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Journal articles on the topic 'Neurosecretion'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 November 2024

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1

Grundschober, Christophe, Maria Luisa Malosio, Laura Astolfi, Tiziana Giordano, Patrick Nef, and Jacopo Meldolesi. "Neurosecretion Competence." Journal of Biological Chemistry 277, no. 39 (June 17, 2002): 36715–24. http://dx.doi.org/10.1074/jbc.m203777200.

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2

Robinson, Linda J., and Thomas FJ Martin. "Docking and fusion in neurosecretion." Current Opinion in Cell Biology 10, no. 4 (August 1998): 483–92. http://dx.doi.org/10.1016/s0955-0674(98)80063-x.

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3

Predel, R., and Manfred Eckert. "Neurosecretion: peptidergic systems in insects." Naturwissenschaften 87, no. 8 (August 25, 2000): 343–50. http://dx.doi.org/10.1007/s001140050737.

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4

Brosius, D. C., J. T. Hackett, and J. B. Tuttle. "Ca(2+)-independent and Ca(2+)-dependent stimulation of quantal neurosecretion in avian ciliary ganglion neurons." Journal of Neurophysiology 68, no. 4 (October 1, 1992): 1229–34. http://dx.doi.org/10.1152/jn.1992.68.4.1229.

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1. Although it is generally agreed that Ca2+ couples depolarization to the release of neurotransmitters, hypertonic saline and ethanol (ETOH) evoke neurosecretion independent of extracellular Ca2+. One possible explanation is that these agents release Ca2+ from an intracellular store that then stimulates Ca(2+)-dependent neurosecretion. An alternative explanation is that these agents act independently of Ca2+. 2. This work extends previous observations on the action of ETOH and hypertonic solutions (HOSM) on neurons to include effects on [Ca2+]i. We have looked for Ca(2+)-independent or -dependent neurosecretion evoked by these agents in parasympathetic postganglionic neurons dissociated from chick ciliary ganglia and maintained in tissue culture. The change in concentration of free Ca2+ in the micromolar range inside neurons ([Ca2+]i) was measured with indo-1 with the use of a Meridian ACAS 470 laser scanning microspectrophotometer. 3. Elevated concentration of extracellular KCl increased [Ca2+]i and the frequency of quantal events. Also, a twofold increase in osmotic pressure (HOSM) produced a similar increase in quantal release and a significant rise in [Ca2+]i; however, the Ca2+ appeared to come from intracellular stores. 4. In contrast, ETOH stimulated quantal neurosecretion without a measurable change in [Ca2+]i. It appears the alcohol exerts its influence on some stage in the process of exocytosis that is distal to or independent of the site of Ca2+ action. 5. The effects of high [KCl]o and osmotic pressure were occlusive. This is explained in part by the observation that hypertonicity reduced Ca2+ current, but an action on Ca2+ stores is also likely.(ABSTRACT TRUNCATED AT 250 WORDS)

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5

Mishra, Nirmal Kumar. "Neurosecretion in reproductive behaviour of leeches." Journal of Biosciences 35, no. 3 (August 7, 2010): 327–28. http://dx.doi.org/10.1007/s12038-010-0036-0.

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6

Galoyan, A. "Neurosecretory Hypothalamus-Endocrine Heart as a Functional System." Physiology 7, no. 6 (December 1, 1992): 279–83. http://dx.doi.org/10.1152/physiologyonline.1992.7.6.279.

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Cardiac atrial neurosecretion is precisely regulated by cardiotropic protein-hormonal complexes, formed by neurosecretory nuclei of the hypothalamus. There is a close neurohumoral interrelation between the neuroendocrine heart and the hypothalamus.

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7

Dunlap, Karthleen, Jennifer I. Luebke, and Timothy J. Turner. "Identification of Calcium Channels That Control Neurosecretion." Science 266, no. 5186 (November 4, 1994): 828–30. http://dx.doi.org/10.1126/science.266.5186.828.b.

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8

Westerink, R. H. S., and A. G. Ewing. "The PC12 cell as model for neurosecretion." Acta Physiologica 192, no. 2 (November 15, 2007): 273–85. http://dx.doi.org/10.1111/j.1748-1716.2007.01805.x.

