- ADIPOR1 (adiponectin receptor 1)
[ACDCR1, CGI-45, CGI45, FLJ25385, FLJ42464, PAQR1, TESBP1A]
The adiponectin receptors, ADIPOR1 and ADIPOR2 mediate elevated AMPK and PPAR-alpha ligand activities, as well as fatty acid oxidation and glucose uptake by adiponectin (OMIM, 2010). In patients with chronic hepatitis C (HCV), adiponectin was found to be linked to steatosis only in males and was increased with inflammation (Jonsson et al., 2005). The hepatic mRNA expression of the adiponectin receptors AdipoR1 and AdipoR2 showed opposite correlations with phosphoenolpyruvate carboxykinase (PEPCK) gene expression.
Related disease:
chronic hepatitis C (HCV)
Reference:
Jonsson, J. R., Moschen, A. R., et al. (2005) Adiponectin and its receptors in patients with chronic hepatitis C. J Hepatol 43, 929-936.
- ADIPOR2 (adiponectin receptor 2)
[ACDCR2, FLJ21432, MGC4640, PAQR2]
The adiponectin receptors, ADIPOR1 and ADIPOR2 mediate elevated AMPK and PPAR-alpha ligand activities, as well as fatty acid oxidation and glucose uptake by adiponectin (OMIM, 2010). In patients with chronic hepatitis C (HCV), adiponectin was found to be linked to steatosis only in males and was increased with inflammation (Jonsson et al., 2005). The hepatic mRNA expression of the adiponectin receptors AdipoR1 and AdipoR2 showed opposite correlations with phosphoenolpyruvate carboxykinase (PEPCK) gene expression.
Related disease:
chronic hepatitis C (HCV)
Reference:
Jonsson, J. R., Moschen, A. R., et al. (2005) Adiponectin and its receptors in patients with chronic hepatitis C. J Hepatol 43, 929-936.
- ADM (adrenomedullin)
[AM]
Adrenomedullin (AM) is a potent vasodepressor that has anti-atherosclerotic and anti-inflammatory effects. In patients with chronic heart failure (CHF), strong association was found between C-terminal-pro endothelin-1 (ET-1) and midregional-pro- Adrenomedullin (ADM) levels with inflammation (Gombos et al., 2009). The peptide has protective cardiovascular effects such as protection of the microcirculation during inflammation (Temmesfeld-Wollbruck et al., 2007). It has been found to be an efficient counter-regulatory molecule in models of sepsis and septic shock. AM may be a potential molecule to treat cardiovascular malfunction during severe infection. In patients with peripheral arterial occlusive disease (PAOD), the plasma AM concentration was increased in proportion to the severity of the disease and linked to vascular inflammation (Suzuki et al., 2004).
With the exposure of human gastric epithelial cells to Helicobacter pylori, Escherichia coli, Salmonella enterica, or Streptococcus bovis, adrenomedullin gene expression was increased in response to these microorganisms (Allaker and Kapas, 2003). Its level was also elevated when the cells were exposed to proinflammatory cytokines such as interleukin 1 alpha (IL-1 alpha), IL-6, tumor necrosis factor alpha and lipopolysaccharide. Epithelial infection, inflammation, and adrenomedullin expression are strongly associated.
Related diseases:
cardiovascular disease, chronic heart failure (CHF), peripheral arterial occlusive disease (PAOD), sepsis, septic shock, microbial and infectious diseases
References:
Allaker, R. P. and Kapas, S. (2003) Adrenomedullin expression by gastric epithelial cells in response to infection. Clin Diagn Lab Immunol 10, 546-551.
Gombos, T., Forhecz, Z., et al. (2009) Adrenomedullin and endothelin-1 are related to inflammation in chronic heart failure. Inflamm Res 58, 298-305.
Suzuki, Y., Horio, T., et al. (2004) Plasma adrenomedullin concentration is increased in patients with peripheral arterial occlusive disease associated with vascular inflammation. Regul Pept 118, 99-104.
Temmesfeld-Wollbruck, B., Hocke, A. C., et al. (2007) Adrenomedullin and endothelial barrier function. Thromb Haemost 98, 944-951.
- ADORA2A (adenosine A2a receptor)
[ADORA2, RDC8, hA2aR]
It is a member of the G-protein coupled receptor family. It is abundant in basal ganglia, vasculature and platelets (RefSeq, 2010) A molecular pathway in mouse and human microglia was found to convert ATP-driven process extension into process retraction during inflammation (Orr et al., 2009). This chemotactic reversal was driven by increased levels of the A(2A) adenosine receptor with decreased levels of P2Y(12). A breakdown product of extracellular ATP adenosine stimulates A(2A) receptor and activates microglia to have amoeboid morphology during brain inflammation.
Related diseases:
Brain injuries and diseases
Reference:
Orr, A. G., Orr, A. L., et al. (2009) Adenosine A(2A) receptor mediates microglial process retraction. Nat Neurosci 12, 872-878.
