These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: ADP-induced rapid inward currents through Ca(2+)-permeable cation channels in mouse, rat and guinea-pig megakaryocytes: a patch-clamp study. Author: Kawa K. Journal: J Physiol; 1996 Sep 01; 495 ( Pt 2)(Pt 2):339-52. PubMed ID: 8887748. Abstract: 1. The rapid inward currents in mouse megakaryocytes evoked by adenosine diphosphate (ADP), a ubiquitous platelet-activating substance, were studied. Time and current resolution were improved by using patch-clamp recording and an extracellular fast perfusion ("Y tube') technique. 2. Application of ADP (40 microM) to megakaryocytes immersed in physiological saline evoked rapid inward currents (80-340 pA at -42 mV). The cellular responses to a second ADP application were markedly reduced, but in the absence of external Ca2+, responses to repeated ADP application were maintained and did not deteriorate. 3. The ADP-induced current recorded in Ca(2+)-free external media showed short latency (less than 20 ms) and approximately exponential decay (time constant, 300-500 ms), which was independent of the holding potential and seemed to be caused mainly by receptor desensitization; it took over 5.5 min for complete recovery. 4. The ADP concentration response relationship of the megakaryocytes revealed that the half-maximal concentration and the Hill coefficient were 12.6 microM and 1.4, respectively. 5. An ion replacement experiment showed that the ADP-induced currents could be carried by Na+, Cs+ and K+, but not Cl-, and the cation channels were permeable to Ca2+, Ba2+ and Mg2+. 6. Neither Ca2+ chelators (10 mM EGTA and 10 mM BAPTA) nor hydrolysis-resistant guanine nucleotides (2 mM GDP-beta-S and 0.4 mM 5'-guanylylimidodiphosphate) in the internal saline affected the rapid responses to ADP, and ADP-induced currents were recorded in excised membrane patches, suggesting that the ADP receptor site and the molecular structure forming the cation channel are tightly coupled and/or parts of the same molecule. 7. In rat and guinea-pig megakaryocytes, ADP-induced rapid inward currents showed the same properties as in mouse megakaryocytes.[Abstract] [Full Text] [Related] [New Search]