Literature DB >> 8772140

Temperature dependence of release of vesicular content in bovine chromaffin cells.

A Walker1, M I Glavinović, J Trifaró.   

Abstract

Recent studies suggest that the time course of secretion of the vesicular content in bovine chromaffin cells is much slower than in the peripheral or the central nervous system, but the reasons for this marked difference are not known. In this study we try to assess the importance of factors that may influence the time course of release of the vesicular content of bovine chromaffin cells, namely: (1) diffusion of catecholamines in the extracellular solution, (2) dissociation of catecholamines from the matrix of chromogranin A, and (3) the kinetics of opening and closing of the fusion pore. The temperature dependence of the time course and the amplitude of the spontaneous current spikes were examined using the carbon filament recording technique in amperometric mode. The change in amplitude was not statistically significant, but both the rise and the decay times were shortened (from 29 +/- 12 to 16 +/- 5 ms, and from 87 +/- 26 to 57 +/- 11 ms respectively) as temperature was raised by 20 degrees C [from 15 to 35 degrees C; n = 6; the changes were statistically significant at the level of P = 0.05; their respective temperature coefficients (Q10) were 1.4 and 1.3]. The areas underneath the spontaneous current spikes, however, were not altered significantly. Neither the relationship between the rise and the decay times nor the frequency of occurrence of the spontaneous current spikes changed consistently as the temperature was raised. However, the frequency histograms could, in all cases, be well described by a monoexponential function. It is concluded that the release of catecholamine content from the individual vesicles in bovine chromaffin cells is probably mostly determined by the dissociation of catecholamines from the matrix of chromogranin A.

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Year:  1996        PMID: 8772140     DOI: 10.1007/s004240050212

Source DB:  PubMed          Journal:  Pflugers Arch        ISSN: 0031-6768            Impact factor:   3.657


  22 in total

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Journal:  J Physiol       Date:  1978-06       Impact factor: 5.182

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Journal:  J Physiol       Date:  1978-01       Impact factor: 5.182

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Journal:  J Biol Chem       Date:  1994-06-24       Impact factor: 5.157

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Journal:  Neuroscience       Date:  1980       Impact factor: 3.590

8.  Temporal characteristics of quantal secretion of catecholamines from adrenal medullary cells.

Authors:  J A Jankowski; T J Schroeder; E L Ciolkowski; R M Wightman
Journal:  J Biol Chem       Date:  1993-07-15       Impact factor: 5.157

9.  Dimerization and tetramerization properties of the C-terminal region of chromogranin A: a thermodynamic analysis.

Authors:  S H Yoo; M S Lewis
Journal:  Biochemistry       Date:  1993-08-31       Impact factor: 3.162

Review 10.  Mucin exocytosis.

Authors:  P Verdugo
Journal:  Am Rev Respir Dis       Date:  1991-09
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  7 in total

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Authors:  Christy L Haynes; Lauren N Siff; R Mark Wightman
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2.  Temperature dependence of vesicular dynamics at excitatory synapses of rat hippocampus.

Authors:  Loc Bui; Mladen I Glavinović
Journal:  Cogn Neurodyn       Date:  2014-02-19       Impact factor: 5.082

Review 3.  Secretory vesicle pools and rate and kinetics of single vesicle exocytosis in neurosecretory cells.

Authors:  J M Trifaró; M Glavinovic; S D Rosé
Journal:  Neurochem Res       Date:  1997-07       Impact factor: 3.996

4.  Regulation by L channels of Ca(2+)-evoked secretory responses in ouabain-treated chromaffin cells.

Authors:  Ricardo De Pascual; Inés Colmena; Lucía Ruiz-Pascual; Andrés Mateo Baraibar; Javier Egea; Luis Gandía; Antonio G García
Journal:  Pflugers Arch       Date:  2016-08-24       Impact factor: 3.657

5.  Facilitation of quantal release induced by a D1-like receptor on bovine chromaffin cells.

Authors:  Melissa Villanueva; R Mark Wightman
Journal:  Biochemistry       Date:  2007-03-06       Impact factor: 3.162

6.  Novel features on the regulation by mitochondria of calcium and secretion transients in chromaffin cells challenged with acetylcholine at 37°C.

Authors:  Afonso Caricati-Neto; Juan-Fernando Padín; Edilson-Dantas Silva-Junior; José-Carlos Fernández-Morales; Antonio-Miguel G de Diego; Aron Jurkiewicz; Antonio G García
Journal:  Physiol Rep       Date:  2013-12-19

7.  Multiple Mechanisms Driving F-actin-Dependent Transport of Organelles to and From Secretory Sites in Bovine Chromaffin Cells.

Authors:  Yolanda Gimenez-Molina; José Villanueva; Maria Del Mar Francés; Salvador Viniegra; Luis M Gutiérrez
Journal:  Front Cell Neurosci       Date:  2018-10-09       Impact factor: 5.505

  7 in total

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