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Artigos de revistas sobre o tema "Chromaffin cells"

Autor: Grafiati

Publicado: 4 de junho de 2021

Última modificação: 27 de janeiro de 2023

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1

Coupland, R. E. "MAST CELLS AND CHROMAFFIN CELLS." Annals of the New York Academy of Sciences 103, no. 1 (December 15, 2006): 139–50. http://dx.doi.org/10.1111/j.1749-6632.1963.tb53694.x.

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2

Shepherd, S. P., and M. A. Holzwarth. "Chromaffin-adrenocortical cell interactions: effects of chromaffin cell activation in adrenal cell cocultures." American Journal of Physiology-Cell Physiology 280, no. 1 (January 1, 2001): C61—C71. http://dx.doi.org/10.1152/ajpcell.2001.280.1.c61.

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Although the adrenal cortex and medulla are both involved in the maintenance of homeostasis and stress response, the functional importance of intra-adrenal interactions remains unclear. When primary cocultures of frog ( Rana pipiens) adrenocortical and chromaffin cells were used, selective chromaffin cell activation dramatically affected both chromaffin and adrenocortical cells. Depolarization with 50 μm veratridine enhanced chromaffin cell neuronal phenotype, contacts with adrenocortical cells, and secretion of norepinephrine, epinephrine, and serotonin. Time-lapse video microscopy recorded t

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3

Furlan, Alessandro, Vyacheslav Dyachuk, Maria Eleni Kastriti, Laura Calvo-Enrique, Hind Abdo, Saida Hadjab, Tatiana Chontorotzea, et al. "Multipotent peripheral glial cells generate neuroendocrine cells of the adrenal medulla." Science 357, no. 6346 (July 6, 2017): eaal3753. http://dx.doi.org/10.1126/science.aal3753.

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Adrenaline is a fundamental circulating hormone for bodily responses to internal and external stressors. Chromaffin cells of the adrenal medulla (AM) represent the main neuroendocrine adrenergic component and are believed to differentiate from neural crest cells. We demonstrate that large numbers of chromaffin cells arise from peripheral glial stem cells, termed Schwann cell precursors (SCPs). SCPs migrate along the visceral motor nerve to the vicinity of the forming adrenal gland, where they detach from the nerve and form postsynaptic neuroendocrine chromaffin cells. An intricate molecular lo

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4

Kim, Yu Mi, Young Hoon Jeon, Gwang Chun Jin, Jeong Ok Lim, and Woon Yi Baek. "In Vivo Biocompatibility of Alginate-PLL Microcapsules with Chromaffin Cells for the Alleviation of Chronic Pain." Key Engineering Materials 277-279 (January 2005): 62–66. http://dx.doi.org/10.4028/www.scientific.net/kem.277-279.62.

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Intrathecal implants of adrenal medullary chromaffin cells relieve chronic pain by secreting catecholamines, opioids and other neuroactive substances. Recently, macrocapsules with hollow fibers were employed to isolate immunologically xenogeneic chromaffin cells, but the poor viability in vivo of the encapsulated chromaffin cells limited the usefulness of this method. In this study, we used microencapsulation technology to increase the viability of chromaffin cells. Bovine adrenal chromaffin cells were microencapsulated with alginate and poly-L-lysine and implanted intrathecally in a rat using

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5

Finotto, S., K. Krieglstein, A. Schober, F. Deimling, K. Lindner, B. Bruhl, K. Beier, et al. "Analysis of mice carrying targeted mutations of the glucocorticoid receptor gene argues against an essential role of glucocorticoid signalling for generating adrenal chromaffin cells." Development 126, no. 13 (July 1, 1999): 2935–44. http://dx.doi.org/10.1242/dev.126.13.2935.

