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  • Title: Efficient association of an amino-terminally extended form of human latent transforming growth factor-beta binding protein with the extracellular matrix.
    Author: Olofsson A, Ichijo H, Morén A, ten Dijke P, Miyazono K, Heldin CH.
    Journal: J Biol Chem; 1995 Dec 29; 270(52):31294-7. PubMed ID: 8537398.
    Abstract:
    Latent transforming growth factor-beta (TGF-beta) binding protein-1 (LTBP-1) is a component of the high molecular weight latent TGF-beta complex found in various cells, including human platelets. LTBP-1 is observed as different molecular sizes in different cell types, probably due to proteolytic processing and alternative splicing. We here report a novel form of human LTBP-1, which is longer in its NH2-terminal part (LTBP-1L). Northern hybridization analysis revealed that the LTBP-1L is derived from a 7.0-kilobase mRNA, whereas the originally reported shorter form (LTBP-1S) is derived from a 5.2-kilobase mRNA. Transfection of cDNA for LTBP-1L and -1S in COS cells revealed that LTBP-1L bound more efficiently to the extracellular matrix than did LTBP-1S. These results suggest that the different splice forms of LTBP-1 mediate different localization patterns of the latent TGF-beta complexes in vivo.
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