Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.6.1.1 (adenylate cyclase)
 19,190 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The present study was initiated to determine whether specific hormones would influence adenylate cyclase activity within the maxillary-palatal complex during formation of the hamster secondary palate. Stages from initial appearance of the palatal processes to shortly after birth were studied. Highest basal adenylate cyclase activities occurred during the earliest periods of palate development. This basal enzyme activity began to diminish as palatal fusion occurred and remained lowered until birth. Activation of adenylate cyclase by fluoride was maximal at concentrations of 5-10 mM, and was observed throughout the span of palatal development. Fluoride activation of adenylate cyclase was greatest prior to fusion of the palatal processes, then decreased until birth when a slightly increased enzymatic stimulation was seen. Norepinephrine and epinphrine were the catecholamines most capable of inducing increased activation of adenylate cyclase at most periods of palatal growth. Increased enzyme activity in the presence of norepinephrine was more susceptible to antagonism by the beta adrenergic agent, propranolol, than to the alpha adrenergic agent, phentolamine. The remaining catecholamines, namely isoproterenol and dopamine, displayed a lesser ability to activate the enzyme, and adenylate cyclase was not equally responsive to these catecholamines at identical developmental stages. Other hormones, i.e. histamine, serotonin, thyrotropin, growth hormone, thyroxine and glucagon were generally ineffective in activating the enzyme. Phosphodiesterase activity was not detected until shortly before birth.
Anat Rec 1976 Jun
PMID:Catecholamine-sensitive adenylate cyclase in the developing golden hamster palate. 17 49

An adenylate cyclase highly responsive to stimulation by parathyroid hormone (PTH) and calcitonin (CT) in vitro was observed at certain times during normal prenatal development of the maxillary-palatal process complex in the golden hamster. Responses of the enzyme to these hormones were barely detectible at the earliest stage examined (day 10/20). The enzyme became extremely sensitive to activation by either hormone during the time of rapid growth of the palatal processes (day 11/20) and during fusion between the palatal processes (day 12/20). Thereafter, responses were greatly diminished and little or no activation of adenylate cyclase was observed until birth. Adenylate cyclase from fetuses in which clefts of the secondary palate were induced by maternal treatment with hydrocortisone (50 mg) on day 11/3 also displayed an enhanced sensitivity to PTH and CT on day 11/20, but the sensitivity of the enzyme was greatly decreased from that in normal animals during the normal time of palatal fusion (day 12/20) and was barely detectible or absent at the remaining time periods studied (days 13/20 and 14/20). Addition of hydrocortisone to the incubation mixture, either separately or in combination with PTH or CT, did not remarkably affect the response of adenylate cyclase to these hormones. Moreover, the appearance of the adenylate cyclase sensitive to hormonal activation did not result from changes in phosphodiesterase activity during palatal maturation.
Anat Rec 1977 Aug
PMID:In vitro activation of adenylate cyclase by parathyroid hormone and calcitonin during normal and hydrocortisone-induced cleft palate development in the golden hamster. 19 59

A cytochemical study was carried out on adenylate cyclase (AC) activity in the early human placenta. Samples of placental villi were incubated in a medium containing adenylyl-imidodiphosphate (AMP-PNP) as specific substrate. No AC reaction product was encountered in placenta villi taken at 5 and 7 weeks of pregnancy. AC activity appeared at 9 weeks. At 9 and 10 weeks, AC reaction product was localized on the basal plasma membranes and on apposed plasma membranes of the Langhans cytotrophoblast. At 11 weeks AC activity was also clearly visible on Langhans cytotrophoblast and syncytiotrophoblast apposed plasma membranes. No AC reaction product was ever detected on the syncytiotrophoblast microvillar membrane. These results are in agreement with biochemical studies that localize AC on the villous trophoblast plasma membranes associated with the fetal circulation.
Anat Rec 1988 Apr
PMID:Ultracytochemical localization of adenylate cyclase in early human placenta. 338 27

The distribution of adenylate cyclase in testis, by means of a specific substrate adenylyl-imidodiphosphate (AMP-PNP), has been determined. Membrane-associated reaction products, indicative of adenylate cyclase activity, are localized by a complete cytochemical medium (containing 10 mM NaF) at the level of the basal compartment of the seminiferous epithelium, on the basal surface of Sertoli cells, and on adjacent plasma membranes of Sertoli cells and spermatogonial cells. At the level of the adluminal compartment, reaction products were found on adjacent plasma membranes of Sertoli cells and early or elongated spermatids. Adenylate cyclase reaction products are detectable by a basal incubation medium (without 10 mM NaF) only in the adluminal compartment on the spermatid plasma membranes.
Anat Rec 1983 Dec
PMID:Cytochemical study on the distribution of adenylate cyclase in guinea pig testis. 667 Jul 58

In the olfactory organ of the squid, Lolliguncula brevis there are five morphological types of olfactory receptor neurons (ORNs). Previous work to characterize odor sensitivity of squid ORNs was performed on only two of the five types in dissociated primary cell cultures. Here, we sought to establish the odorant responsiveness of all five types. We exposed live squid or intact olfactory organs to excitatory odors plus the activity marker, agmatine (AGB), an arginine derivative that enters cells through nonselective cation channels. An antibody against AGB was used to identify odorant-activated neurons. We were able to determine the ORN types of AGB-labeled cells based on their location in the epithelium, morphology and immunolabeling by a set of metabolites: arginine, aspartate, glutamate, glycine, and glutathione. Of 389 neurons identified from metabolite-labeled tissue, 3% were type 1, 32% type 2, 33% type 3, 15% type 4, and 17% type 5. Each ORN type had different odorant specificity with type 3 cells showing the highest percentages of odorant-stimulated AGB labeling. Type 1 cells were rare and none of the identified type 1 cells responded to the tested odorants, which included glutamate, alanine and AGB. Glutamate is a behaviorally attractive odorant and elicited AGB labeling in types 2 and 3. Glutamate-activated AGB labeling was significantly reduced in the presence of the adenylate cyclase inhibitor, SQ22536 (80 microM). These data suggest that the five ORN types differ in their relative abundance and odor responsiveness and that the adenylate cyclase pathway is involved in squid olfactory transduction.
Anat Rec (Hoboken) 2008 Jul
PMID:Odorant responsiveness of squid olfactory receptor neurons. 1848 2