Extracellular ATP activates receptor‐operated cation channels in mouse lacrimal acinar cells to promote calcium influx in the absence of phosphoinositide metabolism

Sasaki, Takuma; Gallacher, D V

doi:10.1016/0014-5793(90)80782-e

Cited by 88 publications

(71 citation statements)

References 17 publications

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“…Reverse transcriptase polymerase chain reaction (RT-PCR) analysis on single acini from the rat pancreas revealed that they contain transcripts for P2X 1 , P2X 4 , P2Y 2 and P2Y 4 receptors [77]. Interestingly, no transcript for P2X 7 receptors was found, although these receptors are expressed in ducts (see below) and also in acini of other exocrine glands [78][79][80][81]. Clearly, P2X 7 receptors, which can form lytic pores under some conditions, would be dangerous in pancreatic acini filled with digestive enzymes.…”

Section: Pancreatic Acinimentioning

confidence: 99%

“…In comparison, about 90% of acini prepared from other exocrine glands (e.g. salivary and lachrymal glands) using similar methods respond to ATP, although there is a functional heterogeneity in P2X 4 , P2Y 2 and P2Y 1 receptors, and these acini also express P2X 7 receptors [78,79,81,[83][84][85][86][87][88]. It is also established in exocrine gland acini that distribution and function of some P2 receptor is influenced by the developmental state, innervation and duration of cell culture [78,[87][88][89][90].…”

Section: Pancreatic Acinimentioning

confidence: 99%

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Purinergic receptors in the endocrine and exocrine pancreas

Novak

2007

Purinergic Signalling

115

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The pancreas is a complex gland performing both endocrine and exocrine functions. In recent years there has been increasing evidence that both endocrine and exocrine cells possess purinergic receptors, which influence processes such as insulin secretion and epithelial ion transport. Most commonly, these processes have been viewed separately. In β cells, stimulation of P2Y 1 receptors amplifies secretion of insulin in the presence of glucose. Nucleotides released from secretory granules could also contribute to autocrine/paracrine regulation in pancreatic islets. In addition to P2Y 1 receptors, there is also evidence for other P2 and adenosine receptors in β cells (P2Y 2 , P2Y 4 , P2Y 6 , P2X subtypes and A 1 receptors) and in glucagon-secreting α cells (P2X 7 , A 2 receptors). In the exocrine pancreas, acini release ATP and ATP-hydrolysing and ATP-generating enzymes. P2 receptors are prominent in pancreatic ducts, and several studies indicate that P2Y 2 , P2Y 4 , P2Y 11 , P2X 4 and P2X 7 receptors could regulate secretion, primarily by affecting Cl − and K + channels and intracellular Ca 2+ signalling. In order to understand the physiology of the whole organ, it is necessary to consider the full complement of purinergic receptors on different cells as well as the structural and functional relation between various cells within the whole organ. In addition to the possible physiological function of purinergic receptors, this review analyses whether the receptors could be potential therapeutic targets for drug design aimed at treatment of pancreatic diseases.

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Section: Pancreatic Acinimentioning

confidence: 99%

Section: Pancreatic Acinimentioning

confidence: 99%

Purinergic receptors in the endocrine and exocrine pancreas

Novak

2007

Purinergic Signalling

115

View full text Add to dashboard Cite

show abstract

“…Позаклітинний АТР спричинює збільшення цитозольної концентрації Са 2+ в екзокринних ацинарних клітинах різних залоз, взаємодіючи з Р2-типом пуринорецепторів [33][34][35]. Із цієї групи, в базальній мембрані ацинарних клітин сльозових залоз мишей, екс пресуються Р2Y 11 і Р2Y 13 -рецептори [36].…”

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IP(3)-sensitive Ca(2+)-channels of endoplasmic reticulum in secretory cells of the rat exorbital lacrimal gland

Kotliarova¹,

Manko²

2013

Ukr.Biochem.J.

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“…Examples include receptor-gated channels (12), channels activated by second messengers such as cyclic nucleotides (13), phosphatidylinositol 3,4,5-trisphosphate (14), and arachidonic acid (15,16) (for a review see Refs. 17 and 18).…”

mentioning

confidence: 99%

Mutual Antagonism of Calcium Entry by Capacitative and Arachidonic Acid-mediated Calcium Entry Pathways

Luo¹,

Broad²,

Bird

et al. 2001

Journal of Biological Chemistry

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In nonexcitable cells, the predominant mechanism for regulated entry of Ca 2؉ is capacitative calcium entry, whereby depletion of intracellular Ca 2؉ stores signals the activation of plasma membrane calcium channels. A number of other regulated Ca 2؉ entry pathways occur in specific cell types, however, and it is not know to what degree the different pathways interact when present in the same cell. In this study, we have examined the interaction between capacitative calcium entry and arachidonic acid-activated calcium entry, which co-exist in HEK293 cells. These two pathways exhibit mutual antagonism. That is, capacitative calcium entry is potently inhibited by arachidonic acid, and arachidonic acid-activated entry is inhibited by the pre-activation of capacitative calcium entry with thapsigargin. In the latter case, the inhibition does not seem to result from a direct action of thapsigargin, inhibition of endoplasmic reticulum Ca 2؉ pumps, depletion of Ca 2؉ stores, or entry of Ca 2؉ through capacitative calcium entry channels. Rather, it seems that a discrete step in the pathway signaling capacitative calcium entry interacts with and inhibits the arachidonic acid pathway. The findings reveal a novel process of mutual antagonism between two distinct calcium entry pathways. This mutual antagonism may provide an important protective mechanism for the cell, guarding against toxic Ca 2؉ overload.

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Extracellular ATP activates receptor‐operated cation channels in mouse lacrimal acinar cells to promote calcium influx in the absence of phosphoinositide metabolism

Cited by 88 publications

References 17 publications

Purinergic receptors in the endocrine and exocrine pancreas

Purinergic receptors in the endocrine and exocrine pancreas

IP(3)-sensitive Ca(2+)-channels of endoplasmic reticulum in secretory cells of the rat exorbital lacrimal gland

Mutual Antagonism of Calcium Entry by Capacitative and Arachidonic Acid-mediated Calcium Entry Pathways

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