Protease-activated receptor

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coagulation factor II thrombin receptor
Identifiers
SymbolF2R
Alt. symbolsTR; HTR; CF2R; PAR1; PAR-1
Chr. 5 q13.3
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StructuresSwiss-model
DomainsInterPro
F2R like trypsin receptor 1
Identifiers
SymbolF2RL1
Alt. symbolsPAR2, GPR11
Chr. 5 q13.3
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StructuresSwiss-model
DomainsInterPro
coagulation factor II thrombin receptor like 2
Identifiers
SymbolF2RL2
Alt. symbolsPAR3; PAR-3
Chr. 5 q13.3
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StructuresSwiss-model
DomainsInterPro
F2R like thrombin or trypsin receptor 3
Identifiers
SymbolF2RL3
Alt. symbolsPAR4
Chr. 19 p13.11
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Protease-activated receptors (PAR) are a subfamily of related

myocytes, neurons, and tissues that line the gastrointestinal tract.[1]

Protease-activated receptors, or PARs, are not to be mistaken with PAR proteins, a group of regulators of cellular polarity[2] named after their associated partitioning phenotype.[3]

Classification

There are four mammalian members of the protease-activated receptor (PAR) family:

G-protein-coupled receptor superfamily, and are expressed throughout the body.[4]

History

When scientists were researching the process of blood clotting in the late 1980s, they made the discovery of protease-activated receptors (PARs). A novel protein that was activated by thrombin, a crucial part of the clotting cascade, was discovered by a research team at the University of California, San Francisco in 1991. The team was directed by Shaun Coughlin. This protein, which was eventually given the designation protease-activated receptor 1 (PAR1), was the first to be recognized as a member of the PAR family.

A second thrombin-activated protein, later known as PAR3, was identified in 1994. Later research revealed that PAR3 works as a cofactor for PAR4 but lacks a useful intracellular domain. A third member of the PAR family, known as PAR2, was discovered as a protein triggered by in 1996.

Activation

Signal transduction by activation of PAR

Protease activated receptors are integral

TFF3 isolated from human breast milk activates PAR-2 receptors of intestinal epithelial cells HT-29. These findings suggest that TFF3 activates intestinal epithelial cells through G-protein-coupled PAR-2, and could actively participate in the immune system of breastfed babies inducing the production of peptides related to innate defense, such as defensins and cytokines.[5]

PARs are activated by the action of

enzymes cleave the N-terminus of the receptor, which in turn acts as a tethered ligand. In the cleaved state, part of the receptor itself acts as the agonist
, causing a physiological response.

Most of the PAR family act through the actions of

q
(calcium signalling) to cause cellular actions.

Function

PARs play a role in a multitude of physiological processes such as hemostasis, thrombosis, inflammation, and pain sensation. The cellular effects of thrombin are mediated by protease-activated receptors (PARs). Endothelial PARs participate in the regulation of vascular tone and permeability while in vascular smooth muscle they mediate contraction, proliferation, and

intercellular adhesion molecule-1 or ICAM-1, and E-selectin).[7] PARs contribute to the pro-inflammatory response. For example PAR4 induces leukocyte migration and PAR2 helps macrophages to produce cytokines such as interleukin-8 (IL-8). Recent research has also implicated these novel receptors in muscle growth and bone cell differentiation and proliferation.[4]

See also

References

  1. PMID 11356985
    .
  2. PMID 16364625
    .
  3. PMID 17981131
    .
  4. ^
    PMID 30976204
    .
  5. ^
    PMID 27546365
    .
  6. PMID 30610085
    .
  7. PMID 19277413
    .

Further reading

External links
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