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9

Dunlap, K., J. Luebke, and T. Turner. "Identification of calcium channels that control neurosecretion." Science 266, no. 5186 (November 4, 1994): 828. http://dx.doi.org/10.1126/science.7973643.

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10

Dunlap, K., J. I. Luebke, and T. J. Turner. "Identification of Calcium Channels That Control Neurosecretion." Science 266, no. 5186 (November 4, 1994): 828–30. http://dx.doi.org/10.1126/science.266.5186.828-a.

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11

Klimenkov, Igor V., Aleksey V. Kurylev, Nikolay S. Kositsyn, Nikolay P. Sudakov, Mikhail V. Pastukhov, Sergey B. Nikiforov, Evgenii G. Belykh, and Vadim A. Byvaltsev. "Dendritic Neurosecretion Phenomenon of Olfactory Receptor Cells." World Neurosurgery 83, no. 3 (March 2015): 278–79. http://dx.doi.org/10.1016/j.wneu.2015.01.001.

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12

Cobb, J. L. S. "Neurohumors and neurosecretion in echinoderms: A review." Comparative Biochemistry and Physiology Part C: Comparative Pharmacology 91, no. 1 (January 1988): 151–58. http://dx.doi.org/10.1016/0742-8413(88)90181-8.

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13

Hays, R. M., N. Franki, H. Simon, and Y. Gao. "Antidiuretic hormone and exocytosis: lessons from neurosecretion." American Journal of Physiology-Cell Physiology 267, no. 6 (December 1, 1994): C1507—C1524. http://dx.doi.org/10.1152/ajpcell.1994.267.6.c1507.

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Many cells, both single and epithelial, are programmed for exocytosis. In most cases, the contents of cytoplasmic vesicles are delivered rapidly and directly to the extracellular fluid. The process has been intensively studied in the chromaffin cell and the nerve terminal, where, as in other cells, exocytosis is under a complex type of cytoskeletal control. An array of vesicle-associated proteins mediates attachment of the vesicles to the cytoskeleton, their release, and their fusion with the plasma membrane. Two functional pools of vesicles, the releasable and reserve pool, carry out immediate and long-term secretory activity. Some of the mediators of neurotransmitter vesicle fusion, originally thought to be restricted to neurosecretory cells, have now been found in nonneuronal cells. The mammalian collecting duct and the amphibian bladder are also engaged in exocytosis. In both epithelia, antidiuretic hormone (ADH) induces the transfer of water channels from cytoplasmic vesicles to the apical cell membrane. The process is slower than in the nerve terminal and ends with channel placement rather than the extrusion of vesicular contents. Nevertheless, there are several respects in which cytoskeletal control, vesicle positioning in the cell, docking, and fusion may prove to resemble the events in neurosecretion. This review begins with a survey of cytoskeletal structure and function in the erythrocyte, the chromaffin cell, and the nerve terminal and then presents current studies of ADH-induced exocytosis, emphasizing common themes in cytoskeletal control.

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14

Grattan, David R., and Armen N. Akopian. "Oscillating from Neurosecretion to Multitasking Dopamine Neurons." Cell Reports 15, no. 4 (April 2016): 681–82. http://dx.doi.org/10.1016/j.celrep.2016.04.013.

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15

Ramos-Miguel, Alfredo, J. Javier Meana, and Jesús A. García-Sevilla. "Cyclin-dependent kinase-5 and p35/p25 activators in schizophrenia and major depression prefrontal cortex: basal contents and effects of psychotropic medications." International Journal of Neuropsychopharmacology 16, no. 3 (April 1, 2013): 683–89. http://dx.doi.org/10.1017/s1461145712000879.