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Molecular mechanisms underlying the generation of distinct cell phenotypes is a key issue in developmental biology. A major paradigm of determination of neural cell fate concerns the development of sympathetic neurones and neuroendocrine chromaffin cells from a common sympathoadrenal (SA) progenitor cell. Two decades of in vitro experiments have suggested an essential role of glucocorticoid receptor (GR)-mediated signalling in generating chromaffin cells. Targeted mutation of the GR should consequently abolish chromaffin cells. The present analysis of mice lacking GR gene product demonstrates

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6

Hong, Hai Yan, Jeong Ok Lim, and Woon Yi Baek. "Effect of Morphine and Bupivacaine on Nicotine-Induced Catecholamine Secretion from Encapsulated Chromaffin Cells." Key Engineering Materials 277-279 (January 2005): 56–61. http://dx.doi.org/10.4028/www.scientific.net/kem.277-279.56.

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The control of intractable pain through transplanted of chromaffin cells has been recently reported where the analgesic effects are principally due to the production of opioid peptides and catecholamines (CAs) by the chromaffin cells. Currently many cancer patients receive general opioids or local anesthetics, such as bupivacaine. Therefore, the present study investigated the effect of morphine or bupivacaine on the secretion of nicotine-induced CAs from encapsulated chromaffin cells over a period of 180 min. As such, bovine chromaffin cells were isolated and encapsulated with alginate–poly–L–

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7

Sol, J. C., R. Y. Li, B. Sallerin, S. Jozan, H. Zhou, V. Lauwers-Cances, F. Tortosa, et al. "Intrathecal Grafting of Porcine Chromaffin Cells Reduces Formalin-Evoked c-Fos Expression in the Rat Spinal Cord." Cell Transplantation 14, no. 6 (July 2005): 353–65. http://dx.doi.org/10.3727/000000005783982963.

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Chromaffin cells from the adrenal gland secrete a combination of neuroactive compounds including catecholamines, opioid peptides, and growth factors that have strong analgesic effects, especially when administered intrathecally. Preclinical studies of intrathecal implantation with xenogeneic bovine chromaffin cells in rats have provided conflicting data with regard to analgesic effects, and recent concern over risk of prion transmission has precluded their use in human clinical trials. We previously developed a new, safer source of adult adrenal chromaffin cells of porcine origin and demonstra

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8

Eaton, M. J., M. Martinez, S. Karmally, T. Lopez, and J. Sagen. "Initial Characterization of the Transplant of Immortalized Chromaffin Cells for the Attenuation of Chronic Neuropathic Pain." Cell Transplantation 9, no. 5 (September 2000): 637–56. http://dx.doi.org/10.1177/096368970000900509.

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Cultures of embryonic day 17 (E17) rat adrenal and neonatal bovine adrenal cells were conditionally immortalized with the temperature-sensitive allele of SV40 large T antigen (tsTag) and chromaffin cell lines established. Indicative of the adrenal chromaffin phenotype, these cells expressed immunoreactivity (ir) for tyrosine hydroxylase (TH), the first enzyme in the synthetic pathway for catecholamines. At permissive temperature in vitro (33°C), these chromaffin cells are proliferative, have a typical rounded chromaffin-like morphology, and contain detectable TH-ir. At nonpermissive temperatur

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9

DUNCAN, Rory R., Andrew C. DON-WAUCHOPE, Sompol TAPECHUM, Michael J. SHIPSTON, Robert H. CHOW, and Peter ESTIBEIRO. "High-efficiency Semliki Forest virus-mediated transduction in bovine adrenal chromaffin cells." Biochemical Journal 342, no. 3 (September 5, 1999): 497–501. http://dx.doi.org/10.1042/bj3420497.

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Adrenal chromaffin cells are commonly used in studies of exocytosis. Progress in characterizing the molecular mechanisms has been slow, because no simple, high-efficiency technique is available for introducing and expressing heterologous cDNA in chromaffin cells. Here we demonstrate that Semliki Forest virus (SFV) vectors allow high-efficiency expression of heterologous protein in chromaffin cells.

