Mikkel Holmen Andersen

TL;DR: Results show that lactadherin can act as link between two surfaces by binding to integrin receptors through its N-terminus and to phospholipids through its C- terminus, and mediation between artificial phosphatidyl serine membranes and MCF-7 cells.

TL;DR: Results obtained by amino acid analyses, amino-acid-sequence analyses, carbohydrate-composition determinations, and MS analyses of glycopeptides revealed that both proteins were glycosylated with a carbohydrate structure that contained galactose, N-acetylgalactosamine and fucose.

TL;DR: Results show that PAS-6/7 is a common protein which can bind to membranes by two distinct mechanisms, one through affinity to integrin alpha v beta 5 and another by direct binding to phospholipids.

TL;DR: A model system that allows analysis of the dynamics between IGF, IGFBP-4 and -5, the IGF receptor, and the proteolytic enzyme PAPP-A is established, and it is shown that cell surface-localized proteolysis of IGF BP-4 represents the final regulatory step of efficient IGF delivery to the receptor.

TL;DR: The highly glycosylated protein MUC1 was purified from bovine milk-fat globule membranes by a procedure involving detergent extraction, ion-exchange chromatography and reverse-phase chromatography, and monosaccharide composition determinations suggested significant structural differences between O-linked glycans of M UC1 originating from either bovines or human milk.