adiponectin

(redirected from ACRP30)
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Related to ACRP30: Resistin

ad·i·po·nec·tin

(ad'i-pō-nek'tin),
Protein hormone produced and secreted by adipocytes into the systemic blood circulation; causes sensitivity of peripheral tissues to insulin.
[adipo- + L. necto, to fasten, + -in]

adiponectin

(ăd′ə-pə-nĕk′tĭn)
n.
A polypeptide hormone that is secreted by fat cells and regulates glucose and lipid metabolism, especially by increasing insulin sensitivity and muscle uptake of glucose and by decreasing glucose production in the liver.

Adiponectin

A circulating protein encoded by ADIPOQ on chromosome 3q27, which is secreted exclusively by mature adipocytes. It is a key adipokine in the control of fat metabolism and insulin sensitivity, and has direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. It stimulates AMPK phosphorylation and activation in the liver and skeletal muscle, enhancing glucose utilisation and fatty acid hydrolysis. It antagonises TNF-alpha by down-regulating its expression in the liver, macrophages and elsewhere, and by counteracting its direct effects. It inhibits endothelial NF-kappa-B signalling by a cAMP-dependent pathway. It may play a role in cell growth, angiogenesis and tissue remodelling by binding and sequestering various growth factors with distinct binding affinities, depending on complex size—low, medium, or high molecular weight.

ad·i·po·nec·tin

(ad'i-pō-nek'tin)
Protective adipokine that reduces lipid accumulation and endothelial adhesion resulting from vascular injury; increases skeletal muscle oxidation of free fatty acids; reduces hepatic glucose output; increases peripheral insulin sensitivity.
[adipo- + L. necto, to fasten, + -in]

adiponectin

A cytokine derived from adipose tissue that has antidiabetic and antiatherosclerotic properties.
References in periodicals archive ?
Hence, all aspects put to consideration; there is accumulating evidence that Acrp30 serves multiple roles in striking the balance between glucose homeostasis/regulation and metabolic abnormalities both in normal and diseased states.
Receptors that serve to mediate effects of Acrp30 comprise AdipoRl and R2 [29,30].
More importantly, wide ranging post-translational modification which entails hydroxylation and glycolysation is critical for Acrp30 assembly and subsequent formation of functional oligomeric complexes [34-37].
Normally, the circulating levels of Acrp30 show reciprocal relationship with the proportion of body fat composition [48].
For instance, decreased systemic Acrp30 levels that is experienced among obese subjects despite a high mass of adipose tissue is a driver for metabolic syndrome that is often characterized by dyslipidaemia, atherosclerosis, cardiovascular disease, endothelial dysfunction, insulin resistance (Type 2 diabetes) among others [10,53].
Immunologically, the inflammatory responses, more specifically a T helper-1 (Th-1) mediated pro-inflammatory milieu by tumor necrosis factor-alpha (TNF-[alpha]), is identified as a primary cause of suppressed Acrp30 expression in obese/diabetic subjects [54-56].
However, Acrp30 levels become increased and localize within injured vascular walls as opposed to intact vessels which functions to suppress macrophage-to-foam cell transformation thereby regulating/inhibiting plaque build-up and resultant atherosclerosis [60,61].
Decreased Acrp30 secretion (hypo-adiponectinaemia) in obesity has been implicated with promotion of insulin resistance [62]; however, the underlying mechanisms modulating Acrp30 activity on insulin metabolism have not been well elucidated.
As such, Acrp30 fails to maintain its inverse relationship with body fat mass during incidences of HIV infection [68], possibly due to adipocyte dysfunction resulting from the effects of HIV virus [69,70].
Human immunodeficiency virus infected individuals on HAART are reported to exhibit markedly reduced Acrp30 levels compared to uninfected persons [73,74].
Endogenous glucose production is inhibited by the adiposederived protein Acrp30. J.
The adipocytesecreted protein Acrp30 enhances hepatic insulin action.