Linked Life Data

10677208

Source:http://linkedlifedata.com/resource/pubmed/id/10677208

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2000-3-13
pubmed:abstractText
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 niTN-5B1-4 (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. Sf9 cells mainly processed the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose, although hybrid and complex N-glycosylations were also detected. In High-Five cells, the peptide was found to be modified with a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides. Most glycans had one or two fucose residues bound through alpha1,3 and alpha1,6 linkages to the innermost GlcNAc. On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1596-603
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10677208-Amino Acid Sequence, pubmed-meshheading:10677208-Animals, pubmed-meshheading:10677208-Baculoviridae, pubmed-meshheading:10677208-Carbohydrate Conformation, pubmed-meshheading:10677208-Carrier Proteins, pubmed-meshheading:10677208-Cell Line, pubmed-meshheading:10677208-Chromatography, High Pressure Liquid, pubmed-meshheading:10677208-Conserved Sequence, pubmed-meshheading:10677208-Cysteine, pubmed-meshheading:10677208-Glycosylation, pubmed-meshheading:10677208-Humans, pubmed-meshheading:10677208-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:10677208-Latent TGF-beta Binding Proteins, pubmed-meshheading:10677208-Molecular Sequence Data, pubmed-meshheading:10677208-Oligosaccharides, pubmed-meshheading:10677208-Peptide Fragments, pubmed-meshheading:10677208-Polysaccharides, pubmed-meshheading:10677208-Protein Structure, Tertiary, pubmed-meshheading:10677208-Recombinant Fusion Proteins, pubmed-meshheading:10677208-Spectrometry, Mass, Matrix-Assisted Laser..., pubmed-meshheading:10677208-Spodoptera, pubmed-meshheading:10677208-Transforming Growth Factor beta
pubmed:year
2000
pubmed:articleTitle
Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
pubmed:affiliation
Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't