Temporal expression and localization of protein farnesyltransferase during spermiogenesis and posttesticular sperm maturation in the hamster

• Published in: Molecular reproduction and development Vol. 48; no. 1; pp. 71 - 76
• Main Authors: Olson, Gary E., Nagdas, Subir K., Winfrey, Virginia P.
• Format: Journal Article
• Language: English
• Published: Hoboken Wiley Subscription Services, Inc., A Wiley Company 01.09.1997; Wiley-Liss
• Subjects: Alkyl and Aryl Transferases; Animals; Biological and medical sciences; Cricetinae; Epididymis - cytology; farnesyltransferase expression and localization; Farnesyltranstransferase; Fluorescent Antibody Technique, Indirect; Fundamental and applied biological sciences. Psychology; hamster sperm; hamster spermatids; Immunoblotting; Male; Mammalian male genital system; Mesocricetus; Morphology. Physiology; protein lipidation; Sperm Maturation; Spermatogenesis; Spermatozoa - enzymology; Spermatozoa - physiology; spermiogenesis; Transferases - analysis; Transferases - biosynthesis; Vertebrates: reproduction; Spermatozoa; Spermiogenesis; Enzyme; Transferases; Rodentia; Male; Male genital duct; Germinal cell; Gene expression; Male genital system; Spermatid; Ripening; Vertebrata; Epididymis; Mammalia; Distribution; Hamster
• ISSN: 1040-452X; 1098-2795
• DOI: 10.1002/(SICI)1098-2795(199709)48:1<71::AID-MRD9>3.0.CO;2-M

Spermiogenesis and posttesticular sperm maturation in the epididymis are distinct developmental processes that result in a polarized spermatozoon possessing a plasma membrane partitioned into segment‐specific domains of distinct composition and function. The mechanisms that specify the distribution of intracellular organelles and target proteins to restricted membrane domains are not well understood. In this study we examined the expression pattern and distribution of protein farnesyltransferase (FTase) in hamster spermatids and epididymal spermatozoa to determine if protein lipidation may represent a potential mechanism to regulate protein association with specific organelles or the plasma membrane. Round spermatids exhibited only weak immunostaining with antibody against the β‐subunit of FTase, whereas elongating spermatids exhibited a high level of FTase expression that was segregated to the cytoplasmic lobe surrounding the anterior flagellum. Although FTase was released with the residual body, mature spermatids retained FTase within the midpiece and cytoplasmic droplet. In epididymal spermatozoa, FTase remained associated with the cytoplasmic droplet during its migration to the midpiece‐principal piece junction; following release of the cytoplasmic droplet, no immunodetectable FTase was noted in the midpiece segment. Immunoblotting demonstrated the presence of both the α and β subunits of FTase in sperm lysates. The temporal expression pattern and restricted distribution of FTase in spermatids and epididymal spermatozoa suggest a potential role in regulating protein association with specific organelles and/or membrane domains of the mature spermatozoon. Mol. Reprod. Dev. 48:71–76, 1997. © 1997 Wiley‐Liss, Inc.