Urban environmental health.

In 1983, Karlsson et al. described a genetic polymorphism associated with human urinary high molecular weight glyco-proteins. In this, four components with different mobilities in sodium dodecyl sulphate polyacrylamide (SDS PAGE) gels were identified by their reaction with radioiodinated peanut lectin and each individual was found to exhibit one or two bands. Familial studies showed that the four alleles within the system are inherited in a normal Mendelian fashion and population analyses confirmed that the observed distribution of phenotypes in normal individuals lies close to Hardy-Weinberg predictions. Subsequently, it was determined that the anti-breast carcinoma monoclonal antibody, NCRC-l 1, like the related anti-human milk fat globule antibodies, HMFG-1 and HMFG-2 (Burchell et al., 1983) and the anti-tumour antibody, Cal (which defines the Ca antigen found on a range of human malignant cells-Ashall et al., 1982), also reacted with a similar family of high molecular weight glycoproteins which are present in the urine of all individuals and in the sera of breast cancer patients (Swallow et al., 1986; Price et al., 1987). In addition, these glycoproteins are found on the luminal surfaces of glandular epithelia, on milk fat globule membranes and associated with most epithelial malignancies (Ellis et al., 1984). It has been suggested that these high molecular weight polymorphic glycoproteins, have a protective function in their normal environment (e.g. stabilization of milk fat emulsions in the digestive tract until milk fat is hydrolysed by lipases and absorbed in the intestine-Shimizu and Yamauchi (1982)-or as a shield in the urothelium providing protection to the underlying cells against low urinary pH-Bramwell et al. (1983). If this is so, then it is feasible that specific phenotypes of the antigen may be associated with a particular susceptibility (or resistance) to carcinogenic insult and/or transformation processes leading to the onset of neoplasia. This proposal has been examined in the present investigation by comparing the distribution of NCRC-11 defined glycoprotein phenotypes in patients with breast cancer with the distribution of phenotypes in a comparable sex-matched healthy population. Urine samples from advanced breast cancer patients with progressive disease and from malignant disease-free female controls (laboratory personnel and outpatients at the University Hospital, Nottingham) were stored at-20°C until use. Urine samples were concentrated approximately 15-fold by dialysis against Aquacide II (Calbiochem, Los Angeles, CA). A panel of concentrated urine samples of defined peanut lectin binding-phenotype was kindly provided and these were employed as standards for phenotype designation. Concentrated …