Sialoglycoprotein synthesis in developing rat brain.

Neurobiology Pub Date : 1975-08-01
D H van den Eijnden, W van Dijk, P A Roukema
{"title":"Sialoglycoprotein synthesis in developing rat brain.","authors":"D H van den Eijnden,&nbsp;W van Dijk,&nbsp;P A Roukema","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The postnatal developmental profiles of the protein-bound sialic acid content and the activities of CMP-N-acetylneuraminic acid (CMP-AcNeu) synthetase (EC 2.7.7.43) and glycoprotein sialyltransferase, enzymes involved in sialoglycoprotein biosynthesis, were estimated in the rat brain. The sialoglycoprotein level appeared to increase 2-fold from birth to about 20 days of age, which correlates with the outgrowth of the cell processes in this period. In contrast, the activities per g wet tissue of the enzymes were highest at birth and showed decreasing tendencies during maturation. This revealed that, at least at a certain stage during development, the sialyltransferase is present in structures other than synaptic membranes, since the new-born rat brain is devoid of these membranes. The developmental profile of the endogenous, sialic acid accepting molecules was very similar to that of the sialoglycoproteins. It was concluded that cerebral sialoglycoprotein biosynthesis during postnatal development is not limited by the activities of the synthetase and the transferase, but may largely depend on the production of the endogenous acceptors, which are presumed to be the natural precursors for the sialoglycoproteins.</p>","PeriodicalId":19126,"journal":{"name":"Neurobiology","volume":"5 4","pages":"221-7"},"PeriodicalIF":0.0000,"publicationDate":"1975-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Neurobiology","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

The postnatal developmental profiles of the protein-bound sialic acid content and the activities of CMP-N-acetylneuraminic acid (CMP-AcNeu) synthetase (EC 2.7.7.43) and glycoprotein sialyltransferase, enzymes involved in sialoglycoprotein biosynthesis, were estimated in the rat brain. The sialoglycoprotein level appeared to increase 2-fold from birth to about 20 days of age, which correlates with the outgrowth of the cell processes in this period. In contrast, the activities per g wet tissue of the enzymes were highest at birth and showed decreasing tendencies during maturation. This revealed that, at least at a certain stage during development, the sialyltransferase is present in structures other than synaptic membranes, since the new-born rat brain is devoid of these membranes. The developmental profile of the endogenous, sialic acid accepting molecules was very similar to that of the sialoglycoproteins. It was concluded that cerebral sialoglycoprotein biosynthesis during postnatal development is not limited by the activities of the synthetase and the transferase, but may largely depend on the production of the endogenous acceptors, which are presumed to be the natural precursors for the sialoglycoproteins.

发育中的大鼠脑唾液糖蛋白合成。
测定了大鼠脑中蛋白结合的唾液酸含量、cmp - n-乙酰神经氨酸(CMP-AcNeu)合成酶(EC 2.7.7.43)和参与唾液糖蛋白生物合成的糖蛋白唾液基转移酶的活性。从出生到大约20日龄,唾液糖蛋白水平增加了2倍,这与这一时期细胞过程的生长有关。每g湿组织酶活性在初生时最高,成熟后呈下降趋势。这表明,至少在发育的某个阶段,唾液基转移酶存在于突触膜以外的结构中,因为新生的大鼠大脑缺乏这些膜。内源性唾液酸接受分子的发育过程与唾液糖蛋白非常相似。由此可见,出生后大脑唾液糖蛋白的合成不受合成酶和转移酶活性的限制,而很大程度上取决于内源性受体的产生,这些受体被认为是唾液糖蛋白的天然前体。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信