M. Bunemann et L. Pott, MEMBRANE-DELIMITED ACTIVATION OF MUSCARINIC-K CURRENT BY AN ALBUMIN-ASSOCIATED FACTOR IN GUINEA-PIG ATRIAL MYOCYTES, Pflugers Archiv, 425(3-4), 1993, pp. 329-334
Atrial myocytes obtained by enzymatic perfusion of hearts from adult g
uinea-pigs and cultured for 0-14 days were studied using different con
figurations of the patch-clamp technique. Activation of muscarinic K c
urrent [I-K(ACh)] in whole-cell voltage-clamp mode by strongly diluted
sera from various sources could be mimicked by corresponding concentr
ations of albumin, but not by delipidated (''fatty-acid-free'') sample
s of albumin. In cell-attached membrane patches activity of I-K(ACh) c
hannels was significantly higher than basal I-K(ACh) channel activity,
if the pipette contained serum, whereas application of serum-containi
ng solution to the cell outside the patch did not affect channel activ
ity. In isolated inside-out membrane patches, strong I-K(ACh) activati
on by internal guanosine triphosphate (GTP, 5 mu M) was observed if th
e pipette contained serum. If no activator was presented to the outer
face of the membrane, only weak opening activity was observed during b
ath application of GTP. These results demonstrate that the serrum fact
or which causes activation of I-K(ACh) is associated with albumin. Fur
thermore activation of I-K(ACh) by that factor proceeds analogous to A
Ch or adenosine, i. e. via a membrane-delimited receptor, G-protein, c
hannel interaction.