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AbstractCyclin-dependent kinase-5 (CDK5) and p35/p25 activators, interacting with the exocytotic machinery (e.g. munc18-1 and syntaxin-1A), play critical roles in neurosecretion. The basal status of CDK5/p35/p25 and the effect of psychotropic drugs (detected in blood/urine samples) were investigated in post-mortem prefrontal cortex (PFC)/Brodmann's area 9 of schizophrenia (SZ) and major depression (MD) subjects. In SZ (all subjects, n = 24), CDK5 and p35, but not p25, were reduced (−28 to −58%) compared to controls. In SZ antipsychotic-free (n = 12), activator p35 was decreased (−52%). In SZ antipsychotic-treated (n = 12), marked reductions of CDK5 (−47%), p35 (−76%) and p25 (−36%) were quantified. In MD (n = 13), including antidepressant-free/treated subgroups, CDK5, p35 and p25 were unaltered. In SZ (n = 24), CDK5, p35 or p25 correlated with munc18-1a, but not with syntaxin-1A. The results demonstrate reduced p35 basal content and down-regulation of CDK5/p35/p25 by antipsychotics in SZ. The suggested CDK5/munc18-1a functional interaction may lead to dysregulated neurosecretion in SZ PFC.

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16

Parsons, T. D., A. L. Obaid, and B. M. Salzberg. "Aminoglycoside antibiotics block voltage-dependent calcium channels in intact vertebrate nerve terminals." Journal of General Physiology 99, no. 4 (April 1, 1992): 491–504. http://dx.doi.org/10.1085/jgp.99.4.491.

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Intrinsic and extrinsic optical signals recorded from the intact nerve terminals of vertebrate neurohypophyses were used to investigate the anatomical site and physiological mechanism of the antagonistic effects of aminoglycoside antibiotics on neurotransmission. Aminoglycoside antibiotics blocked the intrinsic light scattering signal closely associated with neurosecretion in the mouse neurohypophysis in a concentration-dependent manner with an IC50 of approximately 60 microM and the block was relieved by increasing [Ca2+]o. The rank order potency of different aminoglycoside antibiotics for blocking neurosecretion in this preparation was determined to be: neomycin greater than gentamicin = kanamycin greater than streptomycin. Optical recordings of rapid changes in membrane potential using voltage-sensitive dyes revealed that aminoglycoside antibiotics decreased the Ca(2+)-dependent after-hyperpolarization of the normal action potential and both the magnitude and after-hyperpolarization of the regenerative Ca2+ spike. The after-hyperpolarization results from a Ca-activated potassium conductance whose block by aminoglycoside antibiotics was also reversed by increased [Ca2+]o. These studies demonstrate that the capacity of aminoglycoside antibiotics to antagonize neurotransmission can be attributed to the block of Ca channels in the nerve terminal.

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17

Gil, Amparo, Virginia González-Vélez, Luis Miguel Gutiérrez, and José Villanueva. "The Role of Nicotinic Receptors on Ca2+ Signaling in Bovine Chromaffin Cells." Current Issues in Molecular Biology 46, no. 1 (January 17, 2024): 808–20. http://dx.doi.org/10.3390/cimb46010052.

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Chromaffin cells have been used as a physiological model to understand neurosecretion in mammals for many years. Nicotinic receptors located in the cells’ membrane are stimulated by acetylcholine, and they participate in the exocytosis of chromaffin granules, releasing catecholamines in response to stress. In this work, we discuss how the participation of nicotinic receptors and the localization of active zones in the borders of the cytoskeleton can generate local calcium signals leading to secretion. We use a computational model of a cytoskeleton cage to simulate Ca2+ levels in response to voltage and acetylcholine pulses. We find that nicotinic receptors are able to enhance the differences between local and average calcium values, as well as the heterogeneous distributions around the active zones, producing a non-linear, highly localized Ca2+ entry that, although consisting of a few ions, is able to improve secretion responses in chromaffin cells. Our findings emphasize the intricate interplay among nicotinic receptors, the cytoskeleton, and active zones within chromaffin cells as an example of Ca2+-dependent neurosecretion in mammals.

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18

Scharrer, Berta. "Neurosecretion: Beginnings and New Directions in Neuropeptide Research." Annual Review of Neuroscience 10, no. 1 (March 1987): 1–18. http://dx.doi.org/10.1146/annurev.ne.10.030187.000245.

