Anti-Alkaline Phosphatase, Tissue Non-Specific antibody

Target data

Alkaline phosphatase that metabolizes various phosphate compounds and plays a key role in skeletal mineralization and adaptive thermogenesis (PubMed : 10620060, PubMed : 11028439, PubMed : 14982838, PubMed : 23942722, PubMed : 33981039). Has broad substrate specificity and can hydrolyze a considerable variety of compounds : however, only a few substrates, such as diphosphate (inorganic pyrophosphate; PPi), pyridoxal 5'-phosphate (PLP) and N-phosphocreatine are natural substrates (PubMed : 19874193, PubMed : 23942722, PubMed : 33981039). Plays an essential role in skeletal and dental mineralization via its ability to hydrolyze extracellular diphosphate, a potent mineralization inhibitor, to phosphate : it thereby promotes hydroxyapatite crystal formation and increases inorganic phosphate concentration (PubMed : 10620060, PubMed : 11004006, PubMed : 11028439, PubMed : 12082181, PubMed : 14982838, PubMed : 32035618, PubMed : 9056646). Acts in a non-redundant manner with PHOSPHO1 in skeletal mineralization : while PHOSPHO1 mediates the initiation of hydroxyapatite crystallization in the matrix vesicles (MVs), ALPL/TNAP catalyzes the spread of hydroxyapatite crystallization in the extracellular matrix (PubMed : 20684022, PubMed : 26457330). Also promotes dephosphorylation of osteopontin (SSP1), an inhibitor of hydroxyapatite crystallization in its phosphorylated state; it is however unclear whether ALPL/TNAP mediates SSP1 dephosphorylation via a direct or indirect manner (PubMed : 23427088). Catalyzes dephosphorylation of PLP to pyridoxal (PL), the transportable form of vitamin B6, in order to provide a sufficient amount of PLP in the brain, an essential cofactor for enzymes catalyzing the synthesis of diverse neurotransmitters (PubMed : 7550313). Additionally, also able to mediate ATP degradation in a stepwise manner to adenosine, thereby regulating the availability of ligands for purinergic receptors (PubMed : 19874193, PubMed : 23825434, PubMed : 23942722, PubMed : 32028019). Also capable of dephosphorylating microbial products, such as lipopolysaccharides (LPS) as well as other phosphorylated small-molecules, such as poly-inosine : cytosine (poly I : C) (By similarity). Acts as a key regulator of adaptive thermogenesis as part of the futile creatine cycle : localizes to the mitochondria of thermogenic fat cells and acts by mediating hydrolysis of N-phosphocreatine to initiate a futile cycle of creatine dephosphorylation and phosphorylation (PubMed : 33981039). During the futile creatine cycle, creatine and N-phosphocreatine are in a futile cycle, which dissipates the high energy charge of N-phosphocreatine as heat without performing any mechanical or chemical work (PubMed : 33981039).