The primary structure of a cell-binding bone sialoprotein

J Biol Chem. 1988 Dec 25;263(36):19430-2.

Abstract

We have determined the amino acid sequence of rat bone sialoprotein (BSP). The sequence deduced from a 1974-base pair cDNA encodes a protein of 320 residues, including a 16-residues long signal peptide. The mature BSP has a molecular mass of 33,600 and contains predominantly glutamic acid and glycine residues, which constitute 32% of all residues. The glutamic acid residues are typically distributed in clusters of up to 10 consecutive residues. The tissue distribution of BSP mRNA suggests that the protein may be a unique product of cells in bone tissue. BSP contains an Arg-Gly-Asp sequence, which presumably is responsible for its cell binding properties (Oldberg, A., Franzén, A., Heinegård, D., Pierschbacher, M., and Ruoslahti, E. (1988) J. Biol. Chem. 263, 19433-19436).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Animals, Newborn
  • Base Sequence
  • Bone and Bones / metabolism*
  • DNA / genetics
  • Integrin-Binding Sialoprotein
  • Molecular Sequence Data
  • Protein Binding
  • RNA, Messenger / genetics
  • RNA, Messenger / isolation & purification
  • Rats
  • Sialoglycoproteins / genetics*

Substances

  • Ibsp protein, rat
  • Integrin-Binding Sialoprotein
  • RNA, Messenger
  • Sialoglycoproteins
  • DNA

Associated data

  • GENBANK/J04215