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黏液虫巨大轴突中的氨基酸转运:氨基酸库的稳定性、牛磺酸外流及钠的转位效应

Amino acid transport in Myxicola giant axon: stability of the amino acid pool, taurine efflux, and trans effect of sodium.

作者信息

Horn L W

出版信息

J Physiol. 1981 Aug;317:103-27. doi: 10.1113/jphysiol.1981.sp013816.

Abstract
  1. The giant axon of Myxicola infundibulum was assessed for its suitability as a model preparation for study of amino acid transport mechanisms.2. The amino acid composition of axoplasm was measured and compared with those of coelomic fluid, muscle and axon sheath. The axoplasmic composition is unique. Axoplasm/coelomic fluid concentration ratios are all much larger than 1. The axoplasmic amino acid concentrations are (mmol/kg plasm): cysteic acid (104), aspartic acid (75), glutamic acid (10), taurine (64), serine (5), glycine (191) and alanine (5). Other amino acids or primary amines, if present, must have concentrations of less than 1 mm.3. The size of the sheath amino acid pool is 12% or less of the axoplasmic pool.4. The amino acid pool of axons soaked in sea water for up to 24 h is stable. Removal of Na from sea water causes a large increase of net efflux and net production of amino acids.5. Net amino acid production can not be detected in sheath. Metabolic production occurs in axoplasm with little accumulation. Time scales for production and net efflux are therefore similar.6. The Myxicola axon has a vigorous amino acid metabolism and transport systems capable of relatively large fluxes. Homeostasis is strongly linked to Na and may involve Na-coupled co-transport. Conservation of transmembrane amino acid gradients could be promoted in part by trans inhibition of efflux by external Na.7. Taurine is a useful model substrate because it is not catabolized in Myxicola and its net efflux is sensitive to Na. [(3)H]taurine efflux was measured from injected axons. Fluxes and internally recorded action potentials are stable for up to 6 h.8. Axon sheaths take up [(3)H]taurine from 10 mm-taurine sea water with an apparent half-time of 5 h. [(3)H]taurine washout from the apparent extracellular space has a half-time of 5 min. Washout from sheath cells has a half-time of 2-3 h. Sheath is not an important parallel compartment for taurine fluxes in the axon.9. Taurine efflux has a Q(10) of 1.8.10. Taurine efflux is insensitive to external taurine concentrations up to 10 mm.11. Taurine efflux is sensitive to external Na, but only if internal Na is high.12. Taurine is transported by a low-affinity Na-dependent system in Myxicola axon. Results could be explained by a carrier which is more mobile in the empty state than in the substrate-loaded state. Trans inhibition of taurine efflux by external Na is an important property of the system, and contributes to conservation of axoplasmic taurine.
摘要
  1. 对漏斗黏液虫的巨大轴突进行了评估,以确定其作为研究氨基酸转运机制的模型标本的适用性。

  2. 测定了轴浆的氨基酸组成,并与体腔液、肌肉和轴突鞘的氨基酸组成进行了比较。轴浆组成独特。轴浆/体腔液浓度比均远大于1。轴浆中氨基酸浓度(mmol/kg血浆):半胱磺酸(104)、天冬氨酸(75)、谷氨酸(10)、牛磺酸(64)、丝氨酸(5)、甘氨酸(191)和丙氨酸(5)。其他氨基酸或伯胺(如果存在)的浓度必须小于1 mmol。

  3. 鞘氨基酸库的大小为轴浆库的12%或更少。

  4. 在海水中浸泡长达24小时的轴突的氨基酸库是稳定的。从海水中去除钠会导致氨基酸净流出和净产生大幅增加。

  5. 在鞘中未检测到氨基酸净产生。代谢产生发生在轴浆中,积累很少。因此,产生和净流出的时间尺度相似。

  6. 漏斗黏液虫轴突具有活跃的氨基酸代谢和能够进行相对大量通量的转运系统。稳态与钠密切相关,可能涉及钠偶联共转运。跨膜氨基酸梯度的维持可能部分通过外部钠对流出的反抑制来促进。

  7. 牛磺酸是一种有用的模型底物,因为它在漏斗黏液虫中不被分解代谢,其净流出对钠敏感。从注射的轴突中测量了[³H]牛磺酸流出。通量和内部记录的动作电位在长达6小时内是稳定的。

  8. 轴突鞘从10 mmol/L牛磺酸海水中摄取[³H]牛磺酸,表观半衰期为5小时。从表观细胞外空间洗脱出[³H]牛磺酸的半衰期为5分钟。从鞘细胞中洗脱出[³H]牛磺酸的半衰期为2 - 3小时。鞘不是轴突中牛磺酸通量的重要平行隔室。

  9. 牛磺酸流出的Q₁₀为1.8。

  10. 牛磺酸流出对高达10 mmol/L的外部牛磺酸浓度不敏感。

  11. 牛磺酸流出对外部钠敏感,但仅当内部钠含量高时才敏感。

  12. 牛磺酸在漏斗黏液虫轴突中通过低亲和力的钠依赖性系统转运。结果可以用一种在空状态下比在底物负载状态下更易移动的载体来解释。外部钠对牛磺酸流出的反抑制是该系统的一个重要特性,有助于维持轴浆中的牛磺酸。

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Glycine fluxes in squid giant axons.鱿鱼巨大轴突中的甘氨酸通量。
J Physiol. 1978 May;278:1-25. doi: 10.1113/jphysiol.1978.sp012289.

本文引用的文献

1
The giant axons of annelids.环节动物的巨大轴突。
Q Rev Biol. 1948 Dec;23(4):291-323. doi: 10.1086/396594.
3
Phosphagens of marine animals.海洋动物的磷酸原
Ann N Y Acad Sci. 1960 Nov 17;90:923-8. doi: 10.1111/j.1749-6632.1960.tb26439.x.
7
9
Fluorescence reaction for amino acids.氨基酸的荧光反应。
Anal Chem. 1971 Jun;43(7):880-2. doi: 10.1021/ac60302a020.

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