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10

Vukicevic, Vladimir, Janine Schmid, Andreas Hermann, Sven Lange, Nan Qin, Linda Gebauer, Kuei-Fang Chung, et al. "Differentiation of Chromaffin Progenitor Cells to Dopaminergic Neurons." Cell Transplantation 21, no. 11 (November 2012): 2471–86. http://dx.doi.org/10.3727/096368912x638874.

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The differentiation of dopamine-producing neurons from chromaffin progenitors might represent a new valuable source for replacement therapies in Parkinson's disease. However, characterization of their differentiation potential is an important prerequisite for efficient engraftment. Based on our previous studies on isolation and characterization of chromaffin progenitors from adult adrenals, this study investigates their potential to produce dopaminergic neurons and means to enhance their dopaminergic differentiation. Chromaffin progenitors grown in sphere culture showed an increased expression

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11

BROOKS, J., and M. BROOKS. "Thiophosphorylated proteins in chromaffin cells are chromaffin vesicle matrix proteins." Neurochemistry International 20, no. 4 (June 1992): 501–9. http://dx.doi.org/10.1016/0197-0186(92)90029-q.

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12

Cheek, T. R., T. R. Jackson, A. J. O'Sullivan, R. B. Moreton, M. J. Berridge, and R. D. Burgoyne. "Simultaneous measurements of cytosolic calcium and secretion in single bovine adrenal chromaffin cells by fluorescent imaging of fura-2 in cocultured cells." Journal of Cell Biology 109, no. 3 (September 1, 1989): 1219–27. http://dx.doi.org/10.1083/jcb.109.3.1219.

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The cytosolic free calcium concentration ([Ca2+]i) and exocytosis of chromaffin granules were measured simultaneously from single, intact bovine adrenal chromaffin cells using a novel technique involving fluorescent imaging of cocultured cells. Chromaffin cell [Ca2+]i was monitored with fura-2. To simultaneously follow catecholamine secretion, the cells were cocultured with fura-2-loaded NIH-3T3t cells, a cell line chosen because of their irresponsiveness to chromaffin cell secretagogues but their large Ca2+ response to ATP, which is coreleased with catecholamine from the chromaffin cells. In

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13

Kordower, Jeffrey H., Massimo S. Fiandaca, Mary F. D. Notter, John T. Hansen, and Don M. Gash. "NGF-like trophic support from peripheral nerve for grafted rhesus adrenal chromaffin cells." Journal of Neurosurgery 73, no. 3 (September 1990): 418–28. http://dx.doi.org/10.3171/jns.1990.73.3.0418.

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✓ Autopsy results on patients and corresponding studies in nonhuman primates have revealed that autografts of adrenal medulla into the striatum, used as a treatment for Parkinson's disease, do not survive well. Because adrenal chromaffin cell viability may be limited by the low levels of available nerve growth factor (NGF) in the striatum, the present study was conducted to determine if transected peripheral nerve segments could provide sufficient levels of NGF to enhance chromaffin cell survival in vitro and in vivo. Aged female rhesus monkeys, rendered hemiparkinsonian by the drug MPTP (n-me

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14

Parlato, Rosanna, Christiane Otto, Jan Tuckermann, Stefanie Stotz, Sylvia Kaden, Hermann-Josef Gröne, Klaus Unsicker та Günther Schütz. "Conditional Inactivation of Glucocorticoid Receptor Gene in Dopamine-β-Hydroxylase Cells Impairs Chromaffin Cell Survival". Endocrinology 150, № 4 (26 листопада 2008): 1775–81. http://dx.doi.org/10.1210/en.2008-1107.

