It has been appreciated for some time that all mammalian basement membranes contain type IV collagen, laminin, entactin/nidogen and proteoglycans [ 11, but more recently it has become clear that there may be a high degree of tissue specificity in the expression of various forms of these molecules. For example, a chain of laminin known as s-laminin [2], is restricted to basement membranes which are present between two tissues, such as the kidney glomerular loop and the neuromuscular junction. In a similar way, it now appears that many forms of proteoglycan may be present in basement membranes, varying not only in core protein but also carbohydrate characteristics. Basement membrane heparan sulphate proteoglycan (HSPG) was first isolated from the murine transplantable Engelbreth-Holm-Swarm (EHS) tumour matrix [3, 41, and was found to have comparatively low buoyant density (approx. 1.3 g/ml), because of a high protein/carbohydrate ratio, the core protein being 400 kDa. As reported by us and others [ 3, 5, 61, antibodies against this HSPG showed widespread and uniform basement membrane staining of all tissues so far examined, including those of the human. Howcvcr, immunohistochemical analysis with polyclonal antibodies raised against a small HSPG with low protein/carbohydrate ratio and high buoyant density (approx. 1.5 g/ml), indicated this had a heterogeneous distribution in rat basement membranes 171. Although synthesized by most epithelia, including those of the skin and mammary gland, the small HSPG was apparently absent from visceral smooth muscle and cardiac muscle basement membranes. It is currently debated whether small basement membrane HSPGs are derived from the large HSPG by limited proteolysis. Evidence from the EHS tumour and studies on the kidney in vivo have lent support to this view [8, 91. Equally, other evidence has indicated that small HSPGs may be unique [6]. Our studies with antibodies support the case for at least some unique small HSPGs, but the problem can only clearly be resolved by protein sequence data. This is partially available for the large HSPG [lo], and we are currently cloning cDNAs from a mammary epithelial l g t l 1 library, screening with the antibodies against a small basement membrane HSPG [7]. So far, our sequence data do not coincide with those available for the large HSPG, and further important information has emerged from Northern blots. The mRNA encoding the small HSPG was found to be approximately 2.6 kb, whereas that for the large HSPG is 10I 1 kb. Therefore, we now have some evidence for the distinct nature of at least one small HSPG core protein. However, as we and others have indicated [6, 71, there may be some conservation of epitopes between members of this class of basement membrane component which can be detected immunologically. Whether these are protein or carbohydrate determinants is presently unknown. The complexity of basement membrane proteoglycans does not end with HSPGs. We have now identified a chon-