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19

Thesleff, S., L. C. Sellin, and S. Tågerud. "Tetrahydroaminoacridine (tacrine) stimulates neurosecretion at mammalian motor endplates." British Journal of Pharmacology 100, no. 3 (July 1990): 487–90. http://dx.doi.org/10.1111/j.1476-5381.1990.tb15834.x.

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20

Neher, Erwin. "Neurosecretion: what can we learn from chromaffin cells." Pflügers Archiv - European Journal of Physiology 470, no. 1 (August 11, 2017): 7–11. http://dx.doi.org/10.1007/s00424-017-2051-6.

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21

Han, Gayoung A., Nancy T. Malintan, Brett M. Collins, Frederic A. Meunier, and Shuzo Sugita. "Munc18-1 as a key regulator of neurosecretion." Journal of Neurochemistry 115, no. 1 (July 30, 2010): 1–10. http://dx.doi.org/10.1111/j.1471-4159.2010.06900.x.

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22

Martin, Thomas F. J. "The molecular machinery for fast and slow neurosecretion." Current Opinion in Neurobiology 4, no. 5 (October 1994): 626–32. http://dx.doi.org/10.1016/0959-4388(94)90002-7.

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23

Orio, Patricio, Patricio Rojas, Gonzalo Ferreira, and Ramón Latorre. "New Disguises for an Old Channel: MaxiK Channel β-Subunits." Physiology 17, no. 4 (August 2002): 156–61. http://dx.doi.org/10.1152/nips.01387.2002.

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Ca2+-activated K+ channels of large conductance (MaxiK or BK channels) control a large variety of physiological processes, including smooth muscle tone, neurosecretion, and hearing. Despite being coded by a single gene (Slowpoke), the diversity of MaxiK channels is great. Regulatory b-subunits, splicing, and metabolic regulation create this diversity fundamental to the adequate function of many tissues.

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24

Kwong, J., F. L. Roundabush, P. Hutton Moore, M. Montague, W. Oldham, Y. Li, L. S. Chin, and L. Li. "Hrs interacts with SNAP-25 and regulates Ca(2+)-dependent exocytosis." Journal of Cell Science 113, no. 12 (June 15, 2000): 2273–84. http://dx.doi.org/10.1242/jcs.113.12.2273.

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Synaptosome-associated protein of 25 kDa (SNAP-25) is a neuronal membrane protein essential for synaptic vesicle exocytosis. To investigate the mechanisms by which SNAP-25 mediates neurosecretion, we performed a search for proteins that interact with SNAP-25 using a yeast two-hybrid screen. Here, we report the isolation and characterization of a SNAP-25-interacting protein that is the rat homologue of mouse hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs). Hrs specifically interacts with SNAP-25, but not SNAP-23/syndet. The association of Hrs and SNAP-25 is mediated via coiled-coil interactions. Using an Hrs-specific antibody, we have shown that Hrs is highly enriched in brain, where it codistributes with SNAP-25 in most brain regions. Subcellular fractionation studies demonstrate that in brain, Hrs exists in both cytosolic and membrane-associated pools. Studies using indirect immunofluorescence and confocal microscopy reveal that, in addition to early endosomes, Hrs is also localized to large dense-core secretory granules and synaptic-like microvesicles in nerve growth factor-differentiated PC12 cells. Moreover, overexpression of Hrs in PC12 cells inhibits Ca(2+)-dependent exocytosis. These results suggest that Hrs is involved in regulation of neurosecretion through interaction with SNAP-25.

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25

Sawin, Clark T. "Berta and Ernst Scharrer and the Concept of Neurosecretion." Endocrinologist 13, no. 2 (March 2003): 73–76. http://dx.doi.org/10.1097/01.ten.0000076205.95014.f9.

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26

Zeniou-Meyer, M., F. Gambino, Mohamed-Raafet Ammar, Y. Humeau, and N. Vitale. "The Coffin-Lowry Syndrome-Associated Protein rsk2 and Neurosecretion." Cellular and Molecular Neurobiology 30, no. 8 (November 2010): 1401–6. http://dx.doi.org/10.1007/s10571-010-9578-9.

