◽  
Adenylate Cyclase ◽  
Cleft Palate ◽  
Golden Hamster ◽  
Palate Development ◽  
In Vitro Activation

scholarly journals Onset of the acquired potentiality for fusion in the palatal shelves of rats

Development ◽  
1966 ◽  
Vol 16 (1) ◽  
pp. 171-182
Author(s):  
M. Pourtois
Keyword(s):  
Oral Cavity ◽  
Cleft Palate ◽  
Horizontal Plane ◽  
Horizontal Position ◽  
Palate Development

This paper is concerned with that phase of palate development in rats leading to fusion of the shelves in the midline. Previous experimentation in palate development in mammals has encompassed both the earlier phase of assumption of the horizontal position of the palatal shelves, and the subsequent approximation and fusion of the shelves. Since the two processes do not occur simultaneously and can theoretically be studied separately, it was possible and feasible to confine the experiment to the later fusion phase. The present research was designed to eliminate the possible confounding effects of palate rotation in vitro on the fusion of the shelves by approximation of the explanted palatal shelves in the same horizontal plane, irrespective of their original positions in the oral cavity. Current theories of cleft palate pathogenesis hold that either the palatal shelves fail to assume (rotate to) the horizontal position, or, that having done so, they fail to fuse.

scholarly journals In Vitro Activation of Adenylate Cyclase of Atrophic Celiac Intestinal Mucosa by Wheat Gliadin-Derived Peptides

1986 ◽  
Vol 20 (1) ◽  
pp. 42-44 ◽  
Author(s):  
L Beguinot ◽  
S Auricchio ◽  
J E Bernardin ◽  
G De Ritis ◽  
M De Vincenzi ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Intestinal Mucosa ◽  
In Vitro Activation ◽  
Wheat Gliadin

scholarly journals In vitro activation of CMV-specific human CD8+ T cells by adenylate cyclase toxoids delivering pp65 epitopes

2011 ◽  
Vol 47 (2) ◽  
pp. 243-250 ◽  
Author(s):  
J Jelinek ◽  
I Adkins ◽  
Z Mikulkova ◽  
J Jagosova ◽  
R Pacasova ◽  
...  
Keyword(s):  
T Cells ◽  
Adenylate Cyclase ◽  
Cd8 T Cells ◽  
In Vitro Activation

Effects of PTH, calcitonin, and cAMP on calcium transport in rabbit distal nephron segments

1990 ◽  
Vol 259 (3) ◽  
pp. F408-F414 ◽  
Author(s):  
T. Shimizu ◽  
K. Yoshitomi ◽  
M. Nakamura ◽  
M. Imai
Keyword(s):  
Parathyroid Hormone ◽  
Adenylate Cyclase ◽  
Calcium Transport ◽  
Collecting Duct ◽  
Exchange Process ◽  
Cortical Collecting Duct ◽  
Distal Nephron ◽  
Nephron Segments ◽  
Bathing Fluid

Distal nephron segments are heterogenous with respect to adenylate cyclase responses to stimulation with parathyroid hormone (PTH) or calcitonin (CT). We examined effects of these hormones and of 8-(p-chlorophenylthio)-adenosine 3',5'-cyclic monophosphate (CPTcAMP) on net Ca absorption (Jnet Ca2+, pmol.min-1.mm-1) in rabbit distal nephron segments by in vitro microperfusion technique. We studied three segments, including distal convoluted tubule (DCT), connecting tubule (CNT), and cortical collecting duct (CCD). PTH (1 nM) in bath significantly increased Jnet Ca2+ from 2.28 +/- 0.35 to 9.44 +/- 1.13 in CNT, but did not affect Jnet Ca2+ in DCT or CCD. CT (1 nM) in bath significantly increased Jnet Ca2+ from 1.58 +/- 0.29 to 4.45 +/- 1.01 in DCT, whereas it did not affect Jnet Ca2+ either in CNT or in CCD. CPTcAMP (30 microM) in bath significantly increased Jnet Ca2+ from 2.29 +/- 0.42 to 3.97 +/- 0.43 in DCT and from 2.43 +/- 0.18 to 5.83 +/- 0.37 in CNT, but it did not affect Jnet Ca2+ in CCD. When Na+ was removed from bathing fluid or when 0.1 mM ouabain was added to bath, Jnet Ca2+ in both DCT and CNT significantly decreased. Furthermore, stimulatory effects of PTH and CT on Ca2+ absorption in the respective segments were abolished under these conditions. These results suggest that PTH and CT increase Ca2+ absorption in CNT and DCT, respectively, through cAMP-mediated mechanisms. Presence of a basolateral Na(+)-Ca2+ exchange process seems to be a prerequisite for effects of these hormones. However, exact intracellular mechanisms remain uncertain.

scholarly journals In vitro activation of theSaccharomyces cerevisiaeRas/adenylate cyclase system by glucose and some of its analogues

FEBS Letters ◽  
1991 ◽  
Vol 290 (1-2) ◽  
pp. 43-48 ◽  
Author(s):  
Luis Angel Pardo ◽  
Luis Maria Sánchez ◽  
Pedro S. Lazo ◽  
Sofia Ramos
Keyword(s):  
Adenylate Cyclase ◽  
Adenylate Cyclase System ◽  
In Vitro Activation

Effect of Diphosphonates on Adenosine 3′:5′-Cyclic Monophosphate in Mouse Calvaria after Stimulation by Parathyroid Hormone in vitro

1976 ◽  
Vol 50 (6) ◽  
pp. 473-478
Author(s):  
U. Gebauer ◽  
R. G. G. Russell ◽  
M. Touabi ◽  
H. Fleisch
Keyword(s):  
Parathyroid Hormone ◽  
Bone Resorption ◽  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Bone Cells ◽  
Essential Feature ◽  
Cyclic Monophosphate ◽  
Inhibit Bone Resorption ◽  
Mouse Calvaria

1. The diphosphonates, disodium ethane-1-hydroxy-1,1-diphosphonate (EHDP) and disodium dichloromethylene diphosphonate (Cl2MDP), inhibit bone resorption in animals and in explanted bone in tissue culture. The possibility that these effects might be due to inhibition of skeletal adenylate cyclase has been studied. 2. EHDP and Cl2MDP, added for 30 mm to the incubation medium at concentrations known to inhibit bone resorption, had no effect on basal content of adenosine 3′:5′-cyclic monophosphate (cyclic AMP) of mouse calvaria incubated in vitro, nor did they inhibit the rise in cyclic AMP induced by bovine parathyroid hormone. 3. Pretreatment of mice for 3 days with Cl2MDP also had no effect on cyclic AMP under basal conditions or after incubation of explanted calvaria with parathyroid hormone in vitro. EHDP under similar conditions slightly inhibited the increase induced by parathyroid hormone but had no effect on basal concentrations of cyclic AMP. 4. It is suggested that the inhibition of adenylate cyclase is not an essential feature of the reduction of bone resorption by diphosphonates, which may act by direct inhibitory effects on the dissolution of hydroxyapatite and perhaps by other unidentified effects on bone cells.

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).

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