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Abstract
Sphingomyelin synthase (SMS) is a cellular enzyme that catalyzes de novo synthesis of sphingomyelin (SM), which is a vital lipid component of cell membranes. Both members of the SMS family, SMS1 and SMS2, are found in mammalian testes and they are located in distinctive subcellular compartments, with SMS1 in the Golgi apparatus and SMS2 in the plasma membrane. At present, the precise function of SMS in the testis remains unknown. Recent studies have demonstrated an unique association of SMS2 with spermatids, particularly near developing acrosomes and the junction restructuring site at the apical ectoplasmic specialization (a testis-specific atypical adherens junction type) and Leydig cells in the rat testis. These data illustrate the possible involvement of SMS2 in spermiogenesis and, perhaps, steroidogenesis in male reproductive function. This review summarizes the latest findings on SMS in the field, particularly its role in testicular function.
Financial & competing interests disclosure
Studies in the authors’ laboratory were supported in part by grants from the NIH (NICHD, U01 HD045908; R03 HD051512; U54 HD029990 Project 5) and the CONRAD Program (CICCR CIG-01–72). The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.
No writing assistance was utilized in the production of this manuscript.