Abstract
A monoclonal IgM kappa from a patient with Waldenström's macroglobulinaemia (IgM-Rod) was found to react at temperatures below 28 degrees C with all tissue basement membranes and the cell coat of non-haematopoietic cells. IgM-Rod antibody was directed against heparan sulphate side chains of heparan sulphate proteoglycans as shown by binding in a solid-phase ELISA to heparan sulphate glycosaminoglycans but not to other purified subcomponents of the extracellular matrix; and by specific inhibition of the observed reactivity by heparitinase treatment. IgM-Rod showed cross-reactivity by indirect immunofluorescence with an as yet unidentified structure expressed in the nucleus during cell division and becoming associated with the mitotic spindle apparatus. The co-existence of both binding activities for heparan sulphate and nuclei determinants in the same IgM molecule was deduced from adsorption-elution experiments and from the inhibitory effect of a mouse monoclonal anti-idiotypic antibody directed against the paratope of IgM-Rod.