|
|
||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Section of Molecular and Cellular Biology,4
Department of Cell Biology and Human Anatomy, School of Medicine,5 University of California, Davis, Davis, California 95616
Adam2-null and Adam3-null male mice exhibit reduced levels of one or more ADAM proteins on mature sperm, in addition to the loss of the genetically targeted protein. ADAM protein loss was believed to occur posttranslationally, although the timing of loss and the mechanism by which the loss occurred were not explored. In this study we have found that in Adam3-null mice, fertilin beta (also known as ADAM2) is lost during the formation of testicular sperm. In Adam2-null males, most cyritestin (ADAM3) protein is also lost at this stage, but 25% of cyritestin is lost later, during sperm passage through the epididymis. Although normal levels of cyritestin are synthesized and acquire Endoglycosidase H resistance, indicating transit through the Golgi, the protein does not reach the cell surface. We also discovered that the majority of both fertilin beta and cyritestin are found in a Triton X-100 insoluble compartment on testicular sperm, when most of the cyritestin was observed on the cell surface. This insoluble compartment may represent a sorting platform, because in Adam2-knockout cells, only a small fraction of the cyritestin becomes Triton X-100 insoluble. Thus, it appears that cyritestin loss in Adam2-knockout mice may result, at least in part, from a disruption in protein trafficking.
fertilization, gamete biology, sperm, spermatogenesis, testis
2 Correspondence. Fax: 530 752 7522; dgmyles{at}ucdavis.edu
3 Current address: Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892
This article has been cited by other articles:
![]() |
C. Han, E. Choi, I. Park, B. Lee, S. Jin, D. H. Kim, H. Nishimura, and C. Cho Comprehensive Analysis of Reproductive ADAMs: Relationship of ADAM4 and ADAM6 with an ADAM Complex Required for Fertilization in Mice Biol Reprod, May 1, 2009; 80(5): 1001 - 1008. [Abstract] [Full Text] [PDF] |
||||
![]() |
H. Nishimura, D. G. Myles, and P. Primakoff Identification of an ADAM2-ADAM3 Complex on the Surface of Mouse Testicular Germ Cells and Cauda Epididymal Sperm J. Biol. Chem., June 15, 2007; 282(24): 17900 - 17907. [Abstract] [Full Text] [PDF] |
||||
![]() |
R. Yamaguchi, K. Yamagata, M. Ikawa, S. B. Moss, and M. Okabe Aberrant Distribution of ADAM3 in Sperm from Both Angiotensin-Converting Enzyme (Ace)- and Calmegin (Clgn)-Deficient Mice Biol Reprod, November 1, 2006; 75(5): 760 - 766. [Abstract] [Full Text] [PDF] |
||||
![]() |
T. Kim, J. Oh, J.-M. Woo, E. Choi, S. H. Im, Y. J. Yoo, D. H. Kim, H. Nishimura, and C. Cho Expression and Relationship of Male Reproductive ADAMs in Mouse Biol Reprod, April 1, 2006; 74(4): 744 - 750. [Abstract] [Full Text] [PDF] |
||||
![]() |
E. Kim, M. Yamashita, T. Nakanishi, K.-E. Park, M. Kimura, S.-i. Kashiwabara, and T. Baba Mouse Sperm Lacking ADAM1b/ADAM2 Fertilin Can Fuse with the Egg Plasma Membrane and Effect Fertilization J. Biol. Chem., March 3, 2006; 281(9): 5634 - 5639. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |