Influence of Gonadectomy, Sex Hormones and Other Factors, on the Activity of Certain Glycosidases in the Rat and Mouse

Conchie, J.; Findlay, June

doi:10.1677/joe.0.0180132

Cited by 77 publications

(30 citation statements)

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“…In addition, increased epididymal glycosidase activities are age-and hormone-dependent [2,3] in the rat, although the biological significance of this maturational phenomenon is not clear. In the rat as well as other mammals, investigators have detected glycosidase activities associated with sperm, epididymal fluid, epididymal epithelial cells, and seminal plasma [4][5][6][7].…”

Section: Introductionmentioning

confidence: 99%

Synthesis and Processing of Rat Sperm-Associated α-L-Fucosidase1

Hancock¹,

Raab²,

Aronson³

1993

Biology of Reproduction

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alpha-L-Fucosidase (alpha-fucosidase) is the most active of a number of glycosidases measured in rat epididymal sperm through use of artificial 4-methylumbelliferyl substrates. In addition, enzyme activity can be detected in purified populations of testicular germ cells; in comparison to round spermatids, caput epididymal sperm show at least a 1.8-fold increase in alpha-fucosidase activity per cell. Metabolic labeling of cultured testicular germ cells, followed by immunoprecipitation and SDS-PAGE, reveals synthesis of alpha-fucosidase as a polypeptide of 54 kDa in pachytene spermatocytes and round spermatids but no synthesis in condensing spermatids. This polypeptide is N-glycosylated but does not undergo further processing as determined by pulse/chase labeling and treatment with endoglycosidase H. In contrast, the alpha-fucosidase synthesized by cultured clone 9 cells (a rat liver-derived cell line) undergoes processing from a 54-kDa precursor to a slightly larger intermediate centered at 56 kDa on SDS-PAGE (via carbohydrate modification) and finally to a 52-kDa mature polypeptide. Immunoblotting confirms the presence of the 54-kDa form of alpha-fucosidase in testicular germ cells and shows the existence of a 52-kDa mature polypeptide in epididymal sperm. In addition, immunoreactive polypeptide is more prominent in caput epididymal sperm preparations; this is consistent with the increase in enzyme activity. In the absence of alpha-fucosidase synthesis beyond the round spermatid stage of development, it appears that alpha-fucosidase may be acquired from the luminal fluid by sperm during transit through the excurrent duct system. This hypothesis is supported by evidence that metabolically labeled cultured epididymal epithelial cells synthesize and secrete into culture medium an immunoprecipitable 58-kDa alpha-fucosidase polypeptide. Analysis of sperm isolated from the first part of the caput epididymis indicates that both acquisition and processing of sperm-associated alpha-fucosidase takes place prior to or concomitant with arrival of sperm in the epididymis.

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Section: Introductionmentioning

confidence: 99%

Synthesis and Processing of Rat Sperm-Associated α-L-Fucosidase1

Hancock¹,

Raab²,

Aronson³

1993

Biology of Reproduction

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“…Data on both tissue and sperm α‐glucosidase activity suggest an inhibitory effect of ethanol. The inhibitory response of α‐glucosidase may be attributed to low epididymal testosterone and DHT levels, since earlier studies have shown androgen dependence of epididymal α‐glucosidase activity in the rat and mouse ( Conchie & Findlay, 1958; Grandmont et al ., 1983 ). In the present study, activity of α‐glucosidase recovered along with restoration of epididymal androgens in ethanol‐withdrawn rats.…”

Section: Discussionmentioning

confidence: 99%

Effects of ethanol ingestion on epididymal glycosidases and fertility in the rat

et al. 1998

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Epididymal glycosidases play a role in sperm maturation by modifying sperm surface glycoproteins. To study the effects of ethanol on epididymal sperm maturation, ethanol (3 g/kg body weight as 25%, v/v) was administered to a group of rats by gastric-intubation twice daily for 30 days. In another group, rats were also treated with alcohol for 30 days but were then withdrawn from treatment for 30 days to assess the reversibility of ethanol-induced effects. Ethanol-induced changes in epididymal tissue and sperm glycosidases, cauda epididymal sperm motility and the fertility of rats were assessed. Ethanol treatment caused a marked decrease in the specific activities of glycosidases in both tissues and spermatozoa from epididymal segments. Cauda epididymal sperm motility and the fertility of ethanol-treated rats were significantly impaired compared to control rats fed an isocaloric diet. These changes are likely to be the consequence of direct and indirect effects of ethanol mediated through subnormal testosterone and dihydrotestosterone. Most of these changes were found to be reversible. The present study suggests that impaired activity of sperm glycosidases may be one of the factors responsible for defective sperm motility and fertilizing potential in ethanol-treated rats.

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“…The activity of ß-glucuronidase has shown androgen dependency, e.g., in the epi didymis of rat and mouse [28]. Also in the bull epididymis, the activity of ß-glucuroniThe biochemical distribution of ß-gluc uronidase was studied in the different repro ductive organs, seminal plasma and sperma tozoa of the bull.…”

Section: Discussionmentioning

confidence: 99%

ß-Glucuronidase in the Bull Seminal Plasma and Reproductive Organs

Jauhiainen¹,

Vanha‐Perttula²

1986

Enzyme

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The biochemical distribution of ß-glucuronidase activity was studied in different reproductive organs, seminal plasma and spermatozoa of the bull. The highest specific activity was found in the epididymis, where the activity seemed to be mostly in nonsecretory and only partly in secretory form. A molecular weight of 340 X 10^3 to 360 X 10^3 was recorded for ß-glucuronidase in the bull seminal plasma and different reproductive organs with gel filtration on Sepharose 6B. In chromatofocusing four activity areas (CF-1 to CF-4) were usually obtained for ß-glucuronidase in the bull seminal plasma. The major peak CF-2 (also in the different reproductive organs) had a pi value of 5.6-5.3 and the two minor activity areas CF-1 and CF-3 had pi values of 6.0-5,8 and 5.2-4.5, respectively. Peak CF-4 eluted with a NaCl gradient after the Polybuffer elution and possibly represents an enzyme form incompletely detached from negatively charged cellular material. Isoelectric focusing on polyacrylamide gel confirmed the heterogeneity of ß-glucuronidase, since several activity bands were detected in the secretion of the different parts of the epididymis. ß-Glucuronidase activities CF-1, CF-2 and CF-3 had similar pFl activity profiles (pH optimum around pH 3.0-4.0) and response to thermal inactivation at 50 °C. The multiple ß-glucuronidase activities of the bull seminal plasma are proposed to derive mainly from the secretion of the cauda epididymidis.

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Influence of Gonadectomy, Sex Hormones and Other Factors, on the Activity of Certain Glycosidases in the Rat and Mouse

Cited by 77 publications

References 0 publications

Synthesis and Processing of Rat Sperm-Associated α-L-Fucosidase1

Synthesis and Processing of Rat Sperm-Associated α-L-Fucosidase1

Effects of ethanol ingestion on epididymal glycosidases and fertility in the rat

ß-Glucuronidase in the Bull Seminal Plasma and Reproductive Organs

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