GROWTH FACTOR RECEPTORS

Growth factor receptors are transmembrane proteins that attach to particular growth factors and transmit the messages the factors are carrying to the intracellular environment.

A receptor that attaches to a growth factor is called a growth factor receptor. Cells’ growth factor receptors are the starting point of the signaling chain that leads to cell multiplication and differentiation. The first stage in activating the growth factor receptors, which instructs the cell to grow and/or divide, is the binding of growth factors, which are ligands to the receptor.

Hepatocyte Growth Factor (HGF) Receptors

Heparin-binding growth factors, which include hepatocyte growth factor (HGF), are a class of substances with angiogenic potential. Although HGF does not impact fibroblasts, it is secreted by fibroblasts and is a mitogenic substance for melanocytes, epithelial, and endothelial cells. The HGF tyrosine kinase receptor is encoded by the MET gene. The extracellular a-subunit and the transmembrane b-subunit, which are formed by post-translational proteolytic cleavage of a single-chain precursor molecule, disulphide link to create the mature receptor. Upon ligand attachment, the MET receptor undergoes dimerization, which activates it.

Vascular Endothelial Growth Factor (VEGF) Receptors

Vascular endothelial growth factor receptors (VEGF receptors) are growth factor receptors that have an intracellular region with a divided tyrosine-kinase domain, an extracellular region with seven immunoglobulin-like domains, and a single transmembrane region. While VEGFR1 is necessary for the migration of monocytes and macrophages as well as the recruitment of haematopoietic precursors, VEGFR2 and VEGFR3 are needed for the activities of vascular endothelial and lymph endothelial cells, respectively.

Platelet-Derived Growth Factor (PDGF) Receptors

The platelet-derived growth factor receptors (PDGF receptors), which are growth factor receptors, are cell surface receptors that are essential for controlling cell growth, differentiation, proliferation, and development as well as a variety of illnesses, including cancer. PDGF receptor comes in two different varieties: PDGF receptor and PDGF receptor. Due to fusion with various partner genes, constitutive activation of the PDGF receptor or PDGF receptor is observed in myeloid malignancies, and PDGF receptor activating variants are observed in gastrointestinal tumors (GISTs).

Fibroblast Growth Factor (FGF) Receptors

Fibroblast growth factor receptors (FGF receptors) are single-pass membrane proteins with three immunoglobulin-like domains (Ig 1, Ig 2, and Ig 3) in their N-terminal extracellular (EC) domains, one helix in their transmembrane (TM) domain, and a tyrosine kinase domain in their intracellular (IC) region.

Members of the growth factor receptor family, the FGF receptor activates intracellular signaling networks that closely control vital biological processes like cell division, survival, migration, and differentiation. It has been discovered that a variety of processes, such as aberrant expression, mutations, chromosomal rearrangements, and amplifications, contribute to the deregulation of FGF receptors in human cancer.

Insulin-Like Growth Factor (IGF) Receptors

The hormones insulin-like growth factor 1 (IGF-1) and insulin-like growth factor 2 (IGF-2) trigger the insulin-like growth factor receptor (IGF receptor), a cell surface receptor. It is now clear that higher IGF-1 and IGF-2 concentrations, hyperinsulinemia, and enhanced cell proliferation and transformation may all contribute to the development of tumors.

IGF receptors, which are growth factor receptors, have been linked to a number of malignancies, including lung, prostate, and breast cancers.

Epidermal Growth Factor (EGF) Receptors

ErbBs, a group of receptor tyrosine kinases that belong to the epidermal growth factor family, are crucial for controlling cell motility, differentiation, and proliferation. The ErbB receptors play both redundant and specialized roles in the maintenance of tissues in mature mammals and in the development of mammals. Many human illnesses, most notably cancer, are caused by a loss of control over the ErbB receptors.