scholarly journals Spontaneous electrical activity and associated changes in calcium concentration in guinea‐pig gastric smooth muscle

2002 ◽  
Vol 540 (1) ◽  
pp. 249-260 ◽  
Author(s):  
Hiroyasu Fukuta ◽  
Yoshihiko Kito ◽  
Hikaru Suzuki
Keyword(s):  
Smooth Muscle ◽  
Guinea Pig ◽  
Electrical Activity ◽  
Calcium Concentration ◽  
Spontaneous Electrical Activity ◽  
Gastric Smooth Muscle

Long-term observations of spontaneous electrical activity of the uterine smooth muscle

1959 ◽  
Vol 196 (2) ◽  
pp. 343-350 ◽  
Author(s):  
C. Y. Kao
Keyword(s):  
Smooth Muscle ◽  
Electrical Activity ◽  
Action Potentials ◽  
Local Conditions ◽  
Pregnant Uterus ◽  
Implanted Electrodes ◽  
Spontaneous Electrical Activity ◽  
Myometrial Cells ◽  
Uterine Smooth Muscle

The spontaneous electrical activity of uterine smooth muscle was rather variable when acute observations were made. Therefore, a series of chronic experiments was performed with implanted electrodes to monitor a group of myometrial cells under different physiological conditions for periods up to eight weeks. The results showed that consistent behavior of myometrial cells could be observed provided similar hormonal status was maintained. Action potentials were rare or absent in myometrium of oophorectomized animals but were caused to appear by estrogen. In the pregnant uterus, action potentials increased both in amplitude and frequency of discharge as parturition approached, reached a peak at that time, and then declined in the postpartum days. The results indicated that in estrogen treatment and in parturition activities of myometrial cells were more synchronous. There was suggestive evidence that there were central impulses initiating activity in the pregnant uterus, and that the responses of the myometrium were affected by the local conditions.

Modulation of Spontaneous Electrical Activity in Urethral Smooth Muscle

2003 ◽  
Vol 35 (3/4) ◽  
pp. 217-223
Author(s):  
N. G. McHale ◽  
K. D. Thornbury ◽  
M. A. Hollywood ◽  
G. P. Sergeant
Keyword(s):  
Smooth Muscle ◽  
Electrical Activity ◽  
Spontaneous Electrical Activity ◽  
Urethral Smooth Muscle

Smooth muscle cells from guinea pig stomach possess high-affinity galanin receptors that mediate relaxation

1994 ◽  
Vol 266 (5) ◽  
pp. G839-G845 ◽  
Author(s):  
Z. F. Gu ◽  
T. K. Pradhan ◽  
D. H. Coy ◽  
R. T. Jensen
Keyword(s):  
Smooth Muscle ◽  
Guinea Pig ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Maximal Effect ◽  
Dependent Manner ◽  
High Affinity ◽  
Gastric Smooth Muscle ◽  
Guinea Pig Stomach ◽  
Galanin Receptors

Galanin-like immunoactivity occurs in nerves and plexi in muscle layers throughout gastrointestinal tract including the stomach. Galanin can affect gastric emptying and contraction or relaxation of gastric muscle in different species. The aim of this study was to investigate the direct effect of galanin on dispersed gastric smooth muscle cells and to characterize any galanin receptors that mediated any effect. Dispersed gastric smooth muscle cells were prepared from guinea pig stomach by collagenase digestion. Porcine galanin (p-galanin; 1 microM) did not stimulate contraction when present alone; however, p-galanin (1 microM) inhibited carbachol-induced contraction with a half-maximal effect at 7 nM. p-Galanin (1 microM) increased cellular adenosine 3',5'-cyclic monophosphate (cAMP) content by 10 s and caused a maximal increase of 80% over basal. 125I-galanin (porcine) bound to dispersed cells in a time- and temperature-dependent manner. Binding was saturable, reversible, and specific. Binding of 125I-galanin was inhibited almost equally by porcine and rat galanin (Ki = 6-8 nM) but was not inhibited by the galanin-associated peptide [preprogalanin-(108-123)]. The fragment galanin-(1-16) was equally potent to rat galanin; however, the fragment galanin-(9-29) was 56-fold less potent (Ki = 370 nM). Computer analysis demonstrated there were two binding sites for p-galanin on gastric smooth muscle cells, a high-affinity site (Kd = 2.6 nM) with low capacity (Bmax = 175 fmol/mg protein) and a low-affinity site (Kd = 150 nM) with large capacity (Bmax = 3,611 fmol/mg protein).(ABSTRACT TRUNCATED AT 250 WORDS)

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