VEGFB - Vascular Endothelial Growth Factor B | Elisa - Clia - Antibody - Protein

Background:

Vascular Endothelial Growth Factor B (VEGFB) is another member of the VEGF family of proteins, closely related to VEGFA. While both VEGFA and VEGFB are involved in regulating angiogenesis. VEGFB was initially discovered as a protein that binds to the same receptors as VEGFA, particularly VEGFR-1 (Flt-1). However, unlike VEGFA, VEGFB's role in promoting angiogenesis is less pronounced. Instead, VEGFB has been found to primarily influence the survival and function of endothelial cells, particularly in the context of cardiac and skeletal muscle vasculature. VEGFB plays a crucial role in cardiac and skeletal muscle metabolism and function. It promotes the survival of cardiomyocytes (heart muscle cells) and endothelial cells in the heart, which is essential for maintaining cardiac function and protecting against ischemic injury (injury due to inadequate blood supply). Additionally, VEGFB has been implicated in the regulation of fatty acid uptake and metabolism in skeletal muscle, which can impact muscle function and exercise capacity.

Protein Structure:

• Composition: VEGFB is a homodimeric glycoprotein.
• Isoforms: There are two main isoforms of VEGFB generated through alternative splicing: VEGFB167 and VEGFB186.
• Domains:
• Signal Peptide: Directs the protein to the secretory pathway.
• Receptor-Binding Domain: Essential for interaction with VEGF receptors.
• Heparin-Binding Domain: Present in VEGFB167, which allows it to bind to cell surface proteoglycans and extracellular matrix components.

Classification and Subtypes:

• Family: VEGFB is part of the VEGF family, which includes VEGFA, VEGFC, VEGFD, and placental growth factor (PlGF).
• Isoforms: VEGFB exists primarily in two isoforms, VEGFB167 and VEGFB186, differing in their binding properties and interactions with the extracellular matrix.

Function and Biological Significance:

• Cardiovascular Function: VEGFB is involved in the maintenance and function of the cardiovascular system, particularly in the coronary vasculature.
• Energy Metabolism: Recent studies suggest a role for VEGFB in the regulation of lipid metabolism and energy homeostasis.
• Angiogenesis: Unlike VEGFA, VEGFB is not a potent angiogenic factor but may have a role in maintaining the integrity and function of existing blood vessels.
• Neuroprotection: VEGFB has been implicated in neuroprotective roles, particularly in response to ischemic injury.
• Role in Disease: VEGFB is associated with several diseases, including cardiovascular disorders, metabolic syndromes, and neurodegenerative diseases.

Interactions:

• Receptors: VEGFB primarily binds to VEGFR-1 (Flt-1) and neuropilin-1 (NRP-1). These interactions are crucial for its biological functions.
• Proteoglycans: VEGFB167 can bind to heparan sulfate proteoglycans, which modulates its availability and activity in the extracellular matrix.

Clinical Issues:

• Cardiovascular Diseases: VEGFB is involved in the regulation of cardiac function and repair mechanisms post-myocardial infarction. Alterations in VEGFB signaling have been linked to heart diseases.
• Metabolic Disorders: VEGFB influences lipid uptake and storage, and dysregulation of VEGFB may contribute to metabolic syndromes such as obesity and type 2 diabetes.
• Neuroprotection: VEGFB's role in protecting neurons from ischemic damage suggests potential therapeutic applications in stroke and neurodegenerative diseases.
• Therapeutic Potential: While not as widely targeted as VEGFA, VEGFB is being investigated for its therapeutic potential in cardiovascular and metabolic diseases. Modulating VEGFB activity could provide new avenues for treatment.

Summary:

VEGFB (Vascular Endothelial Growth Factor B) is a member of the VEGF family, playing a key role in cardiovascular health and metabolic regulation. While not as potent in angiogenesis as VEGFA, VEGFB is essential for the maintenance of blood vessel function and integrity, particularly in the heart. It is involved in energy metabolism and has neuroprotective properties. VEGFB interacts primarily with VEGFR-1 and neuropilin-1, and its role in disease and therapeutic potential is increasingly being recognized, particularly in cardiovascular and metabolic disorders. Understanding VEGFB's functions and mechanisms offers valuable insights into its therapeutic applications and the development of new treatments.