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Glucocorticoid hormones (GCs) have been thought to determine the fate of chromaffin cells from sympathoadrenal progenitor cells. The analysis of mice carrying a germ line deletion of the glucocorticoid receptor (GR) gene has challenged these previous results because the embryonic development of adrenal chromaffin cells is largely unaltered. In the present study, we have analyzed the role of GC-dependent signaling in the postnatal development of adrenal chromaffin cells by conditional inactivation of the GR gene in cells expressing dopamine-β-hydroxylase, an enzyme required for the synthesis of

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15

Huber, Katrin, Barbara Brühl, François Guillemot, Eric N. Olson, Uwe Ernsberger, and Klaus Unsicker. "Development of chromaffin cells depends on MASH1 function." Development 129, no. 20 (October 15, 2002): 4729–38. http://dx.doi.org/10.1242/dev.129.20.4729.

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The sympathoadrenal (SA) cell lineage is a derivative of the neural crest (NC), which gives rise to sympathetic neurons and neuroendocrine chromaffin cells. Signals that are important for specification of these two types of cells are largely unknown. MASH1 plays an important role for neuronal as well as catecholaminergic differentiation. Mash1 knockout mice display severe deficits in sympathetic ganglia, yet their adrenal medulla has been reported to be largely normal suggesting that MASH1 is essential for neuronal but not for neuroendocrine differentiation. We show now that MASH1 function is

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16

Czech, Kimberly A., Raymond Pollak, George D. Pappas, and Jacqueline Sagen. "Bovine Chromaffin Cells for CNS Transplantation do not Elicit Xenogeneic T Cell Proliferative Responses in Vitro." Cell Transplantation 5, no. 2 (March 1996): 257–67. http://dx.doi.org/10.1177/096368979600500214.

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Adrenal chromaffin cells have been utilized for several neural grafting applications, but limitations in allogeneic donor availability and dangers inherent in auto-grafting limit the widespread use of this approach clinically. While xenogeneic donors offer promise as a source for cell transplantation in the central nervous system (CNS), immunologic responses to cellular components of the adrenal medulla have not been well characterized. To further study the host T cell xenogeneic response to chromaffin and passenger cells of the adrenal medulla, an in vitro lymphocyte proliferation assay was u

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17

Bornstein, S. R., M. Ehrhart-Bornstein, A. Androutsellis-Theotokis, G. Eisenhofer, V. Vukicevic, J. Licinio, M. L. Wong, et al. "Chromaffin cells: the peripheral brain." Molecular Psychiatry 17, no. 4 (January 17, 2012): 354–58. http://dx.doi.org/10.1038/mp.2011.176.

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18

Barg, S., and J. D. Machado. "Compensatory endocytosis in chromaffin cells." Acta Physiologica 192, no. 2 (November 16, 2007): 195–201. http://dx.doi.org/10.1111/j.1748-1716.2007.01813.x.

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19

VITALE, NICOLAS, SYLVETTE CHASSEROT-GOLAZ, and MARIE-FRANCE BADER. "Regulated Secretion in Chromaffin Cells." Annals of the New York Academy of Sciences 971, no. 1 (October 2002): 193–200. http://dx.doi.org/10.1111/j.1749-6632.2002.tb04463.x.

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20

Boarder, M. R. "Phospholipase D in Chromaffin Cells?" Journal of Neurochemistry 60, no. 5 (May 1993): 1978–79. http://dx.doi.org/10.1111/j.1471-4159.1993.tb13435.x.

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21

Caumont, Anne-Sophie, Marie-Christine Galas, Nicolas Vitale, Dominique Aunis, and Marie-France Bader. "Regulated Exocytosis in Chromaffin Cells." Journal of Biological Chemistry 273, no. 3 (January 16, 1998): 1373–79. http://dx.doi.org/10.1074/jbc.273.3.1373.

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22

Galas, Marie-Christine, J. Bernd Helms, Nicolas Vitale, Danièle Thiersé, Dominique Aunis, and Marie-France Bader. "Regulated Exocytosis in Chromaffin Cells." Journal of Biological Chemistry 272, no. 5 (January 31, 1997): 2788–93. http://dx.doi.org/10.1074/jbc.272.5.2788.