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27

Himmelreich, N. H., A. G. Storchak, and N. G. Pozdniakova. "α-Latrotoxin-stimulated neurosecretion: The role of calcium ions." Neurophysiology 30, no. 4-5 (July 1998): 199. http://dx.doi.org/10.1007/bf02462814.

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28

Lando, L., and R. S. Zucker. "Ca2+ cooperativity in neurosecretion measured using photolabile Ca2+ chelators." Journal of Neurophysiology 72, no. 2 (August 1, 1994): 825–30. http://dx.doi.org/10.1152/jn.1994.72.2.825.

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1. The photolabile Ca2+ chelator DM-nitrophen was injected into crayfish motor neuron terminals and photolyzed with light flashes of different intensity to determine the cooperativity of Ca2+ action in releasing neurotransmitter. 2. Each flash elicited a phasic postsynaptic response resembling an excitatory junctional potential, apparently due to a presynaptic ”spike” in intracellular calcium concentration ([Ca2+]i). 3. When postsynaptic currents were measured under voltage clamp, a Ca2+ cooperativity of approximately 3–4 was inferred from a supralinear dependence of responses on changes in peak [Ca2+]i caused by flashes differing in intensity by 32–46%. 4. A similar Ca2+ cooperativity was inferred from postsynaptic potentials in response to flashes of varying intensity. 5. The time course of transmitter release indicated by flash responses had slightly slower rising and falling phases than excitatory postsynaptic potentials. There was also a slow tail of transmitter release lasting for approximately 200 ms after a flash. 6. This time course was explained quantitatively by simulations of DM-nitrophen photolysis and binding reactions and a model of Ca2+ activation of transmitter release.

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29

RASMUSSEN, D. D., J. H. LIU, W. H. SWARTZ, V. S. TUEROS, and S. S. C. YEN. "HUMAN FETAL HYPOTHALAMIC GnRH NEUROSECRETION: DOPAMINERGIC REGULATION IN VITRO." Clinical Endocrinology 25, no. 2 (August 1986): 127–32. http://dx.doi.org/10.1111/j.1365-2265.1986.tb01673.x.

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30

Kasatkina, Ludmila A., Vitaliy P. Gumenyuk, Eva M. Sturm, Akos Heinemann, Tytus Bernas, and Irene O. Trikash. "Modulation of neurosecretion and approaches for its multistep analysis." Biochimica et Biophysica Acta (BBA) - General Subjects 1862, no. 12 (December 2018): 2701–13. http://dx.doi.org/10.1016/j.bbagen.2018.08.004.

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31

Klowden, Marc J. "Contributions of insect research toward our understanding of neurosecretion." Archives of Insect Biochemistry and Physiology 53, no. 3 (June 11, 2003): 101–14. http://dx.doi.org/10.1002/arch.10093.

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32

Fairweather, I., and D. W. Halton. "Neuropeptides in platyhelminths." Parasitology 102, S1 (January 1991): S77—S92. http://dx.doi.org/10.1017/s0031182000073315.

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The neuropeptide story began in 1928 with the description by Ernst Scharrer of gland-like nerve cells in the hypothalamus of the minnow, Phoxinus laevis. Because these nerve cells were overwhelmingly specialized for secretory activity, overshadowing other neuronal properties, Scharrer termed them ‘neurosecretory neurons’. What was even more remarkable about the cells was that their products were released into the bloodstream to act as hormones, specifically neurohormones. Neurosecretory cells were identified largely on morphological grounds. That is, they could be stained with special techniques, such as chrome-haematoxylin and paraldehyde-fuchsin, although the techniques are far from specific, staining non-neurosecretory cells as well. However, the basis for the ‘special’ neurosecretory techniques is the demonstration of sulphur-containing proteins – so they are indicative of peptide-producing neurones. An alternative characteristic of neurosecretory cells is the presence of large (> 100 nm), dense-cored vesicles at the electron microscope level; these are the so-called elementary granules of neurosecretion, or ENGs. However, implicit in the concept of neurosecretion is that the prime function of the neurosecretory cell is in endocrine regulation, exerting a hormone-like control over some aspect of the organism's metabolism, by controlling endocrine glands and other effector organs. To satisfy this criterion, evidence had to be obtained of cycles of secretory activity within the cell that could be correlated with a change in the physiological condition of the organism.

