Loss of a consensus heparin binding site by alternative splicing of latent transforming growth factor-beta binding protein-1.
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.
Oklü
R
R
Department of Biochemistry, Cambridge University, UK. ro212@mole.bio.cam.ac.uk
Metcalfe
J C
JC
Hesketh
T R
TR
Kemp
P R
PR
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D002352:Carrier Proteins / Q000235:genetics* / Q000378:metabolism; D016384:Consensus Sequence; D018076:DNA, Complementary; D005260:Female; D006493:Heparin / Q000378:metabolism*; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D053779:Latent TGF-beta Binding Proteins; D008969:Molecular Sequence Data; D051381:Rats; D012689:Sequence Homology, Nucleic Acid
D002352:Carrier Proteins; D018076:DNA, Complementary; D047908:Intracellular Signaling Peptides and Proteins; C509032:LTBP1 protein, human; D053779:Latent TGF-beta Binding Proteins; D006493:Heparin