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23

Torres, M., P. Molina, and M. T. Miras-Portugal. "Adenosine transporters in chromaffin cells." FEBS Letters 201, no. 1 (May 26, 1986): 124–28. http://dx.doi.org/10.1016/0014-5793(86)80583-x.

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24

UNSICKER, K., and K. KRIEGLSTEIN. "Growth factors in chromaffin cells." Progress in Neurobiology 48, no. 4-5 (March 1996): 307–24. http://dx.doi.org/10.1016/0301-0082(95)00045-3.

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25

Nguyen, Tien T., and André De Léan. "Nonadrenergic modulation by clonidine of the cosecretion of catecholamines and enkephalins in adrenal chromaffin cells." Canadian Journal of Physiology and Pharmacology 65, no. 5 (May 1, 1987): 823–27. http://dx.doi.org/10.1139/y87-132.

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Cultured bovine chromaffin cells cosecrete catecholamines and enkephalins following cholinergic nicotinic stimulation. Initial reports on the inhibitory effect of clonidine on catecholamine secretion raised the possibility of a modulation of chromaffin cell function through a presynaptic adrenergic mechanism. The purpose of this work was to investigate the pharmacological characteristics of this inhibitory effect of clonidine on the cosecretion of catecholamines and enkephalins in 4-day-old cultured chromaffin cells. We observed that clonidine completely inhibits nicotine-stimulated secretion

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26

Trifaró, J. M., M. F. Bader, and J. P. Doucet. "Chromaffin cell cytoskeleton: its possible role in secretion." Canadian Journal of Biochemistry and Cell Biology 63, no. 6 (June 1, 1985): 661–79. http://dx.doi.org/10.1139/o85-084.

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Cytoskeleton proteins (actin, myosin, α-actinin, spectrin, tubulin, neurofilament subunits) and their regulatory proteins (calmodulin, gelsolin) have been isolated from adrenal chromaffin cells and characterized. Their physicochemical properties have been studied and their cell localizations have been revealed by biochemical, immunocytochemical, and ulstrastructural techniques. α-Actinin and spectrin are components of chromaffin granule membranes and some of the cell actin copurifies with these secretory granules. Myosin is not detected in the granules, but is present mainly in the cytosol and

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27

Xie, Z., B. E. Herring, and A. P. Fox. "Excitatory and Inhibitory Actions of Isoflurane in Bovine Chromaffin Cells." Journal of Neurophysiology 96, no. 6 (December 2006): 3042–50. http://dx.doi.org/10.1152/jn.00571.2006.

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Isoflurane, a halogenated volatile anesthetic, is thought to produce anesthesia by depressing CNS function. Many anesthetics, including isoflurane, are thought to modulate and/or directly activate GABAA receptors. Chromaffin cells are known to express functional GABAA receptors. We previously showed that activation of the GABAA receptors, with specific agonists, leads to cellular excitation resulting from the depolarized anion equilibrium potential. In this study, our goal was to determine whether isoflurane mimicked this response and to explore the functional consequences of this activation.

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28

Nassar-Gentina, V., H. B. Pollard, and E. Rojas. "Electrical activity in chromaffin cells of intact mouse adrenal gland." American Journal of Physiology-Cell Physiology 254, no. 5 (May 1, 1988): C675—C683. http://dx.doi.org/10.1152/ajpcell.1988.254.5.c675.

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Membrane potentials of medullary chromaffin cells of the adrenal gland of the mouse were measured in situ. Resting potential (-54.3 +/- 8.8 mV) depended on extracellular [K+] as predicted by the constant-field equation with a permeability ratio, PNa/PK, of 0.09. Current-voltage (I-V) relationships showed that the current is rectified across the chromaffin cell membrane. A rectification ratio of 0.4 was calculated from the slopes of the I-V curves for positive (41 +/- 26 M omega) and negative (103 +/- M omega) currents. Because input resistance for a resting chromaffin cell in isolation is appr

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29

Holz, Ronald W., and Ruth A. Senter. "Plasma Membrane and Chromaffin Granule Characteristics in Digitonin-Treated Chromaffin Cells." Journal of Neurochemistry 45, no. 5 (November 1985): 1548–57. http://dx.doi.org/10.1111/j.1471-4159.1985.tb07226.x.

