SDC2: Cell-cell and Cell-extracellular Matrix Interactions, Regulation of Cell Adhesion, Migration, Invasion and Survival
SDC2: Cell-cell and Cell-extracellular Matrix Interactions, Regulation of Cell Adhesion, Migration, Invasion and Survival
SDC2 (heparan sulfate proteoglycan 1, cell surface-associated) is a protein that is expressed in various cell types, including epithelial, endothelial, and pericytes. It is a member of the heparan sulfate proteoglycan (HSP) family, which is a group of extracellular matrix (ECM) proteins that play a crucial role in cell-cell and cell-extracellular matrix (ECM) interactions.
SDC2 is involved in several cellular processes, including cell adhesion, migration, and invasion. It has been shown to be involved in the regulation of cell-cell adhesion by interacting with cadherins, which are transmembrane proteins that play a central role in cell-cell adhesion.
In addition to its role in cell-cell adhesion, SDC2 is also involved in the regulation of cell migration and invasion. It has been shown to be involved in the migration of various cell types, including cancer cells, and has been shown to play a role in the invasive properties of these cells.
SDC2 is also involved in the regulation of cell survival and angiogenesis. It has been shown to be involved in the regulation of cell apoptosis, which is the process by which cells die as a result of various cellular stressors. It has also been shown to be involved in the regulation of cell proliferation and the Initiation of angiogenesis.
SDC2 is a glycoprotein that consists of two heavy chains and two light chains. The heavy chains contain four domains: a N-terminal domain, a transmembrane domain, and a C-terminal domain. The light chains contain one domain: a variable region and a C-terminal domain.
The N-terminal domain of SDC2 is rich in amino acids that are involved in the regulation of cell adhesion and migration. This includes the amino acids Asp212, Asp213, Asp214, Asp215, and Asp216, which are all involved in the regulation of cadherins.
The transmembrane domain of SDC2 is rich in amino acids that are involved in the regulation of cell migration and invasion. This includes the amino acids Asp217, Asp218, Asp219, and Asp220, which are all involved in the regulation of the actinin-associated protein 2 (ACP-2) and the f-actinin-associated protein (F-actinin), respectively.
The C-terminal domain of SDC2 is rich in amino acids that are involved in the regulation of cell survival and angiogenesis. This includes the amino acids Asp221, Asp222, Asp223, Asp224, and Asp225, which are all involved in the regulation of cell apoptosis, cell proliferation, and angiogenesis, respectively.
SDC2 has been shown to play a role in the development and progression of various diseases, including cancer. For example, it has been shown to be involved in the regulation of cell apoptosis in various cancer cells, including breast, lung, and colorectal cancer cells. It has also been shown to be involved in the regulation of cell proliferation in various cancer cells, including breast, lung, and colorectal cancer cells.
In addition to its role in cancer, SDC2 has also been shown to play a role in the regulation of normal cell function and development. For example, it has been shown to be involved in the regulation of cell adhesion and migration in various normal cell types, including endothelial and epithelial cells. It has also been shown to play a role in the regulation of cell survival and angiogenesis in various normal cell types
Protein Name: Syndecan 2
Functions: Cell surface proteoglycan which regulates dendritic arbor morphogenesis
More Common Targets
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