DOCSLIB.ORG

Novel Autocrine Feedback Control of Catecholamine Release a Discrete Chromogranin a Fragment Is a Noncompetitive Nicotinic Cholinergic Antagonist Sushil K

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Novel Autocrine Feedback Control of Catecholamine Release a Discrete Chromogranin a Fragment Is a Noncompetitive Nicotinic Cholinergic Antagonist Sushil K Novel Autocrine Feedback Control of Catecholamine Release A Discrete Chromogranin A Fragment is a Noncompetitive Nicotinic Cholinergic Antagonist Sushil K. Mahata,* Daniel T. O’Connor,* Manjula Mahata,* Seung Hyun Yoo,‡ Laurent Taupenot,* Hongjiang Wu,* Bruce M. Gill,* and Robert J. Parmer* *Department of Medicine and Center for Molecular Genetics, University of California, San Diego, California 92093 and Department of Veterans Affairs Medical Center, San Diego, California 92161, and ‡National Institute of Deafness and Communicative Disorders, National Institutes of Health, Bethesda, Maryland 20892 Abstract completely established, recent evidence implicates chromogra- nin A as a precursor of several small biologically active secre- Catecholamine secretory vesicle core proteins (chromog- tion-inhibitory peptides that may play an autocrine regulatory ranins) contain an activity that inhibits catecholamine re- role in neuroendocrine secretion from a variety of cell types (3, lease, but the identity of the responsible peptide has been 7–10). The primary structure of chromogranin A reveals 8–10 elusive. Size-fractionated chromogranins antagonized nico- conserved pairs of basic amino acids that represent potential tinic cholinergic-stimulated catecholamine secretion; the in- proteolytic cleavage sites for the generation of such peptides hibitor was enriched in processed chromogranin fragments, (11–17), and chromogranin A is a substrate for the prohor- and was liberated from purified chromogranin A. Of 15 syn- mone convertases (18–20). of chromogranin A, one To date, several chromogranin A–derived peptides have %80 ف thetic peptides spanning (bovine chromogranin A344–364 [RSMRLSFRARGYGFRG- been identified that affect the secretory function of the parent PGLQL], or catestatin) was a potent, dose-dependent (IC50 cells. These peptides include: (a) pancreastatin (porcine chro- ف 200 nM), reversible secretory inhibitor on pheochromocy- mogranin A240–288; 21), originally isolated from porcine pan- toma and adrenal chromaffin cells, as well as noradrenergic creas, which inhibits glucose-stimulated insulin release from is- neurites. An antibody directed against this peptide blocked let ␤ cells and parathyroid hormone release from chief cells; the inhibitory effect of chromogranin A proteolytic frag- (b) the NH2 terminus of chromogranin A, termed ␤-granin (rat ments on nicotinic-stimulated catecholamine secretion. This chromogranin A1–114; 22–24) or vasostatin (human chromogra- region of chromogranin A is extensively processed within nin A1–76; 25, 26), which inhibits parathyroid hormone release chromaffin vesicles in vivo. The inhibitory effect was spe- and relaxes vascular smooth muscle; and parastatin (porcine cific for nicotinic cholinergic stimulation of catecholamine chromogranin A347–419; 27), which inhibits parathyroid hor- release, and was shared by this chromogranin A region from mone release. several species. Nicotinic cationic (Naϩ, Ca2ϩ) signal trans- In 1988 Simon et al. (28) reported that fragmentation of duction was specifically disrupted by catestatin. Even high- chromogranin A generated peptide(s) that inhibit catechol- dose nicotine failed to overcome the inhibition, suggesting amine release from cultured adrenal medullary chromaffin noncompetitive nicotinic antagonism. This small domain cells, but the identity of the responsible peptide has remained within chromogranin A may contribute to a novel, auto- elusive (29–31). crine, homeostatic (negative-feedback) mechanism control- In these experiments, we characterized the catecholamine ling catecholamine release from chromaffin cells and neu- release inhibitory activity in chromogranins, and reproduced it rons. (J. Clin. Invest. 1997. 