Bovine adrenal chromaffin cells

Liu PS, Kao LS, Lin MK. 1994. Organophosphates inhibit catecholamine secretion and calcium influx in bovine adrenal chromaffin cell. Toxicology 90 81-91. 

Figure 4. Effect of pardaxin on intracellular ionized calcium level in bovine adrenal chromaffin cells.

Neher, E. and Marty, A. Discrete changes of cell membrane capacitance observed under conditions of enhanced secretion in bovine adrenal chromaffin cells. Proc. Natl Acad. Sci. U.S.A. 79 6712-6716,1982. 

Morita K, Hamano S, Oka M, Teraoka K. (1990). Stimulatory actions of bioflavonoids on tyrosine uptake into cultured bovine adrenal chromaffin cells. Biochem Biophys Res Commun. 171(3) 1199-204. 

Acetylcholine receptor Genistein Daidzein Bovine adrenal chromaffin cells Bovine adrenal medulla Nicotinic antagonist Nicotinic antagonist Matsumura et ah, 2007 Liu et ah, 2007c... 

Matsumura C, Kuwashima H, Soma S, Kimura T. 2007. Effects of genistein and herbimycin, tyrosine kinase inhibitors, on catecholamine release in bovine adrenal chromaffin cells. Auton Autacoid Pharmacol 27 181-187. 

Wenger, B. W., Bryant, D. L., Boyd, R. T., McKay, D. B. Evidence for Spare Nicotinic Acetylcholine Receptors and a P4 Subunit in Bovine Adrenal Chromaffin Cells Studies... 

Terbush DR, Holz RW (1990) Activation of protein kinase C is not required for exocytosis from bovine adrenal chromaffin cells. The effects of protein kinase C(19-31), Ca/CaM kinase 11(291— 317), and staurosporine. J Biol Chem 265 21179-84 Tesmer VM, Kawano T, Shankaranarayanan A et al (2005) Snapshot of activated G proteins at the membrane the Galphaq-GRK2-Gbetagamma complex. Science 310 1686-90 Thakur P, Stevens DR, Sheng ZH et al (2004) Effects of PKA-mediated phosphorylation of Snapin on synaptic transmission in cultured hippocampal neurons. J Neurosci 24 6476-81 Thompson SM, Capogna M, Scanziani M (1993) Presynaptic inhibition in the hippocampus. Trends Neurosci 16 222-7... 

Currie KP, Fox AP (1996) ATP serves as a negative feedback inhibitor of voltage-gated Ca2+ channel currents in cultured bovine adrenal chromaffin cells. Neuron 16 1027-36 Decking UKM, Schlieper G, Kroll K, Schrader J (1997) Hypoxia-induced inhibition of adenosine kinase potentiates cardiac adenosine release. Circ Res 81 154-64 De Lorenzo S, Veggetti M, Muchnik S et al (2006) Presynaptic inhibition of spontaneous acetylcholine release mediated by P2Y receptors at the mouse neuromuscular junction. Neuroscience. 142 71-85... 

Dar, D.E., and Zinder, O. 1998. Catecholamine secretion from bovine adrenal chromaffin cells induced by the dextrorotatory isomer of anatoxin-a. Gen Pharmacol 31, 737-740. 

Molloy, L., Wonnacott, S., Gallagher, T, Brough, P.A., and Livett, B.G. 1995. Anatoxin-a is a potent agonist of the nicotinic acetylcholine receptor of bovine adrenal chromaffin cells. Eur J Pharmacol 289, 447-453. 

Permeabilized secretory cells are widely used to study the final events during secretion by exocytosis. Convenient cellular models are bovine adrenal chromaffin cells in short term culture and the rat pheochromocytoma cell line PC 12. Both cell types take up labeled catecholamines and store them in secretory vesicles, from which they can be released upon stimulation. The released catecholamines can be detected in the supernatant. After permeabilization of the plasma membrane, release of catecholamines can be triggered by micromolar concentrations of Ca. ... 