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33

Lightman, S. L. "The neuroendocrine paraventricular hypothalamus: receptors, signal transduction, mRNA and neurosecretion." Journal of Experimental Biology 139, no. 1 (September 1, 1988): 31–49. http://dx.doi.org/10.1242/jeb.139.1.31.

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The hypothalamus is one of the most studied areas of the central nervous system. Many of its functions are understood and there is an extensive literature on its role in the control of pituitary hormone secretion, autonomic nervous system activity, regulation of salt, water and food ingestion, body temperature regulation and aspects of behaviour. Although the role of the hypothalamus in the control of pituitary secretion was postulated in the early 1900s, the chemical nature of these control mechanisms has only been documented in the last few years. The opioid peptides represent one particular family of chemical compounds which have been shown to have many effects on pituitary hormone secretion. Exogenous opioids inhibit the neurosecretion of both vasopressin and oxytocin from the posterior pituitary neurosecretory terminals of hypothalamic cell bodies. Opioids also have major actions on the secretory activity of the anterior pituitary which has no innervation from the hypothalamus, but which is regulated by blood-borne factors in the hypophyseal portal circulation which runs from the median eminence of the hypothalamus. It was therefore of considerable interest when it was discovered that endogenous opioid peptides could be detected both in the neurohypophyseal system and in cells which project into the median eminence. The simple presence of a peptide in a neurone does not necessarily imply a function. If, however, we can demonstrate that regulation of the synthesis of the peptide occurs in a manner which corresponds with the expected role of the agent, this provides powerful data in support of a genuine physiological function. The elucidation of the genomic structure of the precursors for the three endogenous opioid peptides has provided us with the ability to measure mRNA for these peptides in defined areas of the brain and to assess their response to appropriate stimuli. Not only does mRNA for the endogenous opioid dynorphin coexist in the same cells as vasopressin but we have now been able to demonstrate that stimuli to vasopressin secretion also result in a markedly increased accumulation of dynorphin mRNA. Similarly, previous studies have shown that opioid peptides derived from another precursor--pro-enkephalin A--coexist with corticotrophin releasing factor in a different group of hypothalamic cells. We have now been able to demonstrate that stresses which result in an accumulation of corticotrophin releasing factor mRNA also result in increased pro-enkephalin mRNA in the same area. This considerably strengthens the hypothesis that endogenous opioids do play a significant role in the control of hypophyseal secretion.(ABSTRACT TRUNCATED AT 400 WORDS)

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34

Oka, Kazuyuki, and Naokuni Takeda. "Relationship between neurosecretion and spermatogenesis in the leech, Erpobdella lineata." Comparative Biochemistry and Physiology Part A: Physiology 84, no. 3 (January 1986): 421–25. http://dx.doi.org/10.1016/0300-9629(86)90340-3.

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35

Subrahmanyam, Bhattiprolu, Thomas Müller, and Heinz Rembold. "Inhibition of turnover of neurosecretion by azadirachtin in Locusta migratoria." Journal of Insect Physiology 35, no. 6 (January 1989): 493–500. http://dx.doi.org/10.1016/0022-1910(89)90056-5.

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36

Tsuda, Kazushi, Hiroki Shima, Masato Kuchii, Ichiro Nishio, and Yoshiaki Masuyama. "Effects of Captopril on Neurosecretion and Vascular Responsiveness in Hypertension." Clinical and Experimental Hypertension. Part A: Theory and Practice 9, no. 2-3 (January 1987): 375–79. http://dx.doi.org/10.3109/10641968709164200.

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37

Thapliyal, Ashish, Rashmi Verma, and Navin Kumar. "Small G Proteins Dexras1 and RHES and Their Role in Pathophysiological Processes." International Journal of Cell Biology 2014 (2014): 1–10. http://dx.doi.org/10.1155/2014/308535.