100:1623–1633.) Key words: as a potent synthetic fragment of chromogranin A. Our results chromogranin A • catestatin • acetylcholine • catechol- suggest that this fragment inhibits catecholamine release spe- amine • PC12 cifically as a nicotinic cholinergic antagonist, perhaps constitut- ing a novel autocrine secretion regulatory mechanism. Introduction Methods kD acidic protein initially described-48 ف Chromogranin A, an in catecholamine storage vesicles of the adrenal medulla (1, 2), Cell culture. Rat PC12 pheochromocytoma cells (32; at passage 8, ob- has a widespread distribution in secretory vesicles throughout tained from Dr. David Schubert, Salk Institute, La Jolla, CA) were the neuroendocrine system (3, 4), where it is colocalized and grown at 37ЊC/6% CO2 in 10-cm plates or 6-well plates in DME/high cosecreted with the usual resident peptide or amine hormone glucose medium supplemented with 5% FBS, 10% horse serum, 100 (3, 5, 6). Although the functions of chromogranin A are not U/ml penicillin, and 100 ␮g/ml streptomycin, as previously described (6). In some experiments, cells were pretreated with pertussis toxin (100 ng/ml, 16 h; 33). Bovine adrenal medullary chromaffin cells were prepared and Address correspondence to Daniel T. O’Connor, M.D., Department grown in primary culture as previously described (34). of Medicine and Center for Molecular Genetics (9111H), University Secretagogue-stimulated norepinephrine release. Norepinephrine of California, San Diego, 3350 La Jolla Village Drive, San Diego, CA secretion was monitored as previously described (35). PC12 cells 92161. Phone: 619-552-8585 ext. 7373; FAX: 619-552-7549; E-mail: were plated on poly-D-lysine–coated polystyrene dishes (Falcon Lab- [email protected] ware, Oxnard, CA), labeled for 3 h with 1 ␮Ci [3H]L-norepinephrine Received for publication 11 November 1996 and accepted in re- (71.7 Ci/mmol, DuPont-NEN, Boston, MA) in 1 ml of PC12 growth vised form 14 July 1997. medium, washed twice with release buffer (150 mM NaCl, 5 mM KCl, 2 mM CaCl2, 10 mM Hepes, pH 7.0), and then incubated at 37ЊC for 30 The Journal of Clinical Investigation min in release buffer with or without secretagogues, such as nicotine Volume 100, Number 6, September 1997, 1623–1633 (60 ␮M), or cell membrane depolarization (55 mM KCl). Release http://www.jci.org buffer for experiments involving KCl as secretagogue had NaCl re- Chromogranin A and Catecholamine Release 1623 duced to 100 mM to maintain isotonicity. After 30 min, secretion was obtained bovine adrenal medullae, on 0.3 M/1.6 M sucrose density terminated by aspirating the release buffer, and by lysing cells into step-gradients, as previously described (41, 43), then lysed in 1 mM 150 mM NaCl, 5 mM KCl, 10 mM Hepes, pH 7.0, and 0.1% (vol/vol) NaH2PO4, pH 6.5, and centrifuged at 100,000 ϫ g for 60 min to re- Triton X-100. Release medium and cell lysates were assayed for move granule membranes. The vesicle soluble core proteins (chro- [3H]norepinephrine by liquid scintillation counting, and results were mogranins; 10 ␮g/lane) were electrophoresed through Tris-Tricine expressed as percent secretion (amount released/[amount released ϩ (16.5–10%) SDS-PAGE slab gels, transferred to nitrocellulose sheets, amount in cell lysate]) ϫ 100. Net secretion is secretagoue-stimulated and visualized with amido black protein stain, or with rabbit antibo- release minus basal release, where basal norepinephrine release is vine catestatin (1:500, vol:vol), followed by horseradish peroxidase– typically 5.8Ϯ0.36% of cell total [3H]norepinephrine released over 30 labeled second antibody, and enhanced chemiluminescence detection min (n ϭ 10 separate secretion assays). (ECL, Amersham Corp., Arlington Heights, IL). Chromogranin size fractions. Bovine adrenal medullary chromaf- Neuronal differentiation of PC12 cells with nerve growth factor. fin granules were prepared by differential and sucrose step gradient PC12 cells were split to 50% confluence and treated with nerve centrifugation, as previously described (36). Granules were lysed into growth factor (2.5S form, 100 ng/ml; Boehringer-Mannheim, India- 1 mM Na Hepes, pH 7.0, and the membranes were pelleted at 100,000 g napolis, IN). The medium was changed every other day, with nerve for 1 h. Soluble core contents were size-fractionated at 4ЊC on a 2.5 ϫ growth factor addition to the new medium. After 5 d of treatment, 80–cm column of Sephacryl S-300, and were equilibrated and eluted the neurite-bearing cells were used for secretion studies as described with 0.3 M ammonium acetate, pH 6.5, at 37 ml/h (37). 