A5003411082- Angiogenesis and VEGF in Cancer
- Cell Adhesion Molecules Research
- Cancer, Hypoxia, and Metabolism
- Axon Guidance and Neuronal Signaling
- Protein Kinase Regulation and GTPase Signaling
- Fibroblast Growth Factor Research
- Lymphatic System and Diseases
- Proteoglycans and glycosaminoglycans research
- Kruppel-like factors research
- PI3K/AKT/mTOR signaling in cancer
- Glycosylation and Glycoproteins Research
- Platelet Disorders and Treatments
- Protease and Inhibitor Mechanisms
- Monoclonal and Polyclonal Antibodies Research
- Protein Tyrosine Phosphatases
- Congenital heart defects research
- Hippo pathway signaling and YAP/TAZ
- Zebrafish Biomedical Research Applications
- Nitric Oxide and Endothelin Effects
- Retinal Diseases and Treatments
- Receptor Mechanisms and Signaling
- Barrier Structure and Function Studies
- TGF-β signaling in diseases
- Apelin-related biomedical research
- Atherosclerosis and Cardiovascular Diseases
Science for Life Laboratory
2016-2025
Uppsala University
2016-2025
Royal Swedish Academy of Sciences
2016
Harvard University
2010-2014
University of Helsinki
1991-2014
Wihuri Research Institute
2014
Eli Lilly (United States)
2014
Boston Children's Hospital
2014
RWTH Aachen University
2012
KU Leuven
2012
Vascular endothelial growth factor (VEGF) is a homodimeric peptide which binds to two structurally related tyrosine kinase receptors denoted Flt1 and KDR. In order compare the signal transduction via these receptors, human KDR proteins were stably expressed in porcine aortic cells. Binding analyses using 125I-VEGF revealed Kd values of 16 pM for 760 Cultured umbilical vein (HUVE) cells found express distinct populations binding sites with affinities similar those KDR, respectively. The...
Vascular endothelial growth factor C (VEGF-C) recently has been described to be a relatively specific for the lymphatic vascular system. Here we report that ectopic application of recombinant VEGF-C also potent angiogenic effects in vivo . is sufficiently stimulate neovascularization from limbal vessels mouse cornea. Similar VEGF, response corneas induced by intensive, with high density new capillaries. However, outgrowth microvessels stimulated was significantly longer than VEGF. In...
The primary structure of the human A-type receptor for platelet-derived growth factor (PDGF) has been determined. A 6.5-kilobase (kb) transcript was identified through low-stringency hybridization with a probe derived from B-type PDGF cDNA. sequence cDNA clone corresponding to 6.5-kb contains an open reading frame that predicts 1089-amino acid receptor-like molecule, which displays 44% overall amino similarity receptor. two receptors have similar domain organization, five immunoglobulin-like...