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Dexras1 and RHES, monomeric G proteins, are members of small GTPase family that are involved in modulation of pathophysiological processes. Dexras1 and RHES levels are modulated by hormones and Dexras1 expression undergoes circadian fluctuations. Both these GTPases are capable of modulating calcium ion channels which in turn can potentially modulate neurosecretion/hormonal release. These two GTPases have been reported to prevent the aberrant cell growth and induce apoptosis in cell lines. Present review focuses on role of these two monomeric GTPases and summarizes their role in pathophysiological processes.

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38

Acosta-Martínez, Maricedes, Ji Luo, Carol Elias, Andrew Wolfe, and Jon E. Levine. "Male-Biased Effects of Gonadotropin-Releasing Hormone Neuron-Specific Deletion of the Phosphoinositide 3-Kinase Regulatory Subunit p85α on the Reproductive Axis." Endocrinology 150, no. 9 (June 18, 2009): 4203–12. http://dx.doi.org/10.1210/en.2008-1753.

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Abstract GnRH neurosecretion is subject to regulation by insulin, IGF-I, leptin, and other neuroendocrine modulators whose effects may be conveyed by activation of phosphoinositide 3-kinase (PI3K)-mediated pathways. It is not known, however, whether any of these regulatory actions are exerted directly, via activation of PI3K in GnRH neurons, or whether they are primarily conveyed via effects on afferent circuitries governing GnRH neurosecretion. To investigate the role of PI3K signaling in GnRH neurons, we used conditional gene targeting to ablate expression of the major PI3K regulatory subunit, p85α, in GnRH neurons. Combined in situ hybridization and immunohistochemistry confirmed reduction of p85α mRNA expression in GnRH neurons of GnRH-p85α knockout (KO) animals. Females of both genotypes exhibited estrous cyclicity and had comparable serum LH, estradiol-17β, and FSH levels. In male GnRH-p85αKO mice, serum LH, testosterone, and sperm counts were significantly reduced compared with wild type. To investigate the role of the other major regulatory subunit, p85β, on the direct control of GnRH neuronal function, we generated mice with a GnRH-neuron-specific p85α deletion on a global βKO background. No additional reproductive effects in male or female mice were found, suggesting that p85β does not substitute p85 activity toward PI3K function in GnRH neurons. Our results suggest that p85α, and thus PI3K activity, participates in the control of GnRH neuronal activity in male mice. The sex-specific phenotype in these mice raises the possibility that PI3K activation during early development may establish sex differences in GnRH neuronal function.

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39

Todd, Robert D., Sarah M. McDavid, Rebecca L. Brindley, Mark L. Jewell, and Kevin P. M. Currie. "Gabapentin Inhibits Catecholamine Release from Adrenal Chromaffin Cells." Anesthesiology 116, no. 5 (May 1, 2012): 1013–24. http://dx.doi.org/10.1097/aln.0b013e31825153ea.

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Background Gabapentin is most commonly prescribed for chronic pain, but acute perioperative effects, including preemptive analgesia and hemodynamic stabilization, have been reported. Adrenal chromaffin cells are a widely used model to investigate neurosecretion, and adrenal catecholamines play important physiologic roles and contribute to the acute stress response. However, the effects of gabapentin on adrenal catecholamine release have never been tested. Methods Primary cultures of bovine adrenal chromaffin cells were treated with gabapentin or vehicle for 18-24 h. The authors quantified catecholamine secretion from dishes of cells using high-performance liquid chromatography and resolved exocytosis of individual secretory vesicles from single cells using carbon fiber amperometry. Voltage-gated calcium channel currents were recorded using patch clamp electrophysiology and intracellular [Ca2+] using fluorescent imaging. Results Gabapentin produced statistically significant reductions in catecholamine secretion evoked by cholinergic agonists (24 ± 3%, n = 12) or KCl (16 ± 4%, n = 8) (mean ± SEM) but did not inhibit Ca2+ entry or calcium channel currents. Amperometry (n = 51 cells) revealed that gabapentin inhibited the number of vesicles released upon stimulation, with no change in quantal size or kinetics of these unitary events. Conclusions The authors show Ca2+ entry was not inhibited by gabapentin but was less effective at triggering vesicle fusion. The work also demonstrates that chromaffin cells are a useful model for additional investigation of the cellular mechanism(s) by which gabapentin controls neurosecretion. In addition, it identifies altered adrenal catecholamine release as a potential contributor to some of the beneficial perioperative effects of gabapentin.