6-ml fractions above. were analyzed by SDS-PAGE and staining with Coomassie blue, and 22Naϩ uptake by PC12 cells. 22Naϩ uptake was performed as de- then high and low molecular weight protein fractions were pooled, scribed by Amy and Kirshner (44) with minor modifications. Before lyophilized (twice, to remove the volatile ammonium acetate buffer), experiments, PC12 cells were washed twice with 50 mM Naϩ-sucrose and resuspended in 1 mM Na Hepes, pH 7.0. Protein concentrations media containing 50 mM NaCl, 187 mM sucrose, 5 mM KCl, 2 mM were determined by the Coomassie blue dye–binding technique (38). CaCl2, and 5 mM Hepes adjusted to pH 7.4 with NaOH. To measure Low molecular weight chromogranin fractions (not containing 22Naϩ influx, this medium was then supplemented with 5 mM ouabain chromogranin A on SDS-PAGE) were further purified and concen- (to prevent active extrusion of newly taken up 22Naϩ from cells) and trated by solid phase extraction onto a Sep-Pak classic C-18 silica 1.5 ␮Ci/ml of 22NaCl. Incubation was carried out at 22ЊC for 5 min in cartridge (Waters-Millipore, Milford, MA). The cartridge was first the presence or absence of secretagogues, and then the cells were washed with 0.1% trifluoroacetic acid (TFA)1 in water, activated with washed within 10 s with three changes (1 ml each) of 50 mM Naϩ- 80%CH3CN/20%H2O/0.1% TFA, and then equilibrated in 0.1% sucrose media with 5 mM ouabain. The cells were lysed (see above), TFA in water. Peptides were adsorbed to the cartridge in 0.1% TFA and 22Naϩ in the cell lysate was measured in a ␥ counter (LKB 1274 in water. The column was washed with 0.1% TFA in water, and the RIAGAMMA; Wallac Inc., Gaithersburg, MD). The data were ex- peptides were eluted with 80% CH3CN/20%H2O/0.1% TFA, lyo- pressed as dpm/well. philized (SpeedVac; Savant Instruments Inc., Farmingdale, NY), and 45Ca2ϩ uptake by PC12 cells.
Load more

Recommended publications
  • Expression Pattern of Delta-Like 1 Homolog in Developing Sympathetic Neurons and Chromaffin Cells
    Published in "Gene Expression Patterns 30: 49–54, 2018" which should be cited to refer to this work. Expression pattern of delta-like 1 homolog in developing sympathetic neurons and chromaffin cells ∗ Tehani El Faitwria,b, Katrin Hubera,c, a Institute of Anatomy & Cell Biology, Albert-Ludwigs-University Freiburg, Albert-Str. 17, 79104, Freiburg, Germany b Department of Histology and Anatomy, Faculty of Medicine, Benghazi University, Benghazi, Libya c Department of Medicine, University of Fribourg, Route Albert-Gockel 1, 1700, Fribourg, Switzerland ABSTRACT Keywords: Delta-like 1 homolog (DLK1) is a member of the epidermal growth factor (EGF)-like family and an atypical notch Sympathetic neurons ligand that is widely expressed during early mammalian development with putative functions in the regulation Chromaffin cells of cell differentiation and proliferation. During later stages of development, DLK1 is downregulated and becomes DLK1 increasingly restricted to specific cell types, including several types of endocrine cells. DLK1 has been linked to Adrenal gland various tumors and associated with tumor stem cell features. Sympathoadrenal precursors are neural crest de- Organ of Zuckerkandl rived cells that give rise to either sympathetic neurons of the autonomic nervous system or the endocrine Development ffi Neural crest chroma n cells located in the adrenal medulla or extraadrenal positions. As these cells are the putative cellular Phox2B origin of neuroblastoma, one of the most common malignant tumors in early childhood, their molecular char- acterization is of high clinical importance. In this study we have examined the precise spatiotemporal expression of DLK1 in developing sympathoadrenal cells. We show that DLK1 mRNA is highly expressed in early sympa- thetic neuron progenitors and that its expression depends on the presence of Phox2B.
