0000000000255619
AUTHOR
Dietmar Vestweber
showing 8 related works from this author
Vom E-Selektin-Liganden 1 abgeleitete Glycopeptide mit variierter Sialyl-Lewisx-Struktur als Zelladhäsionsinhibitoren für E-Selektin
2007
Synthetic Glycopeptides from the E-Selectin Ligand 1 with Varied Sialyl Lewisx Structure as Cell-Adhesion Inhibitors of E-Selectin.
2007
A Novel Cervical Spinal Cord Window Preparation Allows for Two-Photon Imaging of T-Cell Interactions with the Cervical Spinal Cord Microvasculature d…
2017
T-cell migration across the blood-brain barrier (BBB) is a crucial step in the pathogenesis of experimental autoimmune encephalomyelitis (EAE), an animal model of multiple scle rosis (MS). Two-photon intravital microscopy (2P-IVM) has been established as a powerful tool to study cell-cell interactions in inflammatory EAE lesions in living animals. In EAE, central nervous system inflammation is strongly pronounced in the spinal cord, an organ in which 2P-IVM imaging is technically very challenging and has been limited to the lumbar spinal cord. Here, we describe a novel spinal cord window preparation allowing to use 2P-IVM to image immune cell interactions with the cervical spinal cord micro…
Synthetic Inhibitors of Cell Adhesion: A Glycopeptide from E-Selectin Ligand 1 (ESL-1) with the Arabino Sialyl Lewisx Structure
2001
Particularly selective methods are required for the synthesis of arabino sialyl Lewisx glycopeptides owing to the acid-labile β-arabinopyranoside bond. It is important for the inhibition of cell adhesion that the arabino sialyl Lewisx glycopeptide 1, which contains the Gly 672 -Asp 681 sequence of the E-selectin Ligand 1 (ESL-1), binds ten times more strongly than sialyl Lewisx to E-selectin, although it is monovalent and does not contain L-fucose, which is considered essential.
Sulfated and Non-Sulfated Glycopeptide Recognition Domains of P-Selectin Glycoprotein Ligand 1 and their Binding to P- and E-Selectin
2009
Total synthesis through block glycosylation and selective chemical O-sulfation of tyrosine residues yielded the glycopeptide recognition domain A (X=SO(3) (-)) of the P-selectin glycoprotein ligand 1, in which the terminal sialic acid of the complex hexasaccharide side chain was replaced by (S)-cyclohexyl lactic acid. In binding assays the O-sulfated structure A showed high affinity towards P-selectin, the non-sulfated towards E-selectin.
Sulfatierte und nicht sulfatierte Glycopeptid-Erkennungsdomänen des P-Selektin-Glycoprotein-Liganden 1 und ihre Bindung an P- und E-Selektin
2009
Totalsynthese via Blockglycosylierung und selektive chemische O-Sulfatierung von Tyrosinresten ergaben die Glycopeptid-Erkennungsregion A (X=SO3−) des P-Selektin-Glycoprotein-Liganden 1, in dem die terminale Sialinsaure der komplexen Hexasaccharid-Seitenkette durch (S)-Cyclohexylmilchsaure als Mimetikum ersetzt ist. In Bindungsassays zeigt die O-sulfatierte Form A hohe Affinitat zu P-Selektin, die nicht sulfatierte Form zu E-Selektin.