The proliferation and development of haemopoietic stem cells takes place in close association with marrow stromal cells. This intimate cell contact presumably enables the stem cells and their progeny to respond to stimuli present on the stromal cell surface. While the nature of these stimuli has not been determined, it is likely that growth factors play some role. Recently, it was demonstrated that the natural and the recombinant haemopoietic growth factor, granulocyte/macrophage colony stimulating factor (GM-CSF), could be adsorbed out of solution by an extract of human marrow stromal extracellular matrix (ECM) with retention of biological activity. However, the precise ECM molecules involved were not identified. Here, we clearly demonstrate that the major sulphated glycosaminoglycan of mouse marrow stroma, heparan sulphate, possesses the ability to adsorb both GM-CSF and the multilineage haemopoietic growth factor, Interleukin 3 (IL-3). Furthermore, these growth factors, once bound, can be presented in the biologically active form to haemopoietic cells.

This study demonstrated the presence of irritant, carcinogenic and neurotoxic compounds in electrosurgical smoke. This may have considerable implications for the health and safety of all involved in surgical practice, as exposure to these compounds pose potential risks to health.

1. Tamm-Horsfall glycoprotein was isolated from hamster urine and antiserum against it was produced in rabbits. Immunoglobulin G was isolated from the antiserum. 2. Indirect methods of immunofluorescence staining were applied to kidney sections previously fixed by both perfusion and immersion methods. Tamm-Horsfall glycoprotein was identified associated with only the cells of the ascending limb of the loop of Henle and the distal convoluted tubule. Maculae densae were free of the glycoprotein. 3. Indirect immunoperoxidase procedures with light microscopy were applied to kidney sections. The results extended those found by immunofluorescence by showing that the glycoprotein is largely associated with the plasma membrane of the cells. Macula densa cells were shown to be free of the glycoprotein, although the luminal surface of the remaining cells in the transverse section of the nephron at that region was shown to contain it. 4. A variety of immuno-electron-microscopic techniques were applied to sections previously fixed in a number of ways. Providing periodate/lysine/paraformaldehyde was used as the fixative, the glycoprotein was often seen to be present not only on the luminal surface of the cells of the thick ascending limb of the loop of Henle and of the distal convoluted tubule, but also on the basal plasma membrane, including the infoldings. 5. It is generally accepted that the hyperosmolarity in the medulla of the kidney results from passage of Cl(-) ions with their accompanying Na(+) ions across the single cell layer of the lumen of the thick ascending limb of the loop of Henle, a region of the nephron with relatively high impermeability to water. We suggest that Tamm-Horsfall glycoprotein operates as a barrier to decrease the passage of water molecules by trapping the latter at the membrane of the cells. Our hypothesis requires the glycoprotein on the basal plasma membrane also.

Summary. Fractionation of vitamin B12 binders in a normal human serum pool showed a distribution of 92% Transcobalamin II (TCII) and 8% Transcobalamin I (TCI) on DEAE‐cellulose chromatography. Separation of the same serum pool using gel filtration gave 74% TCII and 26% TCI. This 18% discrepancy could be due either to massive contamination of the DEAE‐cellulose TCII peak with TCI, or to the presence of a high molecular weight binder which elutes with TCII on DEAE‐cellulose, and with TCI on gel filtration. Refractionation of the TCII peak showed it to be relatively uncontaminated with TCI. Removal of the low molecular weight binders with charcoal consistently gave a peak in the TCII area on DEAE, which subsequent gel filtration analysis showed to be of high molecular weight. This new binder is further distinguished from TCI by the observation that its vitamin B12 binding capacity does not increase to the same extent as TCI on fasting. Since this binder could be demonstrated in 50 different normal sera, it is clearly not a pathological binder, and should be called Transcobalamin III (TCIII).