Partenaires

CNRS


Rechercher


Accueil > Publications > Recherche par années > Années 2000 > 2000

Rudd, PM ; Downing, AK ; Cadene, M ; Harvey, DJ ; Wormald, MR ; Weir, I ; Dwek, RA ; Rifkin, DB ; Gleizes, PE

Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells

Biochemistry 39 (7) 1596-1603

par Administrateur - publié le

Abstract :

Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta is mediated by the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3. Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia ni TN-SB 1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3. CR3 contains an N-glycosylation site, which is conserved in all forms of LTBP known to date. When we examined the status of this N-glycosylation using MALDI-TOF mass spectrometry and enzymatic analysis, we found that CR3 is one of the rare recombinant peptides modified with complex glycans in insect cells.