Reproduction  
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS  

Reproduction (2006) 132 493-500
DOI: 10.1530/rep.1.01183
Copyright © 2006 Society for Reproduction and Fertility
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Li, S.-H.
Right arrow Articles by Chang, W.-C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Li, S.-H.
Right arrow Articles by Chang, W.-C.

RESEARCH

SSLP-1, a secreted Ly-6 protein purified from mouse seminal vesicle fluid

Sheng-Hsiang Li1,2, Robert Kuo-Kuang Lee1,3, Ming-Huei Lin3, Yuh-Ming Hwu2,3, Chung-Hao Lu1, Ying-Jie Chen1, Hsuan-Chiang Chen1, Wen-Hwei Chang4 and Wei-Chao Chang5

1 Department of Medical Research, Mackay Memorial Hospital, Tamshui 251, Taiwan, ROC, 2 Mackay Medicine, Nursing and Management College, Taipei 112, Taiwan, ROC, 3 Department of Obstetrics and Gynecology, Mackay Memorial Hospital, Taipei 104, Taiwan, ROC, 4 Digitalgene Biosciences Co., Ltd., Taipei 114, Taiwan, ROC, and 5 Genomics Research Center, Academia Sinica, Taipei 115, Taiwan, ROC

Correspondence should be addressed to S-H Li; Email: lsh{at}ms1.mmh.org.tw

The Ly-6 protein family refers to a group of glycophosphatidyl inositol-anchored membrane proteins with ten conserved cysteines. They are thought to be involved in cellular adhesion and signaling. Recently, a subfamily of secreted Ly-6 proteins has been identified. In the present study, we report a secreted Ly-6 protein, secreted seminal vesicle Ly-6 protein 1 (SSLP-1) purified from mouse seminal vesicles using a series of steps including ion-exchange chromatography on a diethylaminoethyl (DEAE)-Sephacel column, gel filtration on a Sephadex G-75 column, and ion-exchange HPLC on a sulfopropyl column. Further analysis demonstrated it to be a novel, previously unnamed, 17 kDa glycoprotein. N-glycosidase F treatment revealed a core protein with a molecular mass of 8720 Da. By Basic Local Alignment Search Tool Protein analysis, we found that SSLP-1 had ten conserved cysteine residues identical with other secreted Ly-6 proteins. The gene Gm191, which is located on chromosome 9, encodes SSLP-1. By Northern blotting with 21 different mouse tissues, we found that Sslp-1 mRNA was predominantly expressed in the seminal vesicle. Immunohistochemistry revealed SSLP-1 protein in the luminal fluid and mucosal epithelium of the seminal vesicles. The amount of Sslp-1 mRNA and SSLP-1 protein in the seminal vesicle was regulated by testosterone and correlated with the stage of animal maturation. The tissue-specific expression pattern suggests that SSLP-1 may play a physiological role in male mouse reproduction.




This article has been cited by other articles:


Home page
ReproductionHome page
M.-H. Lin, R. K.-K. Lee, Y.-M. Hwu, C.-H. Lu, S.-L. Chu, Y.-J. Chen, W.-C. Chang, and S.-H. Li
SPINKL, a Kazal-type serine protease inhibitor-like protein purified from mouse seminal vesicle fluid, is able to inhibit sperm capacitation
Reproduction, November 1, 2008; 136(5): 559 - 571.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. M. Abhyankar, C. Urekar, and P. P. Reddi
A Novel CpG-free Vertebrate Insulator Silences the Testis-specific SP-10 Gene in Somatic Tissues: ROLE FOR TDP-43 IN INSULATOR FUNCTION
J. Biol. Chem., December 14, 2007; 282(50): 36143 - 36154.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS  
Copyright © 2006 by the Society for Reproduction and Fertility.