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蛋白激酶C同工酶的组织分布与发育表达

Tissue distribution and developmental expression of protein kinase C isozymes.

作者信息

Yoshida Y, Huang F L, Nakabayashi H, Huang K P

机构信息

Section on Metabolic Regulation, National Institute of Child Health and Human Development, Bethesda, Maryland 20892.

出版信息

J Biol Chem. 1988 Jul 15;263(20):9868-73.

PMID:3133370
Abstract

Protein kinase C is a ubiquitous enzyme found in a variety of mammalian tissues and is especially highly enriched in brain and lymphoid organs. Based on biochemical and immunological analyses, we have identified three types of protein kinase C isozyme (designated types I-III) from rat brain. Monospecific antibodies against each of the protein kinase C isozymes were prepared for the determination of tissue distribution, subcellular localization, and developmental changes of these enzymes. The various protein kinase C isozymes were found to be distinctively distributed in different tissues: the type I enzyme in brain; the type II enzyme in brain, pituitary and pineal glands, spleen, thymus, retina, lung, and intestine; and the type III enzyme in brain, pineal gland, retina, and spleen. The rat brain enzymes were differentially distributed in different subcellular fractions. The type I enzyme appeared to be most lipophilic and was recovered mostly in the particulate fractions (80-90%) regardless of the EGTA- or Ca2+-containing buffer used in the homogenization. Significant amounts (30-40%) of the type II and III enzymes were recovered in the cytosolic fraction with EGTA-containing buffer. The expressions of different protein kinase C isozymes appear to be differently controlled during development. In rat brain, both type II and III enzymes were found to increase progressively from 3 days before birth up to 2-3 weeks of age and remained constant thereafter. However, the expression of the type I enzyme displayed a different developmental pattern; it was very low within 1 week, and an abrupt increase was observed between 2 and 3 weeks of age. In thymus, the type II enzyme was found to be maximal shortly after birth; whereas the same kinase in spleen was very low within 2 weeks of age, and a significant increase was observed between 2 and 3 weeks. These results demonstrate that protein kinase C isozymes are distinctively distributed in different tissues and subcellular locales and that their expressions are controlled differently during development.

摘要

蛋白激酶C是一种普遍存在于多种哺乳动物组织中的酶,在脑和淋巴器官中尤其高度富集。基于生化和免疫分析,我们从大鼠脑中鉴定出了三种蛋白激酶C同工酶类型(命名为I - III型)。针对每种蛋白激酶C同工酶制备了单特异性抗体,用于测定这些酶的组织分布、亚细胞定位和发育变化。发现各种蛋白激酶C同工酶在不同组织中有独特的分布:I型酶存在于脑中;II型酶存在于脑、垂体、松果体、脾脏、胸腺、视网膜、肺和肠道中;III型酶存在于脑、松果体、视网膜和脾脏中。大鼠脑酶在不同亚细胞组分中的分布也存在差异。I型酶似乎最具亲脂性,无论在匀浆中使用含EGTA还是Ca2+的缓冲液,它大多在颗粒组分中回收(80 - 90%)。使用含EGTA的缓冲液时,II型和III型酶有相当数量(30 - 40%)在胞质组分中回收。不同蛋白激酶C同工酶的表达在发育过程中似乎受到不同的调控。在大鼠脑中,II型和III型酶在出生前3天到出生后2 - 3周逐渐增加,此后保持恒定。然而,I型酶的表达呈现出不同的发育模式;在1周内非常低,在2 - 3周龄之间观察到突然增加。在胸腺中,II型酶在出生后不久达到最大值;而在脾脏中,同一激酶在2周龄内非常低,在2 - 3周龄之间观察到显著增加。这些结果表明,蛋白激酶C同工酶在不同组织和亚细胞位置有独特的分布,并且它们的表达在发育过程中受到不同的控制。

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