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30

Michener, M. L., W. B. Dawson, and C. E. Creutz. "Phosphorylation of a chromaffin granule-binding protein in stimulated chromaffin cells." Journal of Biological Chemistry 261, no. 14 (May 1986): 6548–55. http://dx.doi.org/10.1016/s0021-9258(19)84597-0.

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31

Scheuner, D., C. D. Logsdon, and R. W. Holz. "Bovine chromaffin granule membranes undergo Ca(2+)-regulated exocytosis in frog oocytes." Journal of Cell Biology 116, no. 2 (January 15, 1992): 359–65. http://dx.doi.org/10.1083/jcb.116.2.359.

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We have devised a new method that permits the investigation of exogenous secretory vesicle function using frog oocytes and bovine chromaffin granules, the secretory vesicles from adrenal chromaffin cells. Highly purified chromaffin granule membranes were injected into Xenopus laevis oocytes. Exocytosis was detected by the appearance of dopamine-beta-hydroxylase of the chromaffin granule membrane in the oocyte plasma membrane. The appearance of dopamine-beta-hydroxylase on the oocyte surface was strongly Ca(2+)-dependent and was stimulated by coinjection of the chromaffin granule membranes with

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32

Jousselin-Hosaja, M. "Effects of transplantation on mouse adrenal chromaffin cells." Journal of Endocrinology 116, no. 1 (January 1988): 149—NP. http://dx.doi.org/10.1677/joe.0.1160149.

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ABSTRACT The effects of long-term transplantation on the ultrastructure of adrenaline- and noradrenaline-storing cells from the adrenal medulla were determined using morphometric methods. Mouse adrenal medulla were freed from the adrenal cortex and grafted into the occipital cortex of the brain. Two types of chromaffin cells were identified by electron microscopy in grafts fixed with glutaraldehyde and osmium tetroxide. Noradrenaline-type cells were predominant and formed 70–80% of the surviving population of grafted chromaffin cells. A minority of the chromaffin cells contained medium-sized g

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33

Bayley, Jean-Pierre, Heggert G. Rebel, Kimberly Scheurwater, Dominique Duesman, Juan Zhang, Francesca Schiavi, Esther Korpershoek, Jeroen C. Jansen, Abbey Schepers, and Peter Devilee. "Long-term in vitro 2D-culture of SDHB and SDHD-related human paragangliomas and pheochromocytomas." PLOS ONE 17, no. 9 (September 30, 2022): e0274478. http://dx.doi.org/10.1371/journal.pone.0274478.

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The neuroendocrine tumours paraganglioma and pheochromocytoma (PPGLs) are commonly associated with succinate dehydrogenase (SDH) gene variants, but no human SDH-related PPGL-derived cell line has been developed to date. The aim of this study was to systematically explore practical issues related to the classical 2D-culture of SDH-related human paragangliomas and pheochromocytomas, with the ultimate goal of identifying a viable tumour-derived cell line. PPGL tumour tissue/cells (chromaffin cells) were cultured in a variety of media formulations and supplements. Tumour explants and dissociated p

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34

Jafferjee, Malika, Thairy Reyes Valero, Christine Marrero, Katie A. McCrink, Ava Brill, and Anastasios Lymperopoulos. "GRK2 Up-Regulation Creates a Positive Feedback Loop for Catecholamine Production in Chromaffin Cells." Molecular Endocrinology 30, no. 3 (March 1, 2016): 372–81. http://dx.doi.org/10.1210/me.2015-1305.

