This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Li, S.-H. Articles by Chang, W.-C. Search for Related Content PubMed PubMed Citation Articles by Li, S.-H. Articles by Chang, W.-C.

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

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.