Intestinal alkaline phosphatase (IAP) (IAP)

Intestinal alkaline phosphatase (IAP) is a homodimeric metalloenzyme anchored to the brush-border membrane of the intestinal epithelium (UniProt Consortium, 2023). Its primary biological function involves the dephosphorylation of various phosphate esters, including pro-inflammatory molecules like lipopolysaccharides (LPS), flagellin, and extracellular adenosine triphosphate (ATP) (Lallès, 2010). By detoxifying these compounds at its catalytic site, IAP plays a pivotal role in maintaining the integrity of the intestinal barrier and preventing the translocation of bacteria and toxins into the systemic circulation (Malo et al., 2010). Reduced levels or activity of IAP are associated with chronic inflammatory conditions, such as inflammatory bowel disease and metabolic syndrome (Bilski et al., 2017). Therapeutic strategies often focus on supplementing IAP levels using bovine-derived or recombinant human enzymes to treat sepsis-associated acute kidney injury or to restore gut homeostasis (Pickkers et al., 2018). The enzyme's activity is also a key regulator of the gut microbiome and lipid absorption, making it a central player in metabolic health.

Other names

ALPIIntestinal-type alkaline phosphataseGlycerophosphataseKasahara isozyme

Hydrolysis of phosphate esters from pro-inflammatory substrates (e.g., LPS, ATP) at the catalytic site to reduce their toxicity and prevent systemic inflammation.