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Cyclic GMP-activated channels of the chick pineal gland: Effects of divalent cations, pH, and cyclic AMP (1993)

Dryer, S. E. ; Henderson, D.

Springer

Journal of comparative physiology 172 (1993), S. 271-279

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ISSN: 1432-1351

Keywords: Cyclic GMP ; Cyclic AMP ; Pineal ; Circadian oscillator ; Phototransduction

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: Abstract Chick pineal cells maintained in dissociated cell culture express an intrinsic photosensitive circadian oscillator, but the mechanisms of phototransduction in avian pinealocytes are not fully understood. In this study, we have used inside-out patches to examine the characteristics of cyclic GMP-activated channels of chick pinealocytes in more detail, concentrating on the effects of factors known to modulate the secretion of melatonin and/or the function of circadian pacemakers. In most patches, the predominant conductance state was 19 pS in symmetrical 145 mM NaCl. But in some patches, a second cyclic GMP-activated channel with a unitary conductance of 29 pS was also present. The current flowing through cyclic GMP-activated channels was not affected by application of salines containing 1 μM Ca2+ to the cytoplasmic face of the patch membrane. By contrast, application of 1 mM Ca2+ caused a partial reduction in cyclic GMP-activated current at all membrane potentials. Application of 1–5 mM Mg2+ ions caused a virtually complete blockade of current at positive membrane potentials, but caused only a small decrease in current at negative membrane potentials. No obvious differences in the gating of cyclic GMP-activated channels were observed in pH 8.2, 7.4 or 6.2 salines. Application of salines containing 100 μM, 500 μM, or 1 mM cyclic AMP did not cause activation of the channels, but 5 mM cyclic AMP evoked a low level of channel activity. Application of 5 mM but not 100 μM cyclic AMP decreased the probability of channel activation caused by 20–100 μM cyclic GMP and also increased the percentage of openings to an 11 pS subconductance state. Thus, cyclic AMP acts as a weak partial agonist. Nevertheless, the gating of these channels does not seem to be controlled directly by physiologically relevant changes in intracellular Ca2+, pH, or cyclic AMP.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00216609

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A comparison of shortening and Z line degradation in post-mortem bovine, porcine, and rabbit muscleJournal Paper J-6254 of the Iowa Agriculture and Home Economics Experiment Station, Ames, Iowa, Project 1549. Supported in part by Public Health Servie Research grant GM 12488. (1970)

Henderson, D. W. ; Goll, Darrel E. ; Stromer, M. H.

New York, NY [u.a.] : Wiley-Blackwell

American Journal of Anatomy 128 (1970), S. 117-135

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ISSN: 0002-9106

Keywords: Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Medicine

Notes: Ultrastructural changes in bovine, porcine, and rabbit muscle have been studied during the first 24 hours post-mortem. Samples were taken for phase and electron microscopy immediately after death, after 4, 8, and 24 hours of post-mortem storage at 2° and 37°C, and after 24 hours post-mortem at 16° and 25°C. The results show that two kinds of structural changes occur in muscle during the first 24 hours post-mortem: (a) a variable amount of shortening, this shortening occurring via a sliding of filaments in all species and at all post-mortem storage temperatures examined, and (b) degradation of the Z line, and at higher storage temperatures, of the M line also. Shortening of unrestrained muscle occurs soonest post-mortem at 37°C in all three species and is completed within four hours post-mortem in porcine and rabbit muscle and within eight hours post-mortem in bovine muscle. Post-mortem short-ening of unrestrained rabbit and porcine muscle is greatest at 37°C (sarcomere lengths of 1.5 μ); shortening of rabbit muscle is minimal at 2°C (sarcomere lenght of 1.7 μ), but shortening of porcine muscle is minimal at 25°C (sarcomere length of 1.8 μ) and is slightly greater at 2°C (sarcomere length of 1.6 μ) than at 16°C. Post-mortem shortening of bovine muscle is greatest at 2°C (sarcomere length of 1.3 μ), is minimal at 16-25°C (sarcomere length of 1.8 μ), and increases between 25-37°C (sarcomere length of 1.5 μ at 37°C). Sarcomere length measurements show that some variation occurs in the extent of post-mortem shortening within the same muscle.Z line degradation occurs sooner post-mortem and to a greater extent at storage temperatures of 25°C or above than at temperatures of 16°C or below. Also, bovine muscle Z lines are clearly more resistant to post-mortem degradation than porcine or rabbit muscle Z lines. Loss of fibrillar structure in porcine or rabbit muscle Z lines occurs during the first four hours post-mortem at 37°C, but eight hours of post-mortem storage at 37°C are required to cause loss of fibrillar structure of bovine muscle Z lines. After 24 hours at 25 or 37°C, Z lines of rabbit and porcine muscle are usually completely absent; M lines are also frequently absent in this muscle.

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