Anti-PCK2 antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Phosphoenolpyruvate carboxykinase 2 (PCK2) also known as mitochondrial PEPCK is an enzyme that plays an important role in gluconeogenesis. It catalyzes the conversion of oxaloacetate to phosphoenolpyruvate in the mitochondria. PCK2 has a molecular mass of approximately 69 kDa and is expressed mainly in tissues that require high energy production such as the liver and kidney. Despite its vital function in energy metabolism PCK2 is also present in other metabolic tissues.

Biological function summary

PCK2 contributes to the regulation of glucose homeostasis. It achieves this by being a part of the gluconeogenic pathway working in concert with cytosolic PCK1. PCK2 does not work alone; it integrates into a larger metabolic framework that includes various enzymes essential for converting different substrates into glucose. This enzyme is notably active during fasting states or periods of high energy demands such as intense exercise ensuring a continuous supply of glucose to maintain cellular functions.

Pathways

PCK2 plays an important role in the gluconeogenesis and TCA cycle. The gluconeogenesis pathway allows the liver and kidney to produce glucose from non-carbohydrate substrates which is integral during fasting and low-carbohydrate diet. It is functionally linked with other key enzymes like pyruvate carboxylase in converting pyruvate to glucose and also cooperates with malate dehydrogenase in the TCA cycle. This cooperation ensures efficient energy production and conversion balance in the cell.

Associated diseases and disorders

PCK2 expression is linked to type 2 diabetes and certain cancers. In type 2 diabetes altered PCK2 activity impacts glucose production contributing to hyperglycemia. Studies have shown that its dysregulation may correlate with insulin resistance a characteristic feature of diabetes. In cancer particularly some forms of breast cancer the interplay between PCK2 and oncogenes like KRAS can affect tumor metabolism promoting the adaptation of cancer cells to the energy-demanding environment.