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Abstract Elevated sympathetic nervous system (SNS) activity aggravates several diseases, including heart failure. The molecular cause(s) underlying this SNS hyperactivity are not known. We have previously uncovered a neurohormonal mechanism, operating in adrenomedullary chromaffin cells, by which circulating catecholamine (CA) levels increase in heart failure: severe dysfunction of the adrenal α2-adrenergic receptors (ARs) due to the up-regulation of G protein-coupled receptor-kinase (GRK)-2, the kinase that desensitizes them. Herein we looked at the potential signaling mechanisms that bring a

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35

García, Antonio G., Antonio M. García-De-Diego, Luis Gandía, Ricardo Borges, and Javier García-Sancho. "Calcium Signaling and Exocytosis in Adrenal Chromaffin Cells." Physiological Reviews 86, no. 4 (October 2006): 1093–131. http://dx.doi.org/10.1152/physrev.00039.2005.

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At a given cytosolic domain of a chromaffin cell, the rate and amplitude of the Ca2+ concentration ([Ca2+]c) depends on at least four efficient regulatory systems: 1) plasmalemmal calcium channels, 2) endoplasmic reticulum, 3) mitochondria, and 4) chromaffin vesicles. Different mammalian species express different levels of the L, N, P/Q, and R subtypes of high-voltage-activated calcium channels; in bovine and humans, P/Q channels predominate, whereas in felines and murine species, L-type channels predominate. The calcium channels in chromaffin cells are regulated by G proteins coupled to purin

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Wick, P. F., R. A. Senter, L. A. Parsels, M. D. Uhler, and R. W. Holz. "Transient transfection studies of secretion in bovine chromaffin cells and PC12 cells. Generation of kainate-sensitive chromaffin cells." Journal of Biological Chemistry 268, no. 15 (May 1993): 10983–89. http://dx.doi.org/10.1016/s0021-9258(18)82082-8.

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37

Langley, Keith, and Nancy J. Grant. "Do adrenergic chromaffin cells exocytose like noradrenergic cells." Trends in Neurosciences 18, no. 10 (October 1995): 440–41. http://dx.doi.org/10.1016/0166-2236(95)94492-n.

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38

Callewaert, G., R. G. Johnson, and M. Morad. "Regulation of the secretory response in bovine chromaffin cells." American Journal of Physiology-Cell Physiology 260, no. 4 (April 1, 1991): C851—C860. http://dx.doi.org/10.1152/ajpcell.1991.260.4.c851.

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The nicotine-induced current and the Ca2+ current were studied in cultured bovine chromaffin cells using the whole cell patch-clamp technique. The dose-response curve for the nicotinic current gave a dissociation constant of 53 microM and a Hill coefficient of 1.3. Desensitization of the nicotinic current was rapid, with time constants of 22 and 155 ms at 10 microM nicotine. At higher concentrations of nicotine, both time constants decreased somewhat, but the most prominent effect was on the ratio of the two components. Recovery from desensitization was fitted by a single exponential with a ti

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39

Nakata, T., K. Sobue, and N. Hirokawa. "Conformational change and localization of calpactin I complex involved in exocytosis as revealed by quick-freeze, deep-etch electron microscopy and immunocytochemistry." Journal of Cell Biology 110, no. 1 (January 1, 1990): 13–25. http://dx.doi.org/10.1083/jcb.110.1.13.

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Calpactin I complex, a calcium-dependent phospholipid-binding protein, promotes aggregation of chromaffin vesicles at physiological micromolar calcium ion levels. Calpactin I complex was found to be a globular molecule with a diameter of 10.7 +/- 1.7 (SD) nm on mica. When liposomes were aggregated by calpactin, quick-freeze, deep-etching revealed fine thin strands (6.5 +/- 1.9 [SD] nm long) cross-linking opposing membranes in addition to the globules on the surface of liposomes. Similar fine strands were also observed between aggregated chromaffin vesicles when they were mixed with calpactin i

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LEVINE, MARK. "Ascorbic Acid Enhancement of Norepinephrine Biosynthesis in Chromaffin Cells and Chromaffin Vesicles." Annals of the New York Academy of Sciences 493, no. 1 Cellular and (April 1987): 147–50. http://dx.doi.org/10.1111/j.1749-6632.1987.tb27194.x.