    [Show full text]
  • Extra-Adrenal Chromaffin Cells of the Zuckerkandl´S Paraganglion: Morphological and Electrophysiological Study
    275 Extra-adrenal chromaffin cells of the Zuckerkandl´s paraganglion: morphological and electrophysiological study. Beatriz Galán-Rodríguez, M. Pilar Ramírez-Ponce, Fadwa El Banoua, Juan A. Flores, Juan Bellido and Emilio Fernández-Espejo. Departamento de Fisiología Médica y Biofísica. Universidad de Sevilla. Spain. Correspondence: Dra. Beatriz Galán Rodríguez or Dr. Emilio Fernández-Espejo, Departamento de Fisiología Médica y Biofísica, Facultad de Medicina, Universidad de Sevilla, 41009. Sevilla. Spain. Phone: 34-954-556584; Fax: 34-954-551769; Email: [email protected] ; [email protected] Cell Biology of the Chromaffin Cell R. Borges & L. Gandía Eds. Instituto Teófilo Hernando, Spain, 2004 Cell Biology of the Chromaffin Cell 276 Parkinson´s disease is one of the most important neurodegenerative disorders that affects to one out of a hundred of the world population elder than 65. It has been observed in our laboratory, for the first time, that intrabrain transplantation of chromaffin cell aggregates from the Zuckerkandl´s organ, an extraadrenal paraganglion located adjacent to the lower abdominal aorta, induced gradual improvement of functional deficits in animal models of Parkinson´s disease1. This functional regeneration was likely caused by long-survival of grafted cells and chronic trophic action of dopaminotrophic factors, glial cell line-derived 2,3 4,5 factor (GDNF) and transforming growth factor beta1 (TGF-b1) , which are expressed and delivered by long-surviving grafted chromaffin cells. The objective of this study is to discern the morphological and cytological characteristics of extra-adrenal cells of the Zuckerkandl’s organ. On the other hand, long survival of extra-adrenal chromaffin cells could be related to resistance to hypoxia, since it is certainly know that hypoxia is a primary factor involved in cell death after intrabrain grafting.
    [Show full text]
  • Cell Proliferation
    Proc. Nati. Acad. Sci. USA Vol. 91, pp. 1771-1775, March 1994 Neurobiology Insulin-like growth factors act synergistically with basic fibroblast growth factor and nerve growth factor to promote chromaffin cell proliferation MORTEN FRODIN* AND STEEN GAMMELTOFT*t Department of Clinical Chemistry, Bispebjerg Hospital, DK 2400 Copenhagen NV, Denmark Communicated by Viktor Mutt, November 29, 1993 (receivedfor review August 26, 1993) ABSTRACT We have investigated the effects of insulin- addition, NGF and bFGF stimulate transdifferentiation of like growth factors (IGFs), basic fibroblast growth factor cultured chromaffin cells into a sympathetic neuron-like (bFGF), and nerve growth factor (NGF) on DNA synthesis in phenotype and increase cell survival and catecholamine cultured chromaffin cells from fetal, neonatal, and adult rats synthesis (8, 9, 13-15). In adult rats, chromaffmi-cell replace- by using 5-bromo-2'-deoxyuridine (BrdUrd) pulse labeling for ment decreases after denervation of the adrenal medulla, 24 or 48 h and immunocytochemical staining of cell nuclei. suggesting that neurogenic stimuli can regulate chromaffmi- After 6 days in culture in the absence ofgrowth factors, nuclear cell proliferation (16). BrdUrd incorporation was detected in 30% offetal chromafFin Insulin-like growth factor I and II (IGF-I and IGF-II, cells, 1.5% of neonatal cells, and 0.1% of adult cells. Addition respectively) act as neurotrophic factors in various parts of of 10 nM IGF-I or IGF-ll increased the fraction of BrdUrd- the developing and adult nervous system (17). IGF-II mRNA labeled nuclei to 50% offetal, 20% ofneonatal, and 2% ofadult and immunoreactivity have been demonstrated in adult hu- chromaffn cells.
