A. Sonnenberg
University of Amsterdam
21 Papers
560 Citations
A. Sonnenberg is an academic researcher from University of Amsterdam. The author has contributed to research in topics: Integrin & Epidermolysis bullosa. The author has an hindex of 14, co-authored 21 publications.
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Papers
P-selectin mediates Ca(2+)-dependent adhesion of activated platelets to many different types of leukocytes: detection by flow cytometry.
TL;DR: It is demonstrated that the platelet activation antigen P-selectin4 (PADGEM protein? GMP-140,6 or CD627) plays a critical role in the interaction between platelets and both monocytes and neutrophils, which could be blocked by soluble P- Selectin protein and by antibodies against P- selectin.
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Antibody to integrin α6 subunit specifically inhibits cell-binding to laminin fragment 8
TL;DR: Adhesion to fragment E8 was with one exception completely inhibited by a monoclonal antibody to the α6 integrin subunit, indicating that VLA-6 or a related structure is the major cellular receptor for laminin.
163
Isolation of α6β1 integrins from platelets and adherent cells by affinity chromatography on mouse laminin fragment E8 and human laminin pepsin fragment
TL;DR: Results indicate that both α3β1 and α6β1 can act as receptors for human laminin and may interfere by steric hindrance.
86
Suppression of mouse melanoma metastasis by EA-1, a monoclonal antibody specific for alpha 6 integrins.
TL;DR: It is suggested that alpha 6 integrins play a dual role in the metastatic process, mediating the adhesion of tumor cells to the luminal surface of the endothelium and the adherence to laminin in the subendothelial extracellular matrix during extravasation.
84
Expression of Integrin α6β4 in Junctional Epidermolysis Bullosa
TL;DR: This study has investigated the expression of alpha 6 beta 4 in skin specimens of patients with junctional and dystrophic epidermolysis bullosa using immunofluorescent (IF) staining with five different monoclonal antibodies against the alpha 6 and beta 4 subunits, and found a split between the intra- and extracellular epitopes of the integrin alpha 6beta 4 receptor.
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