GPR55

From WikiMD's Wellness Encyclopedia

GPR55 is a G protein-coupled receptor that in humans is encoded by the GPR55 gene. It is widely distributed throughout the body, with high expression levels in the adrenal gland, gastrointestinal tract, spleen, and endocrine glands. GPR55 has been implicated in a variety of physiological and pathological processes, including pain perception, bone development, and regulation of energy balance.

Function[edit | edit source]

GPR55 is activated by a variety of lipid ligands, including lysophosphatidylinositol (LPI) and various cannabinoids. Upon activation, it can stimulate several different intracellular signaling pathways, including those involving phospholipase C, calcium mobilization, and mitogen-activated protein kinases.

In the central nervous system, GPR55 has been implicated in the modulation of neuronal excitability and synaptic transmission. In the peripheral nervous system, it appears to play a role in the regulation of nociception and inflammation.

Clinical significance[edit | edit source]

Alterations in GPR55 signaling have been associated with a variety of diseases, including cancer, neurodegenerative diseases, and metabolic disorders. For example, overexpression of GPR55 has been observed in several types of cancer, including breast cancer, prostate cancer, and pancreatic cancer, and has been linked to increased cell proliferation and tumor growth.

In the context of neurodegenerative diseases, GPR55 has been implicated in the regulation of neuroinflammation and neuroprotection. In metabolic disorders, alterations in GPR55 signaling have been linked to abnormalities in glucose homeostasis and energy balance.

Research[edit | edit source]

Given its potential involvement in a variety of diseases, GPR55 is currently the subject of intense research. Several pharmacological agents that selectively target GPR55 are being developed and tested for their potential therapeutic effects.

File:GPR55.png
GPR55 is a G protein-coupled receptor that is activated by a variety of lipid ligands.

See also[edit | edit source]

References[edit | edit source]



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Contributors: Prab R. Tumpati, MD