    [Show full text]
  • The Generation of Monoclonal Antibodies That Bind Preferentially to Adrenal Chromaffin Cells and the Cells of Embryonic Sympathetic Ganglia
    The Journal of Neuroscience, November 1991, 7 7(11): 34933506 The Generation of Monoclonal Antibodies that Bind Preferentially to Adrenal Chromaffin Cells and the Cells of Embryonic Sympathetic Ganglia Josette F. Carnahaw and Paul l-i. Patterson Biology Division, California Institute of Technology, Pasadena, California 91125 Adrenal chromaffin ceils, sympathetic neurons, and small technical limitation in this effort is the lack of markers specific intensely fluorescent (SIF) cells are each derived from the for the various stagesof development within a particular lineage. neural crest, produce catecholamines, and share certain Without such markers, cells making key phenotypic decisions morphological features. These cell types are also partially cannot be identified. It has been especially difficult to find mo- interconvertible in cell culture (Doupe et al., 1985a,b; An- lecular labels for committed progenitor cells. Monoclonal an- derson and Axel, 1988). Thus, these cells are said to be tibodies can be used as highly specific markers, and the hybrid- members of the sympathoadrenal (SA) lineage and could oma method can be manipulated so asto enhancethe likelihood share a common progenitor. To investigate the origins of this of obtaining antibodies against rare antigens of interest (Mat- lineage further, we used the cyclophosphamide immuno- thew and Patterson, 1983; Barald and Wessels,1984; Agius and suppression method (Matthew and Patterson, 1983) to gen- Richman, 1986; Barclay and Smith, 1986; Golumbeski and Di- erate five monoclonal antibodies (SAl-5) that bind strongly mond, 1986; Hockfield, 1987; Mahana et al., 1987; Matthew to chromaffin cells, with little or no labeling of sympathetic and Sandrock, 1987; Norton and Benjamini, 1987; Huse et al., neurons or SIF cells in frozen sections from adult rats.
    [Show full text]
  • Stimulus-Secretion Coupling in Chromaffin Cells Isolated
    Proc. Natl. Acad. Sci. USA Vol. 74, No. 11, pp. 5036-5040, November 1977 Cell Biology Stimulus-secretion coupling in chromaffin cells isolated from bovine adrenal medulla (catecholamine secretion/acetylcholine receptors/K+ depolarization/calcium requirement/microtubule disruption) ALLAN S. SCHNEIDER*, RUTH HERZ*, AND KURT ROSENHECKt * Sloan-Kettering Institute for Cancer Research, Cornell University Graduate School of Medical Sciences, New York, New York 10021; and tDepartment of Membrane Research, Weizmann Institute of Science, Rehovot, Israel Communicated by Francis 0. Schmitt, August 19,1977 ABSTRACT Bovine adrenal chromaffin cells were isolated membrane fusion and exocytosis, (iii) the possible role of cyclic by removal of the cortex and sequential collagenase digestion nucleotides coupled with ion translocation in mediating hor- of the medulla. The catecholamine secretory function of these cells was characterized with respect to acetylcholine stimula- mone and neurotransmitter synthesis and secretion, and (iv) tion, cation requirements, and cytoskeletal elements. The the role of microfilaments, microtubules, and/or a calcium- dose-response curve for stimulated release had its half-maxi- modulated contractile protein system in bringing secretory mum value at 10-5 M acetylcholine, and maximum secretion granules together with the plasma membrane to facilitate ex- was on the average 7 times that of control basal secretion. The ocytosis. Further advances may be possible on these and related differential release of epinephrine versus norepinephrine after questions through the use of isolated chromaffin cells. stimulation with 0.1 mM acetylcholine occurred in proportion to their distribution in the cell suspension. The cholinergic re- In the present work we provide a functional characterization ceptors were found to be predominantly nicotinic.
