Proteolytic Reaction of Mammalian Spermatozoa on Gelatin Membranes

Gaddum, Penelope; Blandau, Richard J.

doi:10.1126/science.170.3959.749

Cited by 80 publications

(23 citation statements)

References 5 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…This would afford a passage for the organism through the mucus layer to the susceptible cell, to which the K88 antigen would then allow it to adhere. While this mechanism is hypothetical, it is based on a similar enzymic arrangement which allows spermatozoa to penetrate the mucus of the mammalian cervix (Gaddum & Blandau, 1970;Blandau, 1973). Once adherence is established the bacterium is in a more favourable environment than that of the lumen of the gut; it can now proliferate and cause (if it also produces enterotoxins) disease.…”

Section: Discussionmentioning

confidence: 99%

An Attempt to Identify the Intestinal Receptor for the K88 Adhesin by Means of a Haemagglutination Inhibition Test using Glycoproteins and Fractions from Sow Colostrum

Gibbons

Jones

Sellwood

1975

Journal of General Microbiology

View full text Add to dashboard Cite

S U M M A R YThe K88 antigen of Escherichia coli specifically adheres to the piglet intestinal cell; a solution of this antigen agglutinates guinea-pig red cells at 4 "C. The latter reaction was used as a model of the former, using inhibition of haemagglutination as an index of specific combination with the K88 adhesin. Inhibition was found with mucous glycoproteins and chemical modification of their heterosaccharide residues by mild acid hydrolysis, periodate oxidation or the Smith degradation procedure suggested that the terminal P-D-galactosyl structure in a heterosaccharide sidechain of a glycoprotein might combine specifically with the K88 adhesin and inhibit haemagglutination. One serum glycoprotein (fetuin), after exposure of its subterminal P-D-galactosyl residue, also inhibited haemagglutination, but high inhibitory activity was exhibited by some submaxillary glycoproteins in which this structure was absent or not prominent. It was concluded that in some cases inhibition of haemagglutination by glycoprotein was non-specific. No inhibition was found using glycosaminoglycans, glycogen or any simple sugar or glycoside. Sow colostrum was inhibitory but this was associated mainly with its y-globulin fraction. Some inhibitory activity was traced to a colostral glycopeptide fraction of low molecular weight but the smaller colostral oligosaccharides were not inhibitory; the composition of these components in sow colostrum is reported.

show abstract

Section: Discussionmentioning

confidence: 99%

An Attempt to Identify the Intestinal Receptor for the K88 Adhesin by Means of a Haemagglutination Inhibition Test using Glycoproteins and Fractions from Sow Colostrum

Gibbons

Jones

Sellwood

1975

Journal of General Microbiology

View full text Add to dashboard Cite

show abstract

“…It seems to be generally agreed, however that acrosin (or sperm trypsin-like enzyme) is responsible for sperm penetration of the zona pellucida (Srivastava et al, 1965;Stambaugh et al, 1969;Zaneveld et al, 1973;, but the evidence that these particular enzymes are even found in the acrosome has been largely circumstantial. It has been based on changes in sperm morphology after enzyme extraction (Pedersen, 1972;Brown & Hartree, 1974;Churg et al, 1974;Srivastava et al, 1974), on the localization of labelled non-specific enzyme inhibitors (Stambaugh & Buckley, 1972) and on the detection of proteolytic activity using gelatin films (Gaddum & Blandau, 1970;Benitez-Bribiesca & Velazquez-Meza, 1972;Gaddum-Rosse & Blandau, 1972;Penn et al, 1972;Allen et al, 1974). This proteolytic activity is unlikely to be specific as there is increasing evidence that more than one proteinase exists in spermatozoa (Dott & Dingle, 1968;Allison & Hartree, 1970;Multimaki & Niemi, 1972;Yanagimachi & Teichman, 1972;Bernstein & Teichman, 1973;Srivastava & Foley, 1973).…”

mentioning

confidence: 96%

Acrosomal Enzymes: Immunochemical Localization of Acrosin and Hyaluronidase in Ram Spermatozoa

Morton¹

1975

Reproduction

View full text Add to dashboard Cite

“…It is concluded that (pro)acrosin (acrosin-inhibitor) (Gaddum and Blandau, 1970 ;Sakai and Yasuda, 1981 ;Green and Hockaday, 1978 ;Harrison et al, 1982 ;Huneau et al, 1983) Proacrosin content and radioactivity were assayed in the fractions, and those having proacrosin activity were pooled. The pooled fractions of ( 14 C)-glucosamine-labelled material were further purified by hydrophobic chromatography on a Spheron P-300 1 x 4.8 cm column equilibrated with 0.3 M acetic acid, 0.05 M NaCl, pH 3.0 (Zelezna and 6echov6, 1982).…”

mentioning

confidence: 99%

Studies on acrosome labelling of mammalian spermatozoa by radioactive sugars

Kopečný¹,

Cechová²,

Železná³

et al. 1984

Reprod. Nutr. Dévelop.

View full text Add to dashboard Cite

Summary. The localization of glycoprotein synthesis and storage was studied during acrosome formation in guinea-pig using fine-structure autoradiography after ( 3 H1-fucose incorporation. Three days after ( 3 H1-fucose injection, labelling in spermatids was concentrated in the matrix of developing acrosomes, and it was evident that the fucosylation of acrosomal glycoproteins largely overshadowed the fucosylation of other spermatid glycoproteins.Acrosin labelling and its quantitative relation to labelling of other glycoproteins was examined in mature rabbit spermatozoa after incorporation of (&dquo;CI-fucose or (' 4 C)-glucosamine during spermatogenesis. Cauda epididymis spermatozoa recovered 21 days after intratesticular application of (&dquo;C)-fucose or ('4C1-glucosamine were analysed for acrosin specific labelling after acid extraction and gel filtration. In all the material examined, radioactivity was detected in the proacrosine fractions ; radioactivity in purified proacrosin amounted to at least 2 % of the total radioactivity in the epididymal sperm population. In addition to the peak with radioactive proacrosin, another radioactive peak in ('4C1-glucosamine-labelled material was attributed to a glycoprotein intraacrosomal inhibitor of acrosin.It is concluded that (pro)acrosin (acrosin-inhibitor) complexes seem to contribute significantly to acrosomal glycoprotein labelling by radioactive sugars and that the distribution of these complexes may at least partly correspond to their cytochemically detectable component, acrosin. The superposition of the distribution of acrosin and of other acrosomal glycoproteins during acrosome reaction can be explained by the fact that the dispersal of most of the acrosomal content is linked to proacrosin activation.Introduction.

show abstract

Proteolytic Reaction of Mammalian Spermatozoa on Gelatin Membranes

Cited by 80 publications

References 5 publications

An Attempt to Identify the Intestinal Receptor for the K88 Adhesin by Means of a Haemagglutination Inhibition Test using Glycoproteins and Fractions from Sow Colostrum

An Attempt to Identify the Intestinal Receptor for the K88 Adhesin by Means of a Haemagglutination Inhibition Test using Glycoproteins and Fractions from Sow Colostrum

Acrosomal Enzymes: Immunochemical Localization of Acrosin and Hyaluronidase in Ram Spermatozoa

Studies on acrosome labelling of mammalian spermatozoa by radioactive sugars

Contact Info

Product

Resources

About