Results of a representative experiment are given in Table 1. As expected the ATP-dependent uptake is inhibited by reserpine. A similar experimental protocol can be applied to bovine adrenal chromaffin cells attached to culture plates. 

Ahnert-Hilger G, Wegenhorst U, Stecher B etal. (1992) Exocytosis from permeabilized bovine adrenal chromaffin cells is differently modulated by GTPyS and GMPPNHP. Evidence for the involvement of various guanine nucleotide-binding proteins. Biochem. J. 284 321 —326. 

Fohr KJ, Ahnert-Hilger G, Stecher B et al. (1991) GTP and Ca modulate the inositol 1,4,5,-trisphosphate-dependent Ca release in streptolysin O-permeabilized bovine adrenal chromaffin cells. J. Neurochem. 56 665—670. 

Camphor inhibited catecholamine secretion from bovine adrenal chromaffin cells. 

Liu, P. and C. Lin. Phthalates suppress the calcium signaling of nicotinic acetylcholine receptors in bovine adrenal chromaffin cells. Toxicol. Appl. Pharmacol. 183 92—98, 2002. 

Zhou, Z. and Neher, E. (1993). Mobile and immobile calcium buffers in bovine adrenal chromaffin cells. J. Physiol. 469 245-273. 

Wang, H., Regunathan, S., Meeley. M.P., Reis, D.J., 1992. Isolation and characterisation of imidazoline receptor protein from bovine adrenal chromaffin cells. Mol. Pharmacol. 42, 792-801. 

Higuchi, H., Costa, E., Yang, W.-Y.T. (1988) Neuropeptide Y inhibits the acetylcholine-mediated release of catecholamines from bovine adrenal chromaffin cells. Pharmacol. Exp. Ther. 244, 468-474. 

Norenberg, W., Bek, M., Limberger, N., Takeda, K. Illes, P. (1995) Inhibition of nicotininic acetylcholine receptor channels in bovine adrenal chromaffin cells by Y3-type neuropeptide Y receptors via the adenylate cyclase/protein kinase A system. Namyn Schmiedebergs Arch. Pharmacol. 351, 337-347. 

Saadat, S. and Thoenen, H. (1986) Selective induction of tyrosine hydroxylase by cell-cell contact in bovine adrenal chromaffin cells is mimicked by plasma membranes. J. Cell Biol. 103 1991-1997. 

Bieger, S.C., Henkel, A.W. and Unsicker, K. (1995) Localization of basic fibroblast growth factor in bovine adrenal chromaffin cells. J. Neurochem. 64, 1521-1527. 

Duarte CB, Rosario LM, Sena CM, Carvalho AR A toxin fraction (FTX) from the funnel-web spider poison inhibits dihydropyridine-insensitive Ca channels coupled to catecholamine release in bovine adrenal chromaffin cells. J Neurochem 1993 60(3) 908-13. 

Baltazar G, Ladeira I, Carvalho AR Duarte ER Two types of omega-agatoxin FVA-sensitive Ca channels are coupled to adrenaline and noradrenaline release in bovine adrenal chromaffin cells. PflugersArch 1997 434(5) 592-8. 

Engisch KL, Nowycky MC. Calcium dependence of large dense-cored vesicle exocytosis evoked by calcium influx in bovine adrenal chromaffin cells. J Neurosci 1996 16(4) 1359-69. 

Yoshizumi, M. et al.. Mechanism of palytoxin-induced Na influx into cultured bovine adrenal chromaffin cells possible involvement of Na /H exchange system, Neurosci. Lett. 130, 103, 1991. 

Tong, W. and Yeung, E.S., On-column monitoring of secretion of catecholamines from single bovine adrenal chromaffin cells by capillary electrophoresis, J. Neurosci Methods, 76, 193, 1997. 

Sun, L.R., and J.B. Suszkiw. 1994. Pb activates potassium currents in bovine adrenal chromaffin cells. Neurosci. Lett 182(1) 41 3. 

