Histochemical localization of glycosidases in dog epididymis

Sinowatz, Fred; Fischer, M.; Skolek-Winnisch, Rita; Chandler, John

doi:10.1007/bf01041269

Cited by 19 publications

(9 citation statements)

References 12 publications

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“…localized {3-glucuronidase in the early stages of spermatogenesis in rat. This observation is in sharp contrast to the localization of hyaluronidase which is uniformly concentrated in various stages of germ cell line 18 and specifically at the junctions of cells.te As compared to the localization in human epididymis, Sinowats et al 19 epididymis in dog, whereas Hayashi/" noted positive granules of f)-glucuronidase situated supranuclearly in some cells in the cauda region. The difference in the staining pattern in caput and cauda epididymis of humans is evident, which may represent some modifications of the enzyme.…”

Section: Discessionmentioning

confidence: 66%

Immunological Specificity of Beta‐Glucuronidase From Human Seminal Plasma and its Immunolocalization in the Human Reproductive Tract*

Gupta

Singh

1983

American Journal of Reproductive Immunology

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Beta-glucuronidase (beta-glucuronidase) in human seminal plasma consists of two forms of isozymes (major and minor forms). Antiserum prepared against the purified major form of beta-glucuronidase in rabbits was used for studies of immunological specificity and immunohistochemical localization of beta-glucuronidase in the human male reproductive tract. By ouchterlony immunodiffusion technique, anti-beta-glucuronidase serum showed reaction of identity with human tissue extracts such as liver, spleen, lungs, testis, epididymis, prostate, and seminal vesicles. Though monkey testis and epididymis extracts completely reacted with human seminal beta-glucuronidase antiserum, no cross-reaction was observed with mouse and rat tissue extracts. Immunofluorescent studies revealed that beta-glucuronidase is localized in the early stages of spermatogenesis in testis, in columnar cells of the epididymis, and in glandular cells of the prostate and seminal vesicles. Consistent absence of fluorescence in the lumens of testis and epididymis as well as negative cross-reaction between antiserum and sperm extracts suggested that major form of beta-glucuronidase in human seminal plasma is not immunologically identical with human spermatozoa. It is concluded that major form of beta-glucuronidase in seminal plasma is not tissue-specific although it appears to have limited species specificity.

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Section: Discessionmentioning

confidence: 66%

Immunological Specificity of Beta‐Glucuronidase From Human Seminal Plasma and its Immunolocalization in the Human Reproductive Tract*

Gupta

Singh

1983

American Journal of Reproductive Immunology

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“…It is possible that both populations of acid hydrolasebearing particles come from the epithelium of the duct since it has been demonstrated by other authors that the histochemical activity of AP, NAG, and GLU is almost entirely confined in the epithelial cells (Sinowatz et al, 1979;Moniem and Glover, 1972). Moreover, Kemp and Killian (1978) found that the epithelial cells of the rat epididymis separated at l g in albumin gradients contained most of the activity of various acid glycosidases.…”

Section: Discussionmentioning

confidence: 94%

Two populations of acid hydrolase‐containing particles in rat epididymis

Mayorga

Bertini

1983

Journal Cellular Physiology

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Two populations of acid hydrolase-containing particles were distinguished in homogenates of rat epididymis. One of them was rich in acid phosphatase activity, equilibrated at density 1.17 in a sucrose gradient, and it sedimented between 12,000g 2.5 min and 43,000g 60 min (light particles). The other was poor in acid phosphatase activity and rich in N-acetyl-beta-D-glucosaminidase, arylsulphatase, and beta-glucuronidase activity, equilibrated at density 1.20 in a sucrose gradient and it sedimented between 400g 2.5 min and 12,000g 2.5 min (heavy particles). 131I-albumin (RISA) injected into the lumen of the cauda was partially recovered in subcellular particles of homogenates of this region. These particles, incubated at pH 5, were able to digest the engulfed RISA. The subcellular distribution of RISA-containing particles and RISA-digesting particles was similar to that of the heavy hydrolase-containing particles. This suggests that these latter are engaged, at least in part, in heterophagic processes.

