Biomaterial Database

Signal transduction by vascular endothelial growth factor receptors. 2012

Sina Koch, and Lena Claesson-Welsh

Uppsala University, Department of Immunology, Genetics and Pathology, Rudbeck Laboratory, 751 85 Uppsala, Sweden.

Vascular endothelial growth factors (VEGFs) are master regulators of vascular development and of blood and lymphatic vessel function during health and disease in the adult. It is therefore important to understand the mechanism of action of this family of five mammalian ligands, which act through three receptor tyrosine kinases (RTKs). In addition, coreceptors like neuropilins (NRPs) and integrins associate with the ligand/receptor signaling complex and modulate the output. Therapeutics to block several of the VEGF signaling components have been developed with the aim to halt blood vessel formation, angiogenesis, in diseases that involve tissue growth and inflammation, such as cancer. In this review, we outline the current information on VEGF signal transduction in relation to blood and lymphatic vessel biology.

UI	MeSH Term	Description	Entries
D009389	Neovascularization, Pathologic	A pathologic process consisting of the proliferation of blood vessels in abnormal tissues or in abnormal positions.	Angiogenesis, Pathologic,Angiogenesis, Pathological,Neovascularization, Pathological,Pathologic Angiogenesis,Pathologic Neovascularization,Pathological Angiogenesis,Pathological Neovascularization
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D015398	Signal Transduction	The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.	Cell Signaling,Receptor-Mediated Signal Transduction,Signal Pathways,Receptor Mediated Signal Transduction,Signal Transduction Pathways,Signal Transduction Systems,Pathway, Signal,Pathway, Signal Transduction,Pathways, Signal,Pathways, Signal Transduction,Receptor-Mediated Signal Transductions,Signal Pathway,Signal Transduction Pathway,Signal Transduction System,Signal Transduction, Receptor-Mediated,Signal Transductions,Signal Transductions, Receptor-Mediated,System, Signal Transduction,Systems, Signal Transduction,Transduction, Signal,Transductions, Signal
D016023	Integrins	A family of transmembrane glycoproteins (MEMBRANE GLYCOPROTEINS) consisting of noncovalent heterodimers. They interact with a wide variety of ligands including EXTRACELLULAR MATRIX PROTEINS; COMPLEMENT, and other cells, while their intracellular domains interact with the CYTOSKELETON. The integrins consist of at least three identified families: the cytoadhesin receptors (RECEPTORS, CYTOADHESIN), the leukocyte adhesion receptors (RECEPTORS, LEUKOCYTE ADHESION), and the VERY LATE ANTIGEN RECEPTORS. Each family contains a common beta-subunit (INTEGRIN BETA CHAINS) combined with one or more distinct alpha-subunits (INTEGRIN ALPHA CHAINS). These receptors participate in cell-matrix and cell-cell adhesion in many physiologically important processes, including embryological development; HEMOSTASIS; THROMBOSIS; WOUND HEALING; immune and nonimmune defense mechanisms; and oncogenic transformation.	Integrin
D018919	Neovascularization, Physiologic	The development of new BLOOD VESSELS during the restoration of BLOOD CIRCULATION during the healing process.	Angiogenesis, Physiologic,Angiogenesis, Physiological,Neovascularization, Physiological,Physiologic Angiogenesis,Physiologic Neovascularization,Physiological Angiogenesis,Physiological Neovascularization
D020794	Receptor Protein-Tyrosine Kinases	A class of cellular receptors that have an intrinsic PROTEIN-TYROSINE KINASE activity.	PTK Receptor,Receptors, Protein-Tyrosine Kinase,Tyrosine Kinase Linked Receptor,Tyrosine Kinase Linked Receptors,Tyrosine Kinase Receptor,Tyrosine Kinase Receptors,PTK Receptors,Protein-Tyrosine Kinase Receptor,Receptor Protein-Tyrosine Kinase,Kinase Receptor, Tyrosine,Kinase, Receptor Protein-Tyrosine,Kinases, Receptor Protein-Tyrosine,Protein-Tyrosine Kinase Receptors,Protein-Tyrosine Kinase, Receptor,Protein-Tyrosine Kinases, Receptor,Receptor Protein Tyrosine Kinase,Receptor Protein Tyrosine Kinases,Receptor, PTK,Receptor, Protein-Tyrosine Kinase,Receptor, Tyrosine Kinase,Receptors, PTK,Receptors, Protein Tyrosine Kinase
D039921	Neuropilins	Neuropilins are 140-kDa vertebrate cell surface receptors that bind neuronal guidance molecules during neural development and axonal outgrowth, and modulate VEGF-mediated angiogenesis. NEUROPILIN-1 and NEUROPILIN-2 differ in their binding specificities, and are distributed complementarily in regions of the developing nervous system. Neuropilins are receptors for secreted CLASS 3 SEMAPHORINS as well as for vascular endothelial growth factors, and may form hetero- or homodimers. They may also interact synergistically with plexins and with VEGF RECEPTORS to form receptor complexes with distinct affinities and specificities. Neuropilin binding specificity is determined by CUB and coagulation-factor-like domains in the extracellular portion of the molecule, while a MAM domain is essential for SIGNAL TRANSDUCTION.	Neuropilin
D040262	Receptors, Vascular Endothelial Growth Factor	A family of closely related RECEPTOR PROTEIN-TYROSINE KINASES that bind vascular endothelial growth factors. They share a cluster of seven extracellular IG-LIKE DOMAINS which are important for ligand binding. They are highly expressed in vascular endothelial cells and are critical for the physiological and pathological growth, development and maintenance of blood and lymphatic vessels.	Endothelial Growth Factor Receptor,Receptor, Endothelial Growth Factors,Receptor, Vascular Endothelial Cell Growth Factor,Receptor, Vascular Permeability Factor,VEGF Receptor,VEGF Receptors,VPF Receptor,Vascular Endothelial Cell Growth Factor Receptor,Vascular Endothelial Growth Factor Receptor,Vascular Permeability Factor Receptor,Receptors, VEGF
D040281	Vascular Endothelial Growth Factor Receptor-1	A 180-kDa VEGF receptor found primarily in endothelial cells that is essential for vasculogenesis and vascular maintenance. It is also known as Flt-1 (fms-like tyrosine kinase receptor-1). A soluble, alternatively spliced isoform of the receptor may serve as a binding protein that regulates the availability of various ligands for VEGF receptor binding and signal transduction.	VEGFR-1,FLT1 RTK,FLT1 Receptor Tyrosine Kinase,Proto-Oncogene Protein flt,VEGF Receptor flt-1 Protein,VEGF Receptor, FLT,fms-Like Tyrosine Kinase,FLT VEGF Receptor,Proto Oncogene Protein flt,Receptor, FLT VEGF,Tyrosine Kinase, fms-Like,VEGF Receptor flt 1 Protein,Vascular Endothelial Growth Factor Receptor 1