    [Show full text]
  • Advances in Paraganglioma– Pheochromocytoma Cell Lines and Xenografts
    27 12 Endocrine-Related J-P Bayley and P Devilee PPGL cell lines and xenografts 27:12 R433–R450 Cancer REVIEW Advances in paraganglioma– pheochromocytoma cell lines and xenografts Jean-Pierre Bayley 1 and Peter Devilee 1,2 1Department of Human Genetics, Leiden University Medical Center, Leiden, the Netherlands 2Department of Pathology, Leiden University Medical Center, Leiden, the Netherlands Correspondence should be addressed to J-P Bayley: [email protected] Abstract This review describes human and rodent-derived cell lines and xenografts developed over Key Words the last five decades that are suitable or potentially suitable models for paraganglioma– f paraganglioma pheochromocytoma research. We outline the strengths and weaknesses of various f pheochromocytoma models and emphasize the recurring theme that, despite the major challenges f succinate dehydrogenase involved, more effort is required in the search for valid human and animal cell models f models of paraganglioma–pheochromocytoma, particularly those relevant to cancers carrying f cell lines a mutation in one of the succinate dehydrogenase genes. Despite many setbacks, the f xenografts recent development of a potentially important new model, the RS0 cell line, gives reason f SV40 for optimism regarding the future of models in the paraganglioma–pheochromocytoma f MPC field. We also note that classic approaches to cell line derivation such as SV40-mediated f MTT immortalization and newer approaches such as organoid culture or iPSCs have been f imCC insufficiently explored. As many existing cell lines have been poorly characterized, we f hPheo1 provide recommendations for reporting of paraganglioma and pheochromocytoma f PC12 cell lines, including the strong recommendation that cell lines are made widely available via the ATCC or a similar cell repository.
    [Show full text]
  • Chromaffin Cell Development in Mash1 Mutant Mice 4731
    Development 129, 4729-4738 (2002) 4729 Printed in Great Britain © The Company of Biologists Limited 2002 DEV1866 Development of chromaffin cells depends on MASH1 function Katrin Huber1, Barbara Brühl1, François Guillemot2, Eric N. Olson3, Uwe Ernsberger1 and Klaus Unsicker1,* 1Neuroanatomy, Interdisciplinary Center for Neurosciences (IZN), University of Heidelberg, INF 307, D-69120 Heidelberg, Germany 2IGBMC,CNRS/INSERM/Université Louis Pasteur, BP 163, 67404 Illkirch Cédex, Cu de Strasbourg, France 3Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75239-9148, USA *Author for correspondence (e-mail: [email protected]) Accepted 8 July 2002 SUMMARY The sympathoadrenal (SA) cell lineage is a derivative of population seen in Mash1+/+ mice is maintained in Mash1–/– the neural crest (NC), which gives rise to sympathetic mice at birth. Similar to Phox2b, cells expressing Phox2a neurons and neuroendocrine chromaffin cells. Signals that and Hand2 (dHand) clearly outnumber TH-positive cells. are important for specification of these two types of cells Most cells in the adrenal medulla of Mash1–/– mice do not are largely unknown. MASH1 plays an important role for contain chromaffin granules, display a very immature, neuronal as well as catecholaminergic differentiation. neuroblast-like phenotype, and, unlike wild-type adrenal Mash1 knockout mice display severe deficits in sympathetic chromaffin cells, show prolonged expression of ganglia, yet their adrenal medulla has been reported to be neurofilament and Ret comparable with that observed in largely normal suggesting that MASH1 is essential for wild-type sympathetic ganglia. However, few chromaffin neuronal but not for neuroendocrine differentiation. We cells in Mash1–/– mice become PNMT positive and show now that MASH1 function is necessary for the downregulate neurofilament and Ret expression.
    [Show full text]
  • HISTOLOGICAL TYPING of ENDOCRINE TUMOURS INTERNATIONAL HISTOLOGICAL CLASSIFICATION of TUMOURS No
    HISTOLOGICAL TYPING OF ENDOCRINE TUMOURS INTERNATIONAL HISTOLOGICAL CLASSIFICATION OF TUMOURS No. 23 HISTOLOGICAL TYPING OF ENDOCRINE TUMOURS E. D. WILLIAMS Head, WHO Collaboratmg Centre for the Histologica/ Classificatton of Endocrine Tumours. · Department of Pathology, The Welsh National School of Medicine, Cardiff. Wales, Umted Kingdom in collaboration with R. E. SIEBENMANN L. H. SOBIN lnstitute of Pathology, Pathologist, Stadtspital Triemli, World Hea/th Orgamzation, Zurich, Switzerland Geneva, Switzer/and and pathologists in 13 countries WORLD HEALTH ORGANIZATION GENEVA 1980 ISBN 92 4 176023 O © World Health Organization 1980 Pubhcations ofthe World Health Orgamzation enjoy copyright protection m accordance with the provisions of Protocol2 of the Universal Copyright Convention. For rights of reproduction or translation of WHO publicatwns, m part or in tofo, application should be made to the Office of Publications, World Health Orgamzatwn, Geneva, Sw1tzerland. The World Health Organi­ zation welcomes such applications. The designatwns employed and the presentatwn of the material in this publicatwn do not 1mply the expression of any opinion whatsoever on the part of the Duector-General of the World Health Organization concerning the legal status of any country, territory, city or area or of 1ts authorities, or concerning the delimitation of its front1ers or boundanes. The mention of specific compames or of certam manufacturers' products does not imply that they are endorsed or recommended by the W orld Health Organizatwn in preference to others of a similar nature that are not mentioned. Errors and omJsswns excepted, the names of proprietary products are distingmshed by imt1al capitalletters. Authors alone are responsible for v1ews expressed in th1s publication.
