Role of Posttranslational Protein Modifications in Epididymal Sperm Maturation and Extracellular Quality Control

被引:50
作者
Cornwall, Gail A. [1 ]
机构
[1] Texas Tech Univ, Hlth Sci Ctr, Lubbock, TX 79430 USA
来源
POSTTRANSLATIONAL PROTEIN MODIFICATIONS IN THE REPRODUCTIVE SYSTEM | 2014年 / 759卷
关键词
Epididymis; Luminal fluid; Spermatozoa; Aggregation; Amyloid; Transglutaminase; Phosphorylation; Glycosylation; Ubiquitination; ANGIOTENSIN-CONVERTING ENZYME; GLYCOGEN-SYNTHASE KINASE-3; MALE REPRODUCTIVE-TRACT; MONKEYS MACACA-MULATTA; PLASMA-MEMBRANE; TYROSINE PHOSPHORYLATION; IN-VITRO; SERINE-PROTEASE; MAMMALIAN EPIDIDYMIS; MOUSE SPERMATOZOA;
D O I
10.1007/978-1-4939-0817-2_8
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
The epididymal lumen is a complex microenvironment in which spermatozoa acquire motility and fertility. Spermatozoa are synthetically inactive and therefore the maturation process requires their interaction with proteins that are synthesized and secreted in a highly regionalized manner by the epididymal epithelium. In addition to the integration of epididymal secretory proteins, posttranslational modifications of existing sperm proteins are important for sperm maturation and acquisition of fertilizing potential. Phosphorylation, glycosylation, and processing are several of the posttranslational modifications that sperm proteins undergo during epididymal transit resulting in changes in protein function and localization ultimately leading to mature spermatozoa. In addition to these well-characterized modifications, protein aggregation and cross-linking also occur within the epididymal lumen and may represent unique mechanisms for controlling protein function including that for maturation as well as for extracellular quality control.
引用
收藏
页码:159 / 180
页数:22
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