Publication Date:
1996-05-03
Description:
The P2Z receptor is responsible for adenosine triphosphate (ATP)-dependent lysis of macrophages through the formation of membrane pores permeable to large molecules. Other ATP-gated channels, the P2X receptors, are permeable only to small cations. Here, an ATP receptor, the P2X7 receptor, was cloned from rat brain and exhibited both these properties. This protein is homologous to other P2X receptors but has a unique carboxyl-terminal domain that was required for the lytic actions of ATP. Thus, the P2X7 (or P2Z) receptor is a bifunctional molecule that could function in both fast synaptic transmission and the ATP-mediated lysis of antigen-presenting cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Surprenant, A -- Rassendren, F -- Kawashima, E -- North, R A -- Buell, G -- New York, N.Y. -- Science. 1996 May 3;272(5262):735-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Glaxo Institute for Molecular Biology, Geneva, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614837" target="_blank"〉PubMed〈/a〉
Keywords:
Adenosine Triphosphate/analogs & derivatives/*metabolism/pharmacology
;
Amino Acid Sequence
;
Animals
;
Base Sequence
;
Cations, Divalent/pharmacology
;
Cell Death
;
Cell Line
;
Cloning, Molecular
;
DNA, Complementary/genetics
;
Electric Conductivity
;
Humans
;
Ion Channels/physiology
;
Mice
;
Molecular Sequence Data
;
Patch-Clamp Techniques
;
Rats
;
Receptors, Purinergic P2/chemistry/genetics/*physiology
;
Receptors, Purinergic P2X7
;
Transfection
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
