Expression of a plasma membrane proteolipid during differentiation of neuronal and glial cells in primary culture.
Expression of a plasma membrane proteolipid during differentiation of neuronal and glial cells in primary culture.
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原代培养物中神经元和神经胶质细胞分化过程中质膜蛋白脂质的表达。
DOI：
10.1111/j.1471-4159.1986.tb00668.x
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发表时间：
1986
影响因子：
4.7
通讯作者：
Sapirstein,V
中科院分区：
文献类型：
--
作者：
Shea,TB;Fischer,I;Sapirstein,V
在胚胎大鼠神经元和新生大鼠神经胶质细胞分化过程中，质膜蛋白脂质蛋白（PMPLP）的合成进行了研究。神经胶质细胞培养物用1 mM N6，O2，二丁酰环磷酸腺苷（dbcAMP）汇合后诱导分化，这导致了长细胞过程的阐述。然而，在这些细胞的分化过程中没有观察到PMPLP的生物合成水平的变化。神经元在培养物中自发分化，在铺板后立即形成细胞聚集体，并在7天内形成神经突网络。神经元的分化伴随着PM-PLP合成的7倍增加，在培养的第1天和第3天之间以及第3天和第7天之间观察到生物合成速率增加。神经元的超微结构检查表明，高尔基体也在这段时间内发展，在两个lamelles和代囊泡的数量增加。因此，在培养的第7天，通过莫能菌素和秋水仙碱的脉冲标记实验，在神经元中检查PM-PLP向质膜的转运。发现莫能菌素（1 μM）可抑制质膜中放射性标记的PM-PLP的出现达63%，表明PM-PLP转运至靶膜需要功能性高尔基体。秋水仙素（125 μM）也抑制质膜中新合成的PM-PLP的出现，抑制率> 40%，表明PM-PLP转运到质膜可能也需要微管。
Plasma membrane proteolipid protein (PMPLP) synthesis was examined in embryonic rat neurons and neonatal rat glial cells during differentiation in culture. Glial cultures were treated with 1 mM N6,O2, dibutyryl cyclic adenosine monophosphate (dbcAMP) following confluency to induce differentiation, which resulted in the elaboration of long cellular processes. However, no changes in the biosynthetic level of PMPLP was observed during the differentiation of these cells. Neurons differentiated spontaneously in culture, forming cellular aggregates immediately following plating and elaborating a network of neurites over 7 days. The differentiation of neurons was accompanied by a sevenfold increase in PM‐PLP synthesis with increases in biosynthetic rate observed betvyeen days 1 and 3 and between days 3 and 7 in culture. Ultrastructural examination of neurons indicated that the Golgi apparatus was also developing during this period of time, with an increase in both the number of lamellae and generation of vesicles. The transport of PM‐PLP to the plasma membrane was therefore examined in neurons at day 7 in culture by pulse labeling experiments with monensin and colchicine. Monensin (1 μM) was found to inhibit the appearance of radiolabeled PM‐PLP in the plasma membrane by 63%, indicating that a functional Golgi apparatus is required for transport of PM‐PLP to its target membrane. Colchicine (125 μM) also inhibited the appearance of newly synthesized PM‐PLP in the plasma membrane by >40%, suggesting that microtubules may also be required for PM‐PLP transport to the plasma membrane.