Enhancement of mouse sperm motility by trophinin-binding peptide

Reproductive Biology and Endocrinology

Research

Daita Nadano¹  Kazuhiro Sugihara²  Mun Seog Chang³  Seung Ho Lee⁴  Khatereh Motamedchaboki⁴  Ling Wang⁴  Michiko N Fukuda⁴  Toshiaki K Shibata⁵  Naoaki Tamura⁵  Seong Kyu Park⁶  Jiwon Yoon⁶  Kyung Jun Shim⁶  Shingo Hatakeyama⁷ 

[1] Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, 464-8601, Chikusa, Nagoya, Japan;Department of Gynecology and Obstetrics, Hamamatsu University School of Medicine, 431-3192, Hamamatsu City, Shizuoka, Japan;Department of Prescriptionology, College of Oriental Medicine, Kyung Hee University, 130-701, Seoul, Republic of Korea;Tumor Microenvironment Program, Cancer Center, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Rd, CA 92037, La Jolla, USA;Tumor Microenvironment Program, Cancer Center, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Rd, CA 92037, La Jolla, USA;Department of Gynecology and Obstetrics, Hamamatsu University School of Medicine, 431-3192, Hamamatsu City, Shizuoka, Japan;Tumor Microenvironment Program, Cancer Center, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Rd, CA 92037, La Jolla, USA;Department of Prescriptionology, College of Oriental Medicine, Kyung Hee University, 130-701, Seoul, Republic of Korea;Tumor Microenvironment Program, Cancer Center, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Rd, CA 92037, La Jolla, USA;Department of Urology, Hirosaki University School of Medicine, 036-8562, Hirosaki, Aomori, Japan;

关键词: Microtubule;    Flagella;    Dynein;    ATP;    Mutant;    Gene knockout;   

DOI  :  10.1186/1477-7827-10-101

 received in 2012-10-09, accepted in 2012-11-27,  发布年份 2012

来源: Springer

【 摘 要 】

BackgroundTrophinin is an intrinsic membrane protein that forms a complex in the cytoplasm with bystin and tastin, linking it microtubule-associated motor dynein (ATPase) in some cell types. Previously, we found that human sperm tails contain trophinin, bystin and tastin proteins, and that trophinin-binding GWRQ (glycine, tryptophan, arginine, glutamine) peptide enhanced motility of human sperm.MethodsImmunohistochemistry was employed to determine trophinin protein in mouse spermatozoa from wild type mouse, by using spermatozoa from trophinin null mutant mice as a negative control. Multivalent 8-branched GWRQ (glycine, tryptophan, arginine, glutamine) peptide or GWRQ-MAPS, was chemically synthesized, purified by HPLC and its structure was confirmed by MALDI-TOF mass spectrometry. Effect of GWRQ-MAPS on mouse spermatozoa from wild type and trophinin null mutant was assessed by a computer-assisted semen analyzer (CASA).ResultsAnti-trophinin antibody stained the principal (central) piece of the tail of wild type mouse sperm, whereas the antibody showed no staining on trophinin null sperm. Phage particles displaying GWRQ bound to the principal piece of sperm tail from wild type but not trophinin null mice. GWRQ-MAPS enhanced motility of spermatozoa from wild type but not trophinin null mice. CASA showed that GWRQ-MAPS enhanced both progressive motility and rapid motility in wild type mouse sperm.ConclusionsPresent study established the expression of trophinin in the mouse sperm tail and trophinin-dependent effect of GWRQ-MAPS on sperm motility. GWRQ causes a significant increase in sperm motility.

【 授权许可】

Unknown   
© Park et al.; licensee BioMed Central Ltd. 2012. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.