Localization of sulfated glycoprotein-2 (clusterin) on spermatozoa and in the reproductive tract of the male rat

S R Sylvester; C Morales; R Oko; M D Griswold

doi:10.1095/biolreprod45.1.195

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Localization of sulfated glycoprotein-2 (clusterin) on spermatozoa and in the reproductive tract of the male rat

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Localization of sulfated glycoprotein-2 (clusterin) on spermatozoa and in the reproductive tract of the male rat

S R Sylvester, C Morales, R Oko and M D Griswold

Biology of reproduction, Vol.45(1), pp.195-207

07/1991

DOI: https://doi.org/10.1095/biolreprod45.1.195

Handle:

https://hdl.handle.net/2376/101706

PMID: 1878433

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Abstract

Epididymis - metabolism

Immunohistochemistry

Testis - metabolism

Molecular Weight

Glycoproteins - metabolism

Male

Epididymis - cytology

Spermatozoa - metabolism

RNA, Messenger - metabolism

Rats, Inbred Strains

Clusterin

Sperm Tail - metabolism

Sertoli Cells - cytology

Cell Membrane - metabolism

Organ Culture Techniques

Glycoproteins - genetics

Sertoli Cells - metabolism

Sulfur - metabolism

Molecular Chaperones

Testis - cytology

RNA, Messenger - genetics

Cells, Cultured

Rats

Cell Membrane - ultrastructure

Blotting, Western

Blotting, Northern

Animals

Sperm Tail - ultrastructure

Fluorescent Antibody Technique

Spermatozoa - ultrastructure

Sulfated glycoprotein-2 (SGP-2) is one of the major proteins secreted by rat Sertoli cells and epididymal cells in culture. The disulfide-linked dimeric protein secreted by Sertoli cells and found in seminiferous tubule fluid is composed of monomers of Mr 47 000 and 34 000 whereas the epididymal protein exhibits monomers of Mr 40 000 and 29 000. When both forms were chemically or enzymatically deglycosylated, they yielded proteins of similar molecular weight. No modification of the higher molecular weight testicular form by epididymal cells or fluids could be detected in incubation media. SGP-2 mRNA was localized in epididymal epithelium by in situ hybridization. Northern blot analysis indicated the testicular and epididymal mRNAs were of similar size. These findings suggest that the two forms of the protein occur because of tissue-specific post-translational modifications. The detergent-extracted protein from washed testicular spermatozoa is of the higher molecular weight form while epididymal sperm carry the lower molecular weight form. Immunohistochemical evidence suggests that the testicular form is removed prior to the initial segment of the epididymis and the epididymal form is applied in the proximal caput epididymidis. SGP-2 was immunolocalized to the sperm membrane at the ultrastructural level and was distinctly different from the immunolocalization of outer dense fiber proteins and fibrous sheath proteins.

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Title: Localization of sulfated glycoprotein-2 (clusterin) on spermatozoa and in the reproductive tract of the male rat
Creators: S R Sylvester - Department of Biochemistry and Biophysics, Washington State University, Pullman 99164
C Morales
R Oko
M D Griswold
Publication Details: Biology of reproduction, Vol.45(1), pp.195-207
Academic Unit: Molecular Biosciences, School of
Publisher: United States
Grant note: HD-10808 / NICHD NIH HHS
Identifiers: 99900546657901842
Language: English
Resource Type: Journal article