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Egger, Claudia, and Hans Winkler. "Bovine chromaffin cells: Studies on the biosynthesis of phospholipids in chromaffin granules." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 1211, no. 3 (March 1994): 277–82. http://dx.doi.org/10.1016/0005-2760(94)90151-1.

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Wang, Jun Ming, Dirk Slembrouck, Junhui Tan, Lut Arckens, Frans H. H. Leenen, Pierre J. Courtoy, and Werner P. De Potter. "Presence of cellular renin-angiotensin system in chromaffin cells of bovine adrenal medulla." American Journal of Physiology-Heart and Circulatory Physiology 283, no. 5 (November 1, 2002): H1811—H1818. http://dx.doi.org/10.1152/ajpheart.01092.2001.

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The presence of a local renin-angiotensin system has been established in organs that serve as angiotensin targets. In this study, the expression of angiotensinogen mRNA and subcellular localization of renin, angiotensin-converting enzyme, and angiotensin II were investigated in bovine adrenal medullary cells in primary culture. By light microscopy, expression of angiotensinogen mRNA, immunoreactive renin, angiotensin-converting enzyme, and angiotensin II were readily detectable only in the chromaffin cells. The density distribution of renin and angiotensin II in sucrose gradients suggested a c

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Ehrhart-Bornstein, M., V. Vukicevic, K. F. Chung, and S. R. Bornstein. "Neuronal differentiation of chromaffin progenitor cells." Molecular Psychiatry 14, no. 1 (December 19, 2008): 1. http://dx.doi.org/10.1038/mp.2008.129.

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KIRSHNER, NORMAN, JAMES J. CORCORAN, BYRON CAUGHEY, and MIRA KORNER. "Chromaffin Vesicle Function in Intact Cells." Annals of the New York Academy of Sciences 493, no. 1 Cellular and (April 1987): 207–19. http://dx.doi.org/10.1111/j.1749-6632.1987.tb27202.x.

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MIRAS-PORTUGAL, M. T., J. PINTOR, P. ROTLLÁN, and M. TORRES. "Characterization of Ectonucleotidases in Chromaffin Cells." Annals of the New York Academy of Sciences 603, no. 1 Biological Ac (December 1990): 523–26. http://dx.doi.org/10.1111/j.1749-6632.1990.tb37726.x.

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EKBLOM, A. "Antinociceptive properties of adrenal chromaffin cells." Regional Anesthesia and Pain Medicine 22, no. 5 (September 1997): 486. http://dx.doi.org/10.1016/s1098-7339(97)80044-2.

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García, Antonio G., and Emilio Carbone. "Calcium-current facilitation in chromaffin cells." Trends in Neurosciences 19, no. 9 (January 1996): 383–84. http://dx.doi.org/10.1016/s0166-2236(96)20035-9.

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Delacruz, Joannalyn, Meng Huang, Joan Lenz, Manfred Lindau, and Shailendra Rathore. "Fusion Pore Selectivity in Chromaffin Cells." Biophysical Journal 112, no. 3 (February 2017): 396a. http://dx.doi.org/10.1016/j.bpj.2016.11.2148.

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OKA, Motoo, Kyoji MORITA, Masanori YOSHIZUMI, Hitoshi HOUCHI, Yasuko ISHIMURA, and Yutaka MASUDA. "Catecholamine secretion from adrenal chromaffin cells." Folia Pharmacologica Japonica 98, no. 3 (1991): 209–14. http://dx.doi.org/10.1254/fpj.98.3_209.

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Krause, Winfried, Norbert Michael, Carsten Lübke, Bruce G. Livett, and Peter Oehme. "Catecholamine release from fractionated chromaffin cells." European Journal of Pharmacology 302, no. 1-3 (April 1996): 223–28. http://dx.doi.org/10.1016/0014-2999(96)00103-3.

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