Topic
Cyclase
About: Cyclase is a research topic. Over the lifetime, 10162 publications have been published within this topic receiving 388566 citations.
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TL;DR: The results show that the hormone receptor proteins are separate from the adenyl cyclase, a finding which indicates at least two types of membrane bound epinephrine.
126 citations
TL;DR: The results suggest that activation of ADPR cyclase is an early ABA-signaling event partially insensitive to the abi1-1 mutation and that an increase in cADPR plays an important role in downstream molecular and physiological ABA responses.
Abstract: Cyclic ADP-ribose (cADPR) was previously shown to activate transient expression of two abscisic acid (ABA)-responsive genes in tomato cells. Here, we show that the activity of the enzyme responsible for cADPR synthesis, ADP-ribosyl (ADPR) cyclase, is rapidly induced by ABA in both wild-type (WT) and abi1-1 mutant Arabidopsis plants in the absence of protein synthesis. Furthermore, in transgenic Arabidopsis plants, induced expression of the Aplysia ADPR cyclase gene resulted in an increase in ADPR cyclase activity and cADPR levels, as well as elevated expression of ABA-responsive genes KIN2, RD22, RD29a, and COR47 (although to a lesser extent than after ABA induction). Genome-wide profiling indicated that about 28% of all ABA-responsive genes in Arabidopsis are similarly up- and downregulated by cADPR and contributed to the identification of new ABA-responsive genes. Our results suggest that activation of ADPR cyclase is an early ABA-signaling event partially insensitive to the abi1-1 mutation and that an increase in cADPR plays an important role in downstream molecular and physiological ABA responses.
126 citations
TL;DR: It is suggested that the protein CaM-BP80 may have a role in the cerebrum at the site of neurotransmitter action and at the level of microtubular function in bovine brain.
Abstract: Bovine brain contains a heat-labile, 80,000-dalton calmodulin-binding protein (CaM-BP80) which inhibits the calmodulin-dependent activities of cyclic 3',5'-nucleotide phosphodiesterase, adenylate cyclase, and Ca2+-ATPase in vitro. CaM-BP80 is composed of two polypeptides (60,000 and 18,500 daltons) present in a 1:1 ratio. An antibody directed against CaM-BP80 was raised in rabbits, and a radioimmunoassay was developed, having a sensitivity of 60 fmol of CaM-BP80. Using the radioimmunoassay, we determined the levels of CaM-BP80 in various bovine tissues. The protein was found primarily in the brain, present in particularly high levels in the neostriatum. These results, together with immunohistochemical localization of CaM-BP80 at the postsynaptic densities and the microtubules of postsynaptic dendrites [Wood, J.G., Wallace, R., Whitaker, J., & Cheung, W.Y. (1980) J. Cell Biol. 84, 66-76], suggest that the protein may have a role in the cerebrum at the site of neurotransmitter action and at the level of microtubular function.
125 citations
125 citations
TL;DR: GTP caused stimulation of adenylate cyclase in myocardial membranes, was virtually without effect in frog erythrocytes and resulted in inhibition in adipose membranes, and ability to competitively antagonize stimulation by Gpp(NH)p provided a convenient way of assessing the relative affinities of nucleotides for the regulatory sites.
125 citations