    [Show full text]
  • Uptake and Release of Ca2 by Chromaffin Vesicles
    S timulu s - S ecretion Coupling in Chromaffin Cells Volume I Editors Kurt Rosenheck, Ph.D. Associate Professor Department of Membrane Research The Weizmann Institute of Science Rehovot, Israel Peter I. Lelkes, Ph.D. Laboratory of Cell Biology and Genetics National Institutes of Health Bethesda, Maryland CRC Press, Inc. Boca Raton, Florida TABLE OF CONTENTS Volume 1 Chapter 1 Morphology and Innervation of the Adrenal Medulla 1 Stephen W. Carmichael Chapter 2 Chromaffin Granule Biogenesis and the Exocytosis/Endocytosis Cycle 31 John H. Phillips Chapter 3 The Structure and Dynamics of Chromaffin Granules 55 John H. Phillips Chapter 4 Neuropeptides of the Adrenal Medulla 87 Christopher D. Unsworth and O. Humberto Viveros Chapter 5 Uptake and Release of Ca2+ by Chromaffin Vesicles Ill Manfred Gratzl Chapter 6 Chromaffin Cell Calmodulin 125 J. M. Trifaro and R. L. Kenigsberg Chapter 7 Cytoskeletal Proteins and Chromaffin Cell Activity 155 Dominique Aunis, Dominique Perrin, and O. Keith Langley Index 177 Volume II Chapter 8 Cytosolic Proteins as Intracellular Mediators of Calcium Action During Exocytosis 1 Harvey B. Pollard, Alexander L. Burns, Andres Stutzin, Eduardo Rojas, Peter I. Lelkes, and Kyoji Morita Chapter 9 Liposome-Mediated Introduction of Macromolecules into Isolated Bovine Adrenal Chromaffin Cells 15 Peter I. Lelkes Chapter 10 The Chromaffin Cell Plasma Membrane 37 Kurt Rosenheck Chapter 11 Muscarinic Receptor Mechanisms in Adrenal Chromaffin Cells 51 Allan S. Schneider Chapter 12 Sodium and Calcium Channels in Cultured Bovine Adrenal Medulla Cells 71 Norman Kirshner Chapter 13 Recent Advances in Membrane Biophysics of the Adrenal Chromaffin Cell 87 Yoshiaki Kidokoro Chapter 14 Modulation by Calcium of the Kinetics of the Chromaffin Cell Secretory Response — 97 A.
    [Show full text]
  • Adrenergic Responses to Stress of Crassostrea Gigas 1249
    The Journal of Experimental Biology 204, 1247–1255 (2001) 1247 Printed in Great Britain © The Company of Biologists Limited 2001 JEB3148 EVIDENCE FOR A FORM OF ADRENERGIC RESPONSE TO STRESS IN THE MOLLUSC CRASSOSTREA GIGAS A. LACOSTE*, S. K. MALHAM, A. CUEFF, F. JALABERT, F. GÉLÉBART AND S. A. POULET Station Biologique de Roscoff, CNRS, INSU, Université Pierre et Marie Curie, Paris 6, BP 74, F-29682 ROSCOFF, France *e-mail: [email protected] Accepted 10 January; published on WWW 15 March 2001 Summary Catecholamines and pro-opiomelanocortin (POMC)- Moreover, the nicotinic antagonists hexamethonium and α- derived peptides, some of the central regulators of the bungarotoxin and the muscarinic antagonist atropine stress-response systems of vertebrates, are also present in caused no significant inhibition of catecholamine release in invertebrates. However, studies are needed to determine stressed oysters. Adrenocorticotropic hormone (ACTH) how these hormones participate in the organisation of induced a significant release of noradrenaline, but the neuroendocrine stress-response axes in invertebrates. Our release of dopamine in response to ACTH was not present work provides evidence for the presence of an significant. These results suggest that, unlike that of adrenergic stress-response system in the oyster Crassostrea vertebrates, the adrenergic stress-response system of gigas. Noradrenaline and dopamine are released into the oysters is not under the control of acetylcholine and that circulation in response to stress. Storage and release other factors, such as the neuropeptide ACTH, might of these hormones take place in neurosecretory cells control this system. presenting morphological and biochemical similarities with vertebrate chromaffin cells. Both in vivo and in vitro experiments showed that applications of the Key words: catecholamine, noradrenaline, dopamine, acetylcholine, neurotransmitters acetylcholine or carbachol caused no adrenocorticotropic hormone, chromaffin cell, stress, mollusc, significant release of noradrenaline or dopamine.
