Molecular forms of soluble HLA in body fluids: potential determinants of body odor cues.

The major histocompatibility complex (MHC) has been linked to encoding for individual olfactory identity. Experiments in mice and rats proved that behavior and mating were, at least in part, determined by genes within the MHC. This study was aimed at investigating whether sHLA are excreted in human urine, saliva and sweat. In particular examination of the molecular forms in these fluids would give clues to whether break down forms of soluble MHC molecules might participate in shaping behavior. Major bands of 45, 40, and 23 kD were detectable. Increased levels of sHLA were measured using a quantitative ELISA in urine shortly before ovulation decreasing to normal levels thereafter. In animal models strain specific MHC-linked odor cues have been detected in urine. Thus, excretion of sHLA in urine might indicate a similar role for these molecules in humans.

Immunological and serological data concerning human histocompatibility antigens (HLA) and alpha 1-microglobulin co-purified from urine.

Serologically active glycoproteins (HLA) purified from urine contained only about 4% HLA antigens co-purified with alpha 1-microglobulin. The immunization of rabbits with the serologically active product gave rise to an antiserum containing two kinds of antibodies: anti-HLA-A9 and anti-alpha 1-microglobulin. The anti-HLA-A9 antibodies were detected by the lymphocytotoxicity and indirect immunofluorescence techniques against peripheral blood lymphocytes and cultured lymphoid cell lines. Anti-alpha 1-microblobulin antibodies were detected by immunoprecipitation in gel. Pure alpha 1-microglobulin gave rise to an antiserum directed only against alpha 1-microglobulin. This antiserum did not react with peripheral blood lymphocytes and cultured lymphoid cell lines.

[Molecular aspects of 2 human urinary glycoproteins with histocompatibility antigen (HLA) serological activity]. / Aspects moléculaires concernant deux glycoprotéines urinaires humaines possédant une activité sérologique d'antigènes d'histocompatibilité (HLA).

Two serologically active urinary glycoproteins (HLA-A 9 and HLA-B 12) were isolated from urine provided by a patient suffering from tubular proteinuria. Their N-terminal sequences were automatically determined. The latter were identical with the sequence of another urinary glycoprotein (protein HC). The relationship between protein HC and the serological activity is discussed.

The immunologic and molecular profiles of HLA antigens isolated from urine.

Human urine was shown to be a good source for the isolation of immunologically functional HLA-A9 antigens. The use of complex solubilization procedures can be avoided since the antigens are present in soluble form and are not complexes with membrane fragements. Purification in excess of 400-fold could be achieved by the application of cellulose ion exchange chromatography, isoelectric focusing, and acrylamide gel electrophoresis. The purified HLA-A9 antigen is composed of a glycoprotein of m.w. 38,000 and beta2-microglobulin, a peptide of m.w. 12,000. HLA-A9 antigens isolated from urine proved to be immunologically functional since they not only reacted specifically with anti-HLA-A9 alloantibody but also elicited anti-HLA-A9 xenoantibodies. These antibodies when covalently attached to Sepharose 4B specifically bound HLA-A9 antigens isolated from both serum and urine.

Purification of HLA antigens from urine.

HLA antigens were purified from urines of kidney transplanted patients, HLA was recovered as a single peak of 45,000 mol wt that was dissociated into beta2-microglobulin and a 33,000 mol wt fraction bearing the allospecificity. The purified fractions contain carbohydrates but no lipids. Electrophoretical mobility and the relative salt concentration of eluting buffers in DEAE-Sephadex chromatography were determined for six antigens of the A locus and seven antigens of the B locus. Isolectric points of antigens A1, A2, A9, and B12 were measured. Physiochemical characteristics of HLA purified from urine appear to be similar to those of papain-solubilized cell membrane HLA. Urinary HLA was shown to originate from serum and not from renal or ureteric tissue.