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Loss of a consensus heparin binding site by alternative splicing of latent transforming growth factor‐β binding protein‐1
Author(s) -
Öklü Rahmi,
Metcalfe James C,
Hesketh T.Robin,
Kemp Paul R
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00257-9
Subject(s) - rna splicing , consensus sequence , alternative splicing , binding site , splicing factor , protein splicing , transforming growth factor , cysteine , sequence (biology) , biology , peptide sequence , biochemistry , computational biology , chemistry , microbiology and biotechnology , messenger rna , gene , rna , enzyme
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.