    [Show full text]
  • The Sympathoadrenal Cell Lineage: Specification, Diversification, and New Perspectives ⁎ Katrin Huber
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Developmental Biology 298 (2006) 335–343 www.elsevier.com/locate/ydbio Review The sympathoadrenal cell lineage: Specification, diversification, and new perspectives ⁎ Katrin Huber Department of Neuroanatomy and Interdisciplinary Center for Neurosciences, University of Heidelberg, INF 307, D-69120 Heidelberg, Germany Received for publication 7 January 2006; revised 8 July 2006; accepted 11 July 2006 Available online 14 July 2006 Abstract During the past years considerable progress has been made in understanding the generation of cell diversity in the neural crest (NC). Sympathoadrenal (SA) cells constitute a major lineage among NC derivatives; they give rise to sympathetic neurons, neuroendocrine chromaffin cells, and the intermediate small intensely fluorescent (SIF) cells. The classic perception of how this diversification is achieved implies that (i) there is a common progenitor cell for sympathetic neurons and chromaffin cells, (ii) NC cells are instructed to a SA cell fate by signals derived from the wall of the dorsal aorta, especially bone morphogenetic proteins (BMP), and (iii) the local environments of secondary sympathetic ganglia and adrenal gland, respectively, are crucial for inducing differentiation of SA cells into sympathetic neurons and adrenal chromaffin cells. However, recent studies have suggested that the adrenal cortex is dispensable for the acquisition of a chromaffin cell fate. This review summarizes the current understanding of the development of SA cells. It covers the specification of SA cells from multipotent NC crest cells, the role of transcription factors during their development, the classic model of their subsequent diversification as well as alternative views for explaining the generation of endocrine versus neuronal SA derivatives.
    [Show full text]
  • Seasonal Changes in the Fine Structure of the Basal
    J. Cell Set. 2, 401-410 (1967) 401 Printed in Great Britain SEASONAL CHANGES IN THE FINE STRUCTURE OF THE BASAL GRANULAR CELLS OF THE BAT THYROID E.A.NUNEZ Department of Radiology, Cornell University Medical School, New York City R. P. GOULD Department of Anatomy, The Middlesex Hospital Medical School, London D. W. HAMILTON Department of Anatomy, Harvard Medical School, Boston J. S. HAYWARD Department of Zoology, University of Alberta, Edmonton, Canada AND S. J. HOLT The Courtauld Institute of Biochemistry, The Middlesex Hospital Medical School, London SUMMARY The fine structure of the thyroid gland of non-hibernating, hibernating, and intermittently aroused hibernating bats was examined. It was found that in addition to the ordinary, follicular cell, another widespread thyroid cell type is present in all bats examined. This cell is situated in the basal region of the thyroid follicle and is characterized by a cytoplasm full of secretory- like granules. In the basal cells of bats captured in April and June the granules consist of an extremely dense core and are of a uniform size averaging from 0-1-0-5 /* i*1 diameter. In bats caught in August the solid dense granules vary greatly in size and large granules of diameters from 2 to 5 H are common. These large granules are often found concentrated in groups in the most basal region of the follicular epithelium. Hibernating bats are characterized by partly or totally degranulated basal thyroid cells. The cytoplasmic granules in the partly degranulated cell vary greatly in appearance, ranging from solid dense granules to empty vesicles.
    [Show full text]