Tissue- and developmental stage-specific forms of a neural cell surface antigen linked to differences in glycosylation of a common polypeptide

EMBO J. 1982;1(10):1239-44. doi: 10.1002/j.1460-2075.1982.tb00019.x.

Abstract

We have previously identified a cell surface glycoprotein of the mouse nervous system named brain cell surface protein-2 (BSP-2). Here we report that this antigen is not a single, discrete entity, but a family of antigenically and structurally related molecules. Three components of 180, 140, and 120 K were characteristic for more mature nervous tissues. Adult cerebral cortex contained the 140-K and 120-K antigens, adult spinal cord only the 120-K, and dorsal root ganglia from young mice mainly the 180-K component. Very different forms of the antigen that migrated as a diffuse zone from 180-250-K in SDS-polyacrylamide gels were found in immature nervous tissues. A molecule different from the previous ones was found in a neuroblastoma line. Evidence is presented that the structural diversity of BSP-2 is due to differences in glycosylation. This result indicates that cell type- and developmental stage-specific glycoprotein patterns previously found in the nervous system may in part be due to different glycosylation of identical polypeptides. The finding that a neural cell surface protein may be glycosylated in different ways has important implications for the generation of cell surface specificity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aging
  • Animals
  • Antigens, Surface / analysis*
  • Brain / growth & development*
  • Cell Line
  • Cerebral Cortex / growth & development
  • Electrophoresis, Polyacrylamide Gel
  • Ganglia, Spinal / growth & development
  • Mice
  • Mice, Inbred C57BL
  • Molecular Weight
  • Neuroblastoma
  • Sialic Acids*
  • Spinal Cord / growth & development*

Substances

  • Antigens, Surface
  • Sialic Acids
  • neural cell surface antigen BSP-2