Acid Glycohydrolases in Rat Spermatocytes, Spermatids and Spermatozoa: Enzyme Activities, Biosynthesis and Immunolocalization

Mammalian sperm acrosome contains several glycohydrolases thought to aid in the dispersion and digestion of vestments surrounding the egg. In this study, we have used multiple approaches to examine the origin of acrosome-associated glycohdyrdolases. Mixed spermatogenic cells, prepared from rat testis, were separated by unit gravity sedimentation. The purified germ cells (spermatocytes [SP], round spermatids [RS], and elongated/condensed spermatids [E/CS]) contained several glycohydrolase activities. Metabolic labeling in the cell culture, immunoprecipitation, and autoradiographic approaches revealed that β-D-galactosidase was synthesized in SP and RS in 88/90 kDa forms which undergo processing in a cell-specific manner. Immunohistochemical approaches demonstrated that the enzyme was localized in Golgi membranes/vesicles, and lysosome-like structures in SP and RS, and forming/formed acrosome of E/CS

Analysis of Human Gingival Tissue and Gingival Crevicular Fluid β-Glucuronidase Activity in Specific Periodontal Diseases

Background: beta -glucuronidase (betaG) is one of the enzymes involved in the destruction of non-collagenous components of the extracellular matrix. It is also considered an indicator or predictor of periodontal disease activity. The present study was conducted to determine the presence and the levels of betaG activity in gingival tissue and gingival crevicular fluid (GCF) in periodontal disease and health status. The validity of 2 expressions of data, total betaG activity versus betaG concentration, and the correlations between clinical periodontal status and betaG profile was also evaluated