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真核生物蛋白质糖基化:组织化学家和细胞生物学家入门指南

Eukaryotic protein glycosylation: a primer for histochemists and cell biologists.

作者信息

Corfield Anthony

机构信息

Mucin Research Group, School of Clinical Sciences, Bristol Royal Infirmary, University of Bristol, Bristol, BS2 8HW, UK.

出版信息

Histochem Cell Biol. 2017 Feb;147(2):119-147. doi: 10.1007/s00418-016-1526-4. Epub 2016 Dec 23.

DOI:10.1007/s00418-016-1526-4
PMID:28012131
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5306191/
Abstract

Proteins undergo co- and posttranslational modifications, and their glycosylation is the most frequent and structurally variegated type. Histochemically, the detection of glycan presence has first been performed by stains. The availability of carbohydrate-specific tools (lectins, monoclonal antibodies) has revolutionized glycophenotyping, allowing monitoring of distinct structures. The different types of protein glycosylation in Eukaryotes are described. Following this educational survey, examples where known biological function is related to the glycan structures carried by proteins are given. In particular, mucins and their glycosylation patterns are considered as instructive proof-of-principle case. The tissue and cellular location of glycoprotein biosynthesis and metabolism is reviewed, with attention to new findings in goblet cells. Finally, protein glycosylation in disease is documented, with selected examples, where aberrant glycan expression impacts on normal function to let disease pathology become manifest. The histological applications adopted in these studies are emphasized throughout the text.

摘要

蛋白质会经历共翻译和翻译后修饰,其中糖基化是最常见且结构多样的类型。在组织化学中,聚糖存在的检测最初是通过染色进行的。碳水化合物特异性工具(凝集素、单克隆抗体)的出现彻底改变了糖型分析,使得对不同结构的监测成为可能。本文描述了真核生物中不同类型的蛋白质糖基化。在这一知识综述之后,给出了已知生物学功能与蛋白质所携带的聚糖结构相关的例子。特别是,粘蛋白及其糖基化模式被视为具有指导意义的原理验证案例。本文回顾了糖蛋白生物合成和代谢的组织及细胞定位,并关注了杯状细胞的新发现。最后,记录了疾病中的蛋白质糖基化情况,并列举了一些例子,其中异常的聚糖表达会影响正常功能,从而导致疾病病理表现出来。本文通篇强调了这些研究中采用的组织学应用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/19fefa0d9315/418_2016_1526_Fig10_HTML.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/cc1b2fab84c1/418_2016_1526_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/f5f2c1409c7f/418_2016_1526_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/fe639068025b/418_2016_1526_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/981481237ff6/418_2016_1526_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/8a09673a5f43/418_2016_1526_Fig9_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/19fefa0d9315/418_2016_1526_Fig10_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/23e1abed758c/418_2016_1526_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/676fb552097a/418_2016_1526_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/2192ed832a8c/418_2016_1526_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/d14a8d13b0d4/418_2016_1526_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/cc1b2fab84c1/418_2016_1526_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/f5f2c1409c7f/418_2016_1526_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/fe639068025b/418_2016_1526_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/981481237ff6/418_2016_1526_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/8a09673a5f43/418_2016_1526_Fig9_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af0d/5306191/19fefa0d9315/418_2016_1526_Fig10_HTML.jpg

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Histochem Cell Biol. 2017 Feb;147(2):285-301. doi: 10.1007/s00418-016-1525-5. Epub 2016 Dec 24.
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