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Beltran, Beatriz, Romen Carrillo, Tomas Martin, Victor S. Martin, Jose D. Machado, and Ricardo Borges. "Fluorescent β-Blockers as Tools to Study Presynaptic Mechanisms of Neurosecretion." Pharmaceuticals 4, no. 5 (April 28, 2011): 713–25. http://dx.doi.org/10.3390/ph4050713.

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RASMUSSEN, DENNIS D., JAMES H. LIU, PAUL L. WOLF, and SAMUEL S. C. YEN. "Gonadotropin-Releasing Hormone Neurosecretion in the Human Hypothalamus:In VitroRegulation by Dopamine*." Journal of Clinical Endocrinology & Metabolism 62, no. 3 (March 1986): 479–83. http://dx.doi.org/10.1210/jcem-62-3-479.

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Sawn, Clark T. "Ulf Svante von Euler (1905–1983) and the Neurosecretion of Norepinephrine." Endocrinologist 9, no. 5 (September 1999): 327–30. http://dx.doi.org/10.1097/00019616-199909000-00001.

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Taverna, Elena, Elena Saba, Anna Linetti, Renato Longhi, Andreas Jeromin, Marco Righi, Francesco Clementi, and Patrizia Rosa. "Localization of synaptic proteins involved in neurosecretion in different membrane microdomains." Journal of Neurochemistry 100, no. 3 (February 2007): 664–77. http://dx.doi.org/10.1111/j.1471-4159.2006.04225.x.

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Golding, David W., and David V. Pow. "‘Neurosecretion’ by Synaptic Terminals and Glandular Discharge in the Endocrine Pancreas." Neuroendocrinology 51, no. 4 (1990): 369–75. http://dx.doi.org/10.1159/000125363.

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Kichko, T. I., S. Haux-Oertel, I. Izydorczyk, and P. W. Reeh. "189 STIMULATED NEUROSECRETION IN THE ISOLATED TRACHEA OF TRPV1 MUTANT MICE." European Journal of Pain 10, S1 (September 2006): S52. http://dx.doi.org/10.1016/s1090-3801(06)60192-4.

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Grundschober, Christophe, Maria Luisa Malosio, Laura Astolfi, Tiziana Giordano, Patrick Nef, and Jacopo Meldolesi. "Neurosecretion competence. A comprehensive gene expression program identified in PC12 cells." Journal of Biological Chemistry 277, no. 48 (November 2002): 46840. http://dx.doi.org/10.1016/s0021-9258(19)33304-6.

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Romano, Adele, Tommaso Cassano, Bianca Tempesta, Silvia Cianci, Pasqua Dipasquale, Roberto Coccurello, Vincenzo Cuomo, and Silvana Gaetani. "The satiety signal oleoylethanolamide stimulates oxytocin neurosecretion from rat hypothalamic neurons." Peptides 49 (November 2013): 21–26. http://dx.doi.org/10.1016/j.peptides.2013.08.006.

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Sapronov, N. S., and I. I. Stepanov. "Humoral component of regeneration and learning is a subcase of neurosecretion." European Neuropsychopharmacology 10 (September 2000): 384. http://dx.doi.org/10.1016/s0924-977x(00)80528-3.

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Law, Chris, Matthijs Verhage, and Artur Kania. "ISDN2014_0279: Spinal neuron identity and survival in the absence of neurosecretion." International Journal of Developmental Neuroscience 47, Part_A (December 2015): 83. http://dx.doi.org/10.1016/j.ijdevneu.2015.04.227.

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Kasatkina, L., E. Sturm, A. Heinemann, and I. Trikash. "Modulation of neurosecretion by levetiracetam and approaches for its multistep analysis." European Neuropsychopharmacology 29 (2019): S282—S283. http://dx.doi.org/10.1016/j.euroneuro.2018.11.445.

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