Home  |  Archive  |  Online Submission  |  News & Events  |  Subscribe  |  APFA  |  Society  |  Links  |  Contact Us  |  中文版

Ahead of print
Authors' Accepted
Current Issue
Special Issues
Browse by Category

Manuscript Submission

Online Submission
Online Review
Instruction for Authors
Instruction for Reviewers
English Corner new!

About AJA

About AJA
Editorial Board
Contact Us

Resources & Services

Email alert

Download area

Copyright licence
EndNote style file
Manuscript word template
Guidance for AJA figures
    preparation (in English)

Guidance for AJA figures
    preparation (in Chinese)

Proof-reading for the

AJA Club (in English)
AJA Club (in Chinese)


Societies & Institutes
Databases & Libraries
Other links


Volume 9, Issue 4 (July 2007) 9, 500–507; 10.1111/j.1745-7262.2007.00309.x

Extracellular quality control in the epididymis

Gail A Cornwall, H Henning von Horsten, Douglas Swartz, Seethal Johnson, Kim Chau and Sandra Whelly

Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA

Correspondence: Dr Gail A. Cornwall, Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, 3601 4th Street, Lubbock, TX 79430, USA. Fax: +1-806-743-2990. E-mail: gail.cornwall@ttuhsc.edu


The epididymal lumen represents a unique extracellular environment because of the active sperm maturation process that takes place within its confines. Although much focus has been placed on the interaction of epididymal secretory proteins with spermatozoa in the lumen, very little is known regarding how the complex epididymal milieu as a whole is maintained, including mechanisms to prevent or control proteins that may not stay in their native folded state following secretion. Because some misfolded proteins can form cytotoxic aggregate structures known as amyloid, it is likely that control/surveillance mechanisms exist within the epididymis to protect against this process and allow sperm maturation to occur. To study protein aggregation and to identify extracellular quality control mechanisms in the epididymis, we used the cystatin family of cysteine protease inhibitors, including cystatin-related epididymal spermatogenic and cystatin C as molecular models because both proteins have inherent properties to aggregate and form amyloid. In this chapter, we present a brief summary of protein aggregation by the amyloid pathway based on what is known from other organ systems and describe quality control mechanisms that exist intracellularly to control protein misfolding and aggregation. We then present a summary of our studies of cystatin-related epididymal spermatogenic (CRES) oligomerization within the epididymal lumen, including studies suggesting that transglutaminase cross-linking may be one mechanism of extracellular quality control within the epididymis.

Keywords: epididymis, protein aggregation, extracellular quality control, cystatin, transglutaminase

Full Text | PDF | 中文摘要 |

Browse:  1727
Copyright 1999-2017  Shanghai Materia Medica, Shanghai Jiao Tong University.  All rights reserved