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“…The GPs coating the surface of boar epididymal sperm are gradually lost due to the hydrolytic effects of enzymes secreted by the epididymal epithelium [6]. Canine epididymal fluid contains various types of glycosidases, e.g., N-acetyl-β-glucosaminidase, β-galactosidase and α-manosidase [26]. Thus, DBA-and SBA-lectin-binding GPs on canine sperm surface are therefore presumably removed by the effects of the enzymes in the epididymal fluid during sperm transport through the cor- pus epididymides and the cauda epididymides.…”

Section: Discussionmentioning

confidence: 99%

Lectin-Binding Characteristics and Capacitation of Canine Epididymal Spermatozoa

Kawakami

Morita

Hori

et al. 2002

The Journal of Veterinary Medical Science

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ABSTRACT. Cross sections of the testes and the caput, corpus and cauda epididymides removed from 12 dogs were stamped on glass slides, and the sperm on the slides were stained with 6 different FITC-lectins (Con A, DBA, PNA, PSA, SBA, and WGA) to examine the characteristics of the surface glycoproteins (GPs) on canine epididymal sperm. The corpus epididymal sperm were washed three times by centrifugation, and their lectin-binding characteristics were investigated. The washed sperm from the corpus and cauda epididymides were incubated for 24 hr, and the fertilizing capacity of the sperm was evaluated by calculating the percentages of actively motile sperm (%MO), hyperactivated sperm (%HA), and acrosome-reacted sperm (%AR), and the number of canine zona-pellucida (ZP)-binding sperm. The testicular sperm did not stain with SBA lectin, but the SBA lectin fluorescence was observed on the surface of the enitire heads of the caput epididymal sperm. Although all of the entire heads or acrosomal regions of the corpus epididymal sperm stained with all 6 FITC-lectins, the heads and acrosomal regions of the cauda epididymal sperm did not stain with DBA or SBA lectins. Washing the sperm from the corpus epididymis resulted in loss of the fluorescence of the FITC-DBA and -SBA lectins. The mean %MO, %HA, %AR, and ZP-binding number of the cauda epididymal sperm after 24 hr of incubation were higher than the values for the corpus epididymal sperm. All of the mean values for the washed sperm from the corpus and cauda epididymides were higher than the values for the unwashed sperm from the corpus and cauda, and with the exception of %AR, the values from the washed sperm from the corpus epididymis were significantly higher (P<0.05, 0.01). The results indicate that DBA-and SBA-lectin-binding GPs on the surface of canine epididymal sperm are associated with the fertilizing capacity and may be decapacitation factors. KEY WORDS: canine, capacitation, epididymis, lectin, sperm.J. Vet. Med. Sci. 64 (7): [543][544][545][546][547][548][549] 2002 It is well-known that the mammalian sperm plasma membrane surface is coated with various glycoproteins (GPs) [8,9,20,21,25]. Although some GPs are already present on the surface of immature sperm in the seminiferous tubules of the testis [18,19], the surface of the sperm becomes covered with a wide variety of GPs secreted by the epididymal epithelium during sperm transit through the epididymis [5,6,17,23]. Sperm surface GPs are thought to induce sperm maturation and fertilizing capacity [10,20] in the epididymal duct, and techniques utilizing fluorescein-isothiocyanate (FITC)-labeled lectins have revealed that the sperm surface GPs are biochemically modified during sperm transit through the epididymis and that there are species-dependent differences in sperm surface GPs [1,5,6,17,20,23]. Some of the GPs on the surface of epididymal sperm have been suspected of acting as decapacitation factors (DFs) [16,21], and while sperm fertilizing capacity is induced by removing DFs from the sperm surface [7,1...

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Histochemical localization of glycosidases in dog epididymis

Cited by 19 publications

References 12 publications

Immunological Specificity of Beta‐Glucuronidase From Human Seminal Plasma and its Immunolocalization in the Human Reproductive Tract*

Immunological Specificity of Beta‐Glucuronidase From Human Seminal Plasma and its Immunolocalization in the Human Reproductive Tract*

Two populations of acid hydrolase‐containing particles in rat epididymis

Lectin-Binding Characteristics and Capacitation of Canine Epididymal Spermatozoa

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