One of the biologically active forms of nicotinic acid. Differs from NAD by an additional phosphate group at the 2?position of the adenosine moiety. Serves as a coenzyme of hydrogenases and dehydrogenases. Present in living cells primarily in the r
β-NADPH-d4 is the isotope labelled analog of β-NADPH. One of the biologically active forms of nicotinic acid. Differs from NAD by an additional phosphate group at the 2’-position of the adenosine moiety. Serves as a coenzyme of hydrogenases and dehydrogenases. Present in living cells primarily in the reduced form (NADPH) and is involved in synthetic reactions.
A coenzyme composed of ribosylnicotinamide 5′-
phosphate coupled by pyrophosphate linkage to
the 5′-phosphate adenosine 2′,5′-bisphosphate. The
reduced from of NADP. It is an energy-storage form
that can be transferred to the Calvin cycle where it
participates in the production of carbohydrate.
Nicotinamide adenine dinucleotide phosphate (NADPH) is used to maintain reduced glutathione (GSH) and thioredoxin (TRX). It is also well known as an essential electron donor and an indispensable cofactor for transferring and reserving reduction potential for numerous anabolic reactions. A growing body of evidence has shown that regeneration and maintenance of the cellular NADP(H) content is strongly implicated in various pathological conditions, such as diabetes, cardiovascular disease, neurodegenerative diseases, and aging, especially in tumorigenesis and cancer progression. Compared with non-tumor cells, tumor cells usually maintain high levels of NADPH to power redox defense and use biosynthetic reactions to sustain their rapid growth[1].
NADPH is predominantly bound to intracellular proteins with different affinities. The intracellular content of NADP(H) differs markedly among tissues and cell types. For instance, the total NADP(H) is about 420?nmol/g wet weight in rat liver 59% of total NADP(H) is found in mitochondria, and 30?nmol/g wet weight in skeletal muscle, and the NADPH concentration in the cytosol is 3.1?±?0.3 and 37?±?2?μM in the mitochondrial matrix in HeLa cells. In addition, the redox potentials of the mitochondrial and cytosolic NADP(H) systems are the same, around—400?mV in the liver[1].
[1] Huai-Qiang Ju. “NADPH homeostasis in cancer: functions, mechanisms and therapeutic implications.” Signal Transduction and Targeted Therapy (2020): 231.
