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Summary Chondroitin 4-sulfate proteoglycan (C4S-PG) was localized both in rat and human central nervous system (CNS) by monoclonal and polyclonal antisera recognizing the 4-sulfate disaccharide (C4S). In the rat the whole CNS was studied in serial coronal sections. A positive extracellular meshwork was observed both in white and grey matters. In the white matter (WM) C4S-PG formed a network around myelinated axons, sparing myelin sheaths and axoplasms. The neuropil of the grey matter (GM) showed a positive meshwork constituted by delicate intermingling filaments. The cytoplasms of neuronal, glial and endothelial cells were negative. Stronger straining than in the neuropil was observed around the soma and the proximal part of the cell processes of some neurons located in the cortex, in the deep cerebellar nuclei and in some other CNS nuclei. A similar pattern was also observed in human CNS, the only difference being a smaller amount of cortical neurons surrounded by a rim of C4S-PG. This study shows that a PG bearing C4S disaccharide is located extracellularly in the rodent and human CNS and that C4S disaccarides can be present in different types of CNS proteoglycans (PGs).

The availability of antisera against collagen and non-collagen proteins of the extracellular matrix has opened new possibilities of studying fibrous infiltration in muscular diseases. We have examined muscle biopsies from 5 controls and 27 patients with various neuromuscular diseases by immunofluorescence and peroxidase—anti-peroxidase. We investigated the distribution of fibronectin and of laminin, a protein present in basement membranes. In normal muscle both were present around blood vessels, axons, muscle spindles and muscle fibres. In addition fibronectin filled the endomysial and perimysial space, the endoneurium and the space between the intrafusal fibres. In pathological muscle laminin distribution was similar to that in normal muscle, but some atrophic fibres appeared to have a thickened contour and irregular profiles were occasionally observed in the absence of histologically demonstrable muscle fibres. Fibronectin was increased in all the conditions with thickened endomysium and perimysium, without displaying any disease-specific character. Findings are compared with the few published observations on fibronectin and collagen types.

The two-dimensional immunoelectrophoresis on cellulose acetate, already utilized for serum proteins, has been applied to CSF proteins. The technical modifications which allow the use of unconcentrated CSF are described. By utilizing a particularly suitable supporting medium, a good separation of proteins is achieved; consequently narrow-based peaks are obtained and the isoantigens can be displayed as distinct components in spite of closely similar migration velocities. The preliminary results of this method are given. Particulary interesting appears a beta-migrating protein and the gamma-migrating oligoclonal bands. The first may present an anodic cleavage suggesting that it may be the beta1C/beta1A-globulin. If this hypothesis is confirmed, the relative concentrations of the two components can be investigated. No clear-cut peaks corresponding to the gamma-migrating oligoclonal bands have been observed, their place being taken by a low precipitation line continuous with the IgG peak. The reasons for this phenomenon may be tentatively ascribed to a local specificity of these IgG.