| Post Translational Modifications | HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagen-like domain of adiponectin seem to be critically involved in regulating the formation and/or secretion of HMW complexes and consequently contribute to the insulin-sensitizing activity of adiponectin in hepatocytes. O-glycosylated. Not N-glycosylated. O-linked glycans on hydroxylysines consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. Sialylated to varying degrees depending on tissue. Thr-22 appears to be the major site of sialylation. Higher sialylation found in SGBS adipocytes than in HEK fibroblasts. Sialylation is not required neither for heterodimerization nor for secretion. Not sialylated on the glycosylated hydroxylysines. Desialylated forms are rapidly cleared from the circulation. Succination of Cys-36 by the Krebs cycle intermediate fumarate, which leads to S-(2-succinyl)cysteine residues, inhibits polymerization and secretion of adiponectin. Adiponectin is a major target for succination in both adipocytes and adipose tissue of diabetic mammals. It was proposed that succination of proteins is a biomarker of mitochondrial stress and accumulation of Krebs cycle intermediates in adipose tissue in diabetes and that succination of adiponectin may contribute to the decrease in plasma adiponectin in diabetes. |
| Function | Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW. |
| Protein Name | Adiponectin30 Kda Adipocyte Complement-Related ProteinAdipocyte Complement-Related 30 Kda ProteinAcrp30Adipocyte - C1q And Collagen Domain-Containing ProteinAdipose Most Abundant Gene Transcript 1 ProteinApm-1Gelatin-Binding Protein |
| Database Links | Reactome: R-HSA-163680Reactome: R-HSA-381340 |
| Cellular Localisation | Secreted |
| Alternative Nanobody Names | Anti-Adiponectin nanobodyAnti-30 Kda Adipocyte Complement-Related Protein nanobodyAnti-Adipocyte Complement-Related 30 Kda Protein nanobodyAnti-Acrp30 nanobodyAnti-Adipocyte - C1q And Collagen Domain-Containing Protein nanobodyAnti-Adipose Most Abundant Gene Transcript 1 Protein nanobodyAnti-Apm-1 nanobodyAnti-Gelatin-Binding Protein nanobodyAnti-ADIPOQ nanobodyAnti-ACDC nanobodyAnti-ACRP30 nanobodyAnti-APM1 nanobodyAnti-GBP28 nanobody |
Information sourced from Uniprot.org
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