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The Journal of experimental biology1994; 190; 239-252; doi: 10.1242/jeb.190.1.239

Extracellular ATP can activate autonomic signal transduction pathways in cultured equine sweat gland epithelial cells.

Abstract: Changes in intracellular free calcium concentration ([Ca2+]i) were monitored in a cell line that was derived from the equine sweat gland epithelium. ATP and closely related compounds could increase [Ca2+]i with a rank order of potency of UTP > or = ATP > ADP >> AMP = adenosine = alpha,beta-methylene-ATP. The responses to ATP and to UTP were initiated by the release of calcium from an internal store and subsequently sustained by calcium influx. The rise in [Ca2+]i thus seems to be mediated by P2U receptors that are coupled to phosphoinositidase C. Some desensitisation of this response developed during repeated stimulation with ATP and this was blocked by staurosporine, an inhibitor of protein kinase C, and augmented by a phorbol ester which acts as an exogenous activator of this enzyme. A protein-kinase-C-dependent inhibitory pathway thus seems to become active during repeated stimulation with ATP. ATP and related compounds could also raise cellular cyclic AMP content. The order of potency was ATP > ADP = AMP = adenosine >> UTP, suggesting that this response is mediated via a separate subclass of P2 receptor. The present results demonstrate that ATP can activate autonomic signal-transduction pathways in cultured equine sweat gland cells and suggest that there may be a purinergic component to the control of secretory activity in the equine sweat gland.
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Publication Date: 1994-05-01 PubMed ID: 7964393DOI: 10.1242/jeb.190.1.239Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This study explores the effect of ATP (a molecule involved in energy transfer) on the autonomic signal-transduction pathways in horse sweat gland cells. The research indicates ATP and related compounds can induce changes in intracellular free calcium concentrations, suggesting potential regulatory roles in secretion processes of the equine sweat gland.

Investigation of ATP’s effect on equine sweat gland cells

  • The focus of this research paper is to understand the influence of ATP (adenosine triphosphate) and related compounds on the intracellular concentration of free calcium ions ([Ca2+]i) in a cell line derived from the equine sweat gland epithelium.
  • The compounds evaluated alongside ATP include UTP, ADP, AMP, adenosine, and α,β-methylene-ATP. Presence of these compounds was found to increase the [Ca2+]i. In terms of potency, the rank order was observed as UTP ≥ ATP > ADP > AMP = adenosine = α,β-methylene-ATP.
  • The rise in [Ca2+]i is mediated by P2U receptors that are linked to phosphoinositidase C, beginning with a release of calcium from an internal store and sustained by calcium influx.

Role of different enzymes and pathway desensitisation

  • The paper also notes the development of desensitisation to this reaction upon repeated stimulation with ATP, which can be blocked by staurosporine. Staurosporine is an inhibitor of protein kinase C, an enzyme that regulates cellular functions.
  • A phorbol ester, an exogenous activator of protein kinase C, was found to increase desensitisation.
  • Consequently, repeated ATP stimulation appears to bring into action a protein-kinase-C-dependent inhibitory pathway.

The impact of ATP on cellular cyclic AMP content

  • The study also records that ATP and related compounds can increase the cyclic AMP content in the cell. The potency order was ATP > ADP = AMP = adenosine > UTP.
  • This observation indicates that this reaction is mediated via a different subclass of the P2 receptor.

Possibility of a purinergic component controlling secretory activity

  • The research suggests that ATP can activate autonomic signal transduction pathways in cultured equine sweat gland cells.
  • The findings propose that there could be a purinergic component involved in controlling the secretory activity of the equine sweat gland.

Cite This Article

APA
Ko WH, O'Dowd JJ, Pediani JD, Bovell DL, Elder HY, Jenkinson DM, Wilson SM. (1994). Extracellular ATP can activate autonomic signal transduction pathways in cultured equine sweat gland epithelial cells. J Exp Biol, 190, 239-252. https://doi.org/10.1242/jeb.190.1.239

Publication

The Journal of experimental biology
ISSN: 0022-0949
NlmUniqueID: 0243705
Country: England
Language: English
Volume: 190
Pages: 239-252

Researcher Affiliations

Ko, W H
  • Institute of Physiology, University of Glasgow.
O'Dowd, J J
    Pediani, J D
      Bovell, D L
        Elder, H Y
          Jenkinson, D M
            Wilson, S M

              MeSH Terms

              • Adenosine Triphosphate / pharmacology
              • Alkaloids / pharmacology
              • Animals
              • Calcium / metabolism
              • Cell Line
              • Cells, Cultured
              • Cyclic AMP / metabolism
              • Epithelium / metabolism
              • Horses / physiology
              • Phorbol Esters / pharmacology
              • Phosphoric Diester Hydrolases / metabolism
              • Receptors, Purinergic / metabolism
              • Signal Transduction / drug effects
              • Staurosporine
              • Sweat Glands / cytology
              • Sweat Glands / metabolism

              Citations

              This article has been cited 7 times.
              1. Patterson Rosa L, Mallicote MF, MacKay RJ, Brooks SA. Ion Channel and Ubiquitin Differential Expression during Erythromycin-Induced Anhidrosis in Foals. Animals (Basel) 2021 Nov 25;11(12).
                doi: 10.3390/ani11123379pubmed: 34944156google scholar: lookup
              2. Zamboulis DE, Senior JM, Clegg PD, Gallagher JA, Carter SD, Milner PI. Distribution of purinergic P2X receptors in the equine digit, cervical spinal cord and dorsal root ganglia. Purinergic Signal 2013 Sep;9(3):383-93.
                doi: 10.1007/s11302-013-9356-5pubmed: 23381684google scholar: lookup
              3. Pediani JD, McGrath JC, Wilson SM. P2Y receptor-mediated Ca2+ signalling in cultured rat aortic smooth muscle cells. Br J Pharmacol 1999 Apr;126(7):1660-6.
                doi: 10.1038/sj.bjp.0702470pubmed: 10323600google scholar: lookup
              4. Ko WH, Chan HC, Wong PY. Anion secretion induced by capacitative Ca2+ entry through apical and basolateral membranes of cultured equine sweat gland epithelium. J Physiol 1996 Nov 15;497 ( Pt 1)(Pt 1):19-29.
                doi: 10.1113/jphysiol.1996.sp021746pubmed: 8951708google scholar: lookup
              5. . Ion Transport in Health and Disease. Symposium proceedings. University College Cork, 19-20 September 1995. J Physiol 1995 Nov;489(P):1S-20S.
                doi: 10.1113/jphysiol.1995.sp021122pubmed: 8648565google scholar: lookup
              6. Pediani JD, Wilson SM. The effect of a phorbol ester upon the cholinergic regulation of potassium permeability in the rat submandibular gland. Experientia 1995 Feb 15;51(2):110-2.
                doi: 10.1007/BF01929350pubmed: 7875247google scholar: lookup
              7. Martin SC, Shuttleworth TJ. Activation by ATP of a P2U 'nucleotide' receptor in an exocrine cell. Br J Pharmacol 1995 May;115(2):321-9.
                doi: 10.1111/j.1476-5381.1995.tb15880.xpubmed: 7670734google scholar: lookup
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