Enhancing integrin function by VEGF/neuropilin signaling: implications for tumor biology.
This review advances the hypothesis that the ability of integrins to engage their extracellular matrix ligands and signal can be regulated in tumor cells by vascular endothelial growth factor (VEGF), a major angiogenic factor that also has direct effects on the function of tumor cells. More specifically, we will discuss how neuropilins (NRPs), a distinct class of VEGF receptors, enable the function of specific integrins that contribute to tumor initiation and progression.
Department of Cancer Biology University of Massachusetts Medical School Worcester, MA, USA.
Hira Lal
HL
Goel
Arthur M
AM
Mercurio
D002471:Cell Transformation, Neoplastic / Q000235:genetics / Q000378:metabolism / Q000473:pathology*; D018450:Disease Progression; D004789:Enzyme Activation; D005109:Extracellular Matrix / Q000378:metabolism / Q000473:pathology; D051417:Focal Adhesion Kinase 1 / Q000235:genetics / Q000378:metabolism; D022001:Focal Adhesions / Q000378:metabolism; D006801:Humans; D039121:Integrin alpha6beta1 / Q000235:genetics / Q000378:metabolism*; D008024:Ligands; D009389:Neovascularization, Pathologic / Q000378:metabolism / Q000473:pathology*; D039943:Neuropilin-2 / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D025941:Protein Interaction Mapping; D015398:Signal Transduction; D059016:Tumor Microenvironment; D042461:Vascular Endothelial Growth Factor A / Q000235:genetics / Q000378:metabolism*
D039121:Integrin alpha6beta1; D008024:Ligands; D039943:Neuropilin-2; C467484:VEGFA protein, human; D042461:Vascular Endothelial Growth Factor A; C581308:neuropilin-2, human; D051417:Focal Adhesion Kinase 1; C496050:PTK2 protein, human