Investigating the role of the novel LRWD1 protein in testis and spermatozoa

Chia Nan University of Pharmacy & Science Institutional Repository > 藥理學院 > 2008第五屆海峽化學、生物及材料研討會 > Item 310902800/30515

jsp.display-item.identifier=請使用永久網址來引用或連結此文件: https://ir.cnu.edu.tw/handle/310902800/30515

標題:	Investigating the role of the novel LRWD1 protein in testis and spermatozoa 探討新穎蛋白LRWD1在睪丸與精子上所扮演的角色
作者:	Lin(林揚斌), Yang-Ben Kuo(郭保麟), Pao-Lin Teng(鄧燕妮), Yen-Ni
貢獻者:	Department of Biotechnology, Chia-Nan University of Pharmacy and Science Department of Obstetrics & Gynecology, National Cheng Kung University, College of Medicine
日期:	2008-07
上傳時間:	2017-12-04 16:00:11 (UTC+8)
摘要:	Background and Purpose: LRWD1 (Leucine-Rich repeats and WD repeat domain containing 1) is a testis-enriched gene. The human LRWD1 gene contains 15 exons and was mapped to chromosome 7q22.1. The protein was predicted to contain one leucine-rich repeats (LRR) and three WD-40 domains by SMART protein prediction web site (http://smart.embl-heidelberg.de/). The cDNA microarray analyses showed the transcript amount of this gene was significantly decreased in the testicular tissue of men with spermatogenic defect.Methods and Results: In our results, the LRWD1 protein was mainly expressed in postmeiotic germ cells. Immunofluorescence microscopic study of human and mouse spermatozoa showed strong homogeneous staining in the centrosome region (by colocalization with centrin) and less intense signal in the principal piece and tail region. It is assumed that the sperm centriole has an important role in the sperm motility and sperm morphology. Therefore, LRWD1 defects is probably not only correlated with decreased or absent motility of the sperm but might also be associated with sperm morphology.Conclusions: The study will provide valuable information regarding the roles of LRWD1 centrosomal proteins during spermatogenesis.
關聯:	第五屆海峽化學、生物及材料研討會，起迄日：2008/07/21-2008/07/22，地點：嘉南藥理科技大學
显示于类别:	[藥理學院] 2008第五屆海峽化學、生物及材料研討會

文件中的档案:

档案	描述	大小	格式	浏览次数
B13.pdf		337Kb	Adobe PDF	177	检视/开启

在CNU IR中所有的数据项都受到原著作权保护.

TAIR相关文章

数据加载中.....