Type Cl and D botulinum neurotoxins as ADP-ribosyl transferases. As shown by Knight et al. (3), type D botulinum neurotoxin was able to inhibit exocytosis in cultured chromaffin cells. Fig. 1 represents the results of our experiments showing the time course of this inhibition. When cultured bovine adrenal chromaffin cells were incubated with type D botulinum neurotoxin, inhibition of acetylcholine-evoked catecholamine release appeared. This inhibition, however, did not occur instantaneously but appeared and increased with days of incubation, suggesting involvement... 

Fig. 1. Geft) Inhibition of acetylcholine-induced catecholamine release by botulinum toxin in cultured adtenal chromaffin cells. Bovine adrenal chromaffin cells were isolated and cultured at a density of 5 x lOVml. After two days of culture, the cells were washed and suspended in a fresh medium containing 20 pg/ml of type D botulinum neurotoxin. After incubation for indicated days, the cells were washed and stimulated 500 with pM acetylcholine. Catecholamines in the media and cells were extracted separately and quantified electrochemically. Catecholamine release is expressed as % of the total amount , acetylcholine-evoked release O, basal release.

D. ASSAY FOR EXOCYTOSIS FROM BOVINE ADRENAL CHROMAFFIN CELLS IN PRIMARY CULTURE... 

Table I gives an example of noradrenaline release from a-toxin- or SLO-permeabilized bovine adrenal chromaffin cells.

The bovine adrenal chromaffin cells used by Wightman et al. typically release roughly 5 attomoles of detectable epinephrine and norepinephrine. Efforts have been made to detect smaller numbers of molecules released via exocytosis to the point where it has been reported that the release of 4700 and 6000 molecules can be detected per event from release of a small portion of transmitter in a vesicle (28, 29). 

The majority of work concerning exocytosis at the single-cell level has been carried out on bovine adrenal chromaffin cells [8,17,19,21a]. However, amperomet-ric studies of exocytosis have also been performed at mast cells [12], pancreatic P-cells [12,22], and of course at PC12 cells. For each of these cell types, the vesicular radii have been shown previously to have a gaussian distribution [12]. As previously discussed, spherical volumes are proportional to the cube of the vesicular radius. Thus, histograms depicting the cubed root of spike areas of the amperometricaUy detected events for each cell type have been found to yield a more gaussian distribution of events, with a relative standard deviation similar to that calculated for the distribution of vesicular radii [12],... 

As for the catalytic activity of TH for substrates other than tyrosine, the catalytic hydroxylation of phenylalanine by TH was reported as early as the 1960s with partially purified enzyme [146-150]. Later it was found that the hydroxylation of phenylalanine is not catalyzed by highly purified TH [143]. However, it was revealed that phenylalanine is almost as good a substrate for highly purified TH as tyrosine itself under certain experimental conditions in vitro [151] and can also be utilized for the biosynthesis of catecholamines in isolated bovine adrenal chromaffin cells [152]. The hydroxylation of L-phenylalanine gives first L-p-tyrosine as the initial product and then DOPA [152]. 

Oheim, M. Naraghi, M. Muller, X. H. Neher, E. Xwo dye two wavelength excitation calcium imaging results from bovine adrenal chromaffin cells. Cell Calcium 1998, 24, 71-84. 

Tsai, C.-C., Yang, C.-C., Shih, P.-Y. et al. 2008. Exocytosis of a single bovine adrenal chromaffin cell The electrical and morphological studies. J. Phys. Chem. B 112 9165-9173. 

Bovine adrenal chromaffin cells were used to demonstrate a new multimicrowell array, shown in Fig. 17, with tiny indium-tin oxide semitransparent disk working electrodes at the bottoms, and with the wells suitably sized to house single cells and monitor quantal exocytosis of dopamine [91]. Disk electrodes 20 pm in diameter were recessed from the surface of an insulating film (SU-8) laminated to a microscope slide glass substrate. Polylysine modification of the ITO surfaces allowed the size-selective capture of individual cells facilitated by gravity. Poly(ethylene glycol) was used to coat the outer surfaces with a hydrophilic. 

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