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

Rahmi Öklü, James C. Metcalfe, T. Robin Hesketh, Paul R. Kemp

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

Latent transforming growth factor-β binding protein-1 (LTBP-1), plays an important role in controlling localisation and activation of transforming growth factor-β (TGF-β). We show that alternative splicing generates a form of mRNA,which lacks bases 1277-1435 (termed LTBP-1Δ53). 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-1Δ53 will bind to the extracellular matrix less efficiently than LTBP-1.

Original languageEnglish (US)
Pages (from-to)281-285
Number of pages5
JournalFEBS Letters
Volume425
Issue number2
DOIs
StatePublished - Mar 27 1998

Keywords

  • Alternative splicing
  • Cysteine rich repeat
  • Heparin binding
  • Latent transforming growth factor-β binding protein

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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