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anti-Human NNT Antikörper:
anti-Mouse (Murine) NNT Antikörper:
anti-Rat (Rattus) NNT Antikörper:
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Human Monoclonal NNT Primary Antibody für IF, ELISA - ABIN565110
Picklo: Ethanol intoxication increases hepatic N-lysyl protein acetylation. in Biochemical and biophysical research communications 2008
Cow (Bovine) Polyclonal NNT Primary Antibody für WB - ABIN2782785
Mehrle, Rosenfelder, Schupp, del Val, Arlt, Hahne, Bechtel, Simpson, Hofmann, Hide, Glatting, Huber, Pepperkok, Poustka, Wiemann: The LIFEdb database in 2006. in Nucleic acids research 2005
nnt-1 is important in the defense against mitochondrial oxidative stress
Study describes the fi rst (zeige SLC22A12 Antikörper) structural model of the human NNT. The 3D model identifies functional and structural H-NNT key motifs and gain essential insight into the structural and functional effect of deleterious amino acid substitutions causing glucocorticoid de fi ciency and LVNC cardiomyopathy, as well as rare homozygote amino acid variations.
NNT should be sequenced in all primary adrenal insufficiencies for which the most frequent etiologies have been ruled out. As NNT is involved in oxidative stress, careful follow-up is needed to evaluate mineralocorticoid biosynthesis extent, and gonadal, heart and thyroid function.
identified a 6.67 Mb homozygous region harboring the NNT gene in a Dutch patient presenting with familial glucocorticoid deficiency (FGD (zeige FGD1 Antikörper)); a novel homozygous mutation (NM_012343.3: c.1259dupG) in NNT was revealed; reviewed the literature for all the reported NNT mutations and their clinical presentation
This report of a novel NNT mutation, p.G200S, expands the phenotype of NNT mutations to include mineralocorticoid deficiency. It provides the first evidence that NNT mutations can cause oxidative stress and mitochondrial defects.
Data suggest mutations in nicotinamide nucleotide transhydrogenase (NNT) as contributory to left ventricular noncompaction (LVNC).
NNT mRNA expression is significantly higher in visceral fat of obese patients and correlates with body weight, BMI, % body fat, visceral and sc fat area, waist and hip circumference, and fasting plasma insulin (zeige INS Antikörper).
Results suggest that NNT may have a role in ROS (zeige ROS1 Antikörper) detoxification in human adrenal glands.
In the failing heart a partial loss of Nnt activity adversely impacts NADPH-dependent enzymes and the capacity to maintain membrane potential, thus contributing to a decline in bioenergetic capacity, redox regulation and antioxidant defense.
adrenal redox homeostasis mediated not only by under expression of NNT but also by its overexpression
this study demonstrates that the respiratory state and/or substrates that sustain energy metabolism markedly influence the relative contribution of NNT (i.e. varies between nearly 0 and 100%) to NADPH-dependent mitochondrial peroxide metabolism.
Pathologic workload reverses Nnt to deplete NADPH (zeige FDXR Antikörper) and antioxidative capacity. Reverse Nnt induces mitochondrial oxidative stress and necrosis.
In mitochondria, genetic or pharmacological disruptions in the PDHC-NNT redox circuit negate counterbalance changes in energy expenditure
Data conclude that Herpud1 (zeige HERPUD1 Antikörper) regulates insulin (zeige INS Antikörper) secretion via control of Nnt expression.
our data suggest that NNT functions as a high-capacity source of mitochondrial NADPH (zeige FDXR Antikörper) and that its functional loss due to the Nnt mutation results in mitochondrial redox abnormalities
the role of NNT in regulating central carbon metabolism via redox balance, calling for other mechanisms that coordinate substrate preference to maintain a functional TCA cycle.