Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain

Nature. 1986 Oct;323(6087):455-8. doi: 10.1038/323455a0.


Gelsolin is representative of a class of actin-modulating proteins found in lower eukaryotes to mammals, which sever actin filaments. Gelsolin found in the cytoplasm of cells is functionally similar to a mammalian plasma protein of similar size, originally called ADF or brevin. Human plasma and rabbit macrophage gelsolins differ by the presence of a 25-amino-acid residue extension on plasma gelsolin which appears to account for the difference in relative molecular mass (Mr) between the proteins as assessed by SDS-polyacrylamide gel electrophoresis (PAGE), 93,000 (93K) and 90K, respectively. Here we report the isolation of full-length human plasma gelsolin complementary DNA clones from a HepG2 library. The inferred amino-acid sequence reveals the presence of a signal peptide, a long tandem repeat that matches the actin-binding domains of gelsolin, a tetrapeptide present in actin and extended regions of identical sequence with rabbit macrophage gelsolin. Southern blot analysis indicates that a single gene in the haploid genome encodes both protein forms.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Calcium-Binding Proteins / blood
  • Calcium-Binding Proteins / genetics*
  • Cytoplasm / metabolism
  • DNA
  • Gelsolin
  • Genes
  • Humans
  • Microfilament Proteins / blood
  • Microfilament Proteins / genetics*
  • Repetitive Sequences, Nucleic Acid
  • Sequence Homology, Nucleic Acid


  • Calcium-Binding Proteins
  • Gelsolin
  • Microfilament Proteins
  • DNA

Associated data

  • GENBANK/X04412