Neurotrophic control of 16S acetylcholinesterase from mammalian skeletal muscle in organ culture

Wiley - Tập 11 Số 6 - Trang 557-570 - 1980
Hugo L. Fernández1,2, Michael R. Patterson1, Myron J. Duell1
1Medical Research Service, Veterans Administration Medical Center, Kansas City, Missouri 64128, and Department of Physiology, University of Kansas Medical Center, Kansas City, Kansas 66103
2Neurosciences Research Laboratory, Veterans Administration Medical Center, 4801 Linwood Boulevard, Kansas City, Missouri 64128

Tóm tắt

AbstractThe effects of rat obturator nerve extracts on total and 16S acetylcholinesterase (AChE) activity were studied in endplate regions of denervated anterior gracilis muscles maintained in organ culture for 48 hr. The decrease of total AChE activity in cultured muscles was similar to that observed in denervated muscles in vivo. This decrease in activity was partly prevented by addition of either 100 or 200 μl nerve extract (2.7 mg/ml protein) to the nutrient medium. Nerve extract treatment also decreased the release of AChE activity from the muscle into the bathing medium. Conversely, rat serum (20 μl; 90 mg/ml protein) had no effect on total AChE activity in muscle endplates, nor on release of the enzyme by the muscle. The 16S form of AChE was confined to motor endplate muscle regions and its activity was drastically decreased by denervation in both organ culture and in vivo preparations in a comparable manner. Nerve‐extract supplemented cultures contained a significantly (p ≪ 0.001) larger amount of endplate 16S AChE activity (140–145%) than the corresponding controls (100‐). Our results suggest that some nerve soluble substance, other than serum contaminants or 16S AChE itself, affects the maintenance of 16S AChE at the neuromuscular junction.

Từ khóa


Tài liệu tham khảo

10.1016/0003-2697(76)90143-3

10.1016/0014-5793(76)80668-0

10.1042/bj0540695

Belmar J., 1966, Pacemaker site of fibrillation potentials in denervated mammalian muscle, J. Neurophysiol., 29, 425, 10.1152/jn.1966.29.3.425

10.1016/0014-4886(78)90210-8

10.1113/jphysiol.1979.sp012749

10.1111/j.1471-4159.1980.tb07872.x

10.1002/neu.480100503

10.1111/j.1471-4159.1979.tb00387.x

10.1002/neu.480110105

10.1038/262055a0

10.1002/neu.480040404

10.1038/newbio232062a0

10.1038/280504a0

10.1111/j.1471-4159.1977.tb10654.x

Jarcho L. W., 1952, Spread of excitation in skeletal muscle: Some factors contributing to the form of the electromyogram, Am. J. Physiol., 168, 446, 10.1152/ajplegacy.1952.168.2.446

10.1016/0003-2697(75)90423-6

10.1038/271075a0

10.1126/science.171.3967.187

10.1083/jcb.55.1.93

10.1038/newbio238154a0

10.1111/j.1749-6632.1974.tb20521.x

10.1016/0306-4522(79)90129-5

Lmo T. andSlater C. R.(1976). Control of neuromuscular synapse formation. In:Synaptogenesis L. Tauc Ed. Naturalia and Biologia Jouy en Josas 9–30.

10.1021/bi00652a012

10.1016/0003-2697(78)90586-9

Martin R. G., 1961, A method for determining sedimentation behavior of enzymes: Application to protein mixtures, J. Biol. Chem., 236, 1372, 10.1016/S0021-9258(18)64180-8

10.1016/0014-4886(76)90012-1

10.1126/science.178.4067.1298

10.1126/science.635593

Silver A., 1974, The Biology of Cholinesterses, 449

10.1038/275224a0

10.1016/0014-4827(59)90201-0

10.1111/j.1471-4159.1976.tb02614.x

10.1038/256215a0

10.1016/0012-1606(79)90233-1

10.1126/science.78522