WATER-SOLUBLE AND PENTANOL-EXTRACTABLE PROTEINS IN HUMAN BRAIN NORMAL TISSUE AND HUMAN BRAIN TUMOURS, WITH SPECIAL REFERENCE TO S-100 PROTEIN

Authors

  • K. G. Haglid,

    1. Institute of Neurobiology, Medical Faculty, University of Göteborg, Göteborg, Sweden and Institut für Allgemeine Pathologie und Neuropathologie der Tierärztlichen Fakultät der Universität München, BRD
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  • D. Stavrou

    1. Institute of Neurobiology, Medical Faculty, University of Göteborg, Göteborg, Sweden and Institut für Allgemeine Pathologie und Neuropathologie der Tierärztlichen Fakultät der Universität München, BRD
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  • This work was supported by Riksföreningen mot Cancer, grant No. 72-96, and Göteborgs Läkarsällskap and Collianders Stiftelse and Deutsche Forschungsgeneinschaft (SFB 51). The authors are indebted to Professors Holger Hydén, Gösta Norlén and Erwin Dahme and Dr. Galo Ramirez for their interest and encouragement, and to Mrs. Anita Palm for skillful technical assistance. The authors are also indebted to Dr. Pietro Calissano, under whose guidance one of the authors isolated one of the batches of S-100 used, and also for the initiation of the study of pentanol-extractable proteins from the different tissues. We are grateful to Dr. C.-A. Carlsson for his help in supplying tumour material and to Dr. Hengo Haljamäe for Ca2+ determinations.

Abstract

Disc electrophoretic separation of water-soluble and pentanol-extractable protein from normal human brain and human brain tumours (glioblastoma, neurinoma and medulloblastoma) on 10 per cent polyacrylamide gels showed minor differences between tissues. After disc electrophoresis ependymomal tumour cells contained high concentrations of a rapidly migrating anodic protein fraction which was immunologically distinct from S-100 protein. After electrophoresis of normal brain grey matter in a continuous buffer system, a rapidly migrating anodic protein fraction which was immunologically distinct from S-100 protein was found, and this protein fraction had a similar relative mobility to that of ependymomal tumour cells. This protein fraction was present to a low extent in human normal white matter, but absent from neurinoma and glioblastoma.

In a continuous buffer system at least two separable protein fractions, immunologically equivalent to S-100 protein, were observed in normal human brain. The more anodic of these two fractions was shown to be present in relatively high amounts in neurinomas, and may be of Schwann cell origin. Additional S-100 protein could be extracted from residual material remaining after removal of water-soluble proteins; 2.8-10 per cent of the water-soluble S-100 in normal material, and 0.1-0.6 per cent of that present in tumour material, was extractable from the water-insoluble residue by pentanol.

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