Loss of a consensus heparin binding site by alternative splicing of latent transforming growth factor-beta binding protein-1

FEBS Lett. 1998 Mar 27;425(2):281-5. doi: 10.1016/s0014-5793(98)00257-9.

Abstract

Latent transforming growth factor-beta binding protein-1 (LTBP-1), plays an important role in controlling localisation and activation of transforming growth factor-beta (TGF-beta). We show that alternative splicing generates a form of mRNA which lacks bases 1277-1435 (termed LTBP-1delta53). The 53 amino acids encoded by these bases include the eighth cysteine of the first cysteine repeat and a consensus heparin binding sequence. Sequencing of genomic clones showed that alternative splicing resulted from the use of an intra-exonic 3' splice acceptor site. The loss of the heparin binding site implies that LTBP-1delta53 will bind to the extracellular matrix less efficiently than LTBP-1.

Publication types

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

MeSH terms

  • Alternative Splicing*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • Carrier Proteins / genetics*
  • Carrier Proteins / metabolism
  • Consensus Sequence*
  • DNA, Complementary
  • Female
  • Heparin / metabolism*
  • Humans
  • Intracellular Signaling Peptides and Proteins*
  • Latent TGF-beta Binding Proteins
  • Molecular Sequence Data
  • Rats
  • Sequence Homology, Nucleic Acid

Substances

  • Carrier Proteins
  • DNA, Complementary
  • Intracellular Signaling Peptides and Proteins
  • LTBP1 protein, human
  • Latent TGF-beta Binding Proteins
  • Heparin