Biomedical subjects

S Naaby-Hansen

Publications and source records attributed to S Naaby-Hansen.

22 records · Page 2Linked to original sources

PubMed1990

Electrophoretic map of acidic and neutral human spermatozoal proteins.

A high resolution two dimensional electrophoretic technique (2-D), isoelectric focusing followed by polyacrylamide gel electrophoresis, for separation of neutral and acidic human spermatozoal proteins was established. Silver stained 2-D gels revealed over 260 proteins with Mr 20-200 kDa and pI between 4.5 and 7.8. Membrane proteins were radio-iodinated in their hydrophobic cores with the hydrophobic photoactivatable reagent 3 (trifluoromethyl)-3-(m-[125I]iodophenyl) diazirine (TID). Externally exposed carbohydrate side chains were radiolabelled by NaB(3H)4 reduction. 2-D lectin blotting was performed with horseradish peroxidase conjugated Concanavalin A (Con A), biotinylated Vicia faba agglutinin (VFA) and Solanum tuberosum agglutinin (STA). A map of 258 human spermatozoal proteins is presented and 48 TID-labelled proteins have been biochemically characterized.

Affinity Labels↗

PubMed1990

The humoral autoimmune response to vasectomy described by immunoblotting from two-dimensional gels and demonstration of a human spermatozoal antigen immunochemically crossreactive with the D2 adhesion molecule.

The specificity of human serum antispermatozoal antibodies was analysed by immunoblotting after two-dimensional electrophoretic separation (IEF/PAGE) of human spermatozoal proteins. Spermatozoal proteins with Mr 20-200 kDa and pI between 4.5 and 7.8 were analysed for antigenicity. Fifteen sera (four female and 11 male) were analysed for antisperm IgG antibodies. Individual IgG binding patterns were observed. The antisperm antibody response to ligation of the vas deferens was described by immunoblotting analysis of sera taken pre- and post-operatively at regular intervals from three men undergoing vasectomy. The high resolution of spermatozoal antigens allowed a specific description of the humoral response to vasectomy. Both appearance and disappearance of spots were observed in the postoperative period, indicating induction of new antibody producing clones and binding of former free antibodies in circulating immunocomplexes. In one patient five glycosylated proteins induced an IgM response 2 weeks after vasectomy. Four of these autoantigens with Mr of 122 kDa, 119 kDa, 104 kDa and 77 kDa and pI of 5.9, 6.1, 7.7 and 6.0, respectively, have previously been shown to be intrinsic membrane proteins (Naaby-Hansen, (1990) J., Reprod. Immunol. 17). An observed immunochemical crossreactivity between the interneuronal adhesion molecule, D2-protein and an antigen extracted from human sperm and teratomas is discussed.

Adolescent↗

PubMed1987

Autoantibodies against spermatozoal antigens detected by immunoblotting and agglutination. A longitudinal study of vasectomized males.

Sera taken pre- and post-operatively at regular intervals within a year from 16 men undergoing vasectomy were analysed for autoantibodies against spermatozoal proteins by immunoblotting. The reaction patterns were compared with the results of sperm agglutination tests. Immunoblotting revealed the presence of autoantibodies against various spermatozoal polypeptides in all sera taken pre-operatively and post-operatively. On average, seven polypeptides showed reaction. During the post-operative period two patients developed spermatozoal agglutinins in moderate titers (greater than 16) but in immunoblotting no change in band reactivity was observed for these two patients. However, scanning of the immunoblotting results revealed that one of the patients, although without sperm agglutinins, during the post-operative period showed an increasing band colouring of a polypeptide of Mr 31,500, reflecting an increased level of the corresponding antibodies.

Adult↗

PubMed1985

Auto- and iso-antigens of human spermatozoa detected by immunoblotting with human sera after SDS-PAGE.

A sodium dodecylsulphate-polyacrylamide gel electrophoretic system for analysis of the proteins of human spermatozoa was established. Subsequent immunoblotting of the gels with human sera gave a reproducible immunolabelling of distinctive polypeptide bands. To identify auto- and isoantigens, 28 well-characterized sera from the WHO Reference Bank for Reproductive Immunology (1977, Acta Pathol. Microbiol. Scand. Sect. C, Suppl. 252) containing agglutinating and complement fixating antibodies (9 female (F) and 19 male (M) and 30 normal sera (14 F and 16 M) were analysed with reference to binding of IgG. Three spermatozoal antigens with Mr values in reduced state of 120,000 (6), 41,000 (6) and 32,000 (15) were found to be specifically correlated to the agglutinating activity of the reactive sea. (The number of these are given in parentheses). Furthermore, IgG from 2 and 3 of the normal sera and 14 and 17 of the agglutinating sera reacted with 78 and 64 kDA polypeptide, respectively. Identical binding patterns of IgG to spermatozoal polypeptides were obtained with IgG from male and female sera. The IgG-binding could not be correlated to the modes of spermatozoal agglutination. In a similar analysis of the IgM binding antigens of 21 agglutinating and 12 normal sera no differences in binding between the sera were found, except for a specific reaction to a 78 kDa antigen for 5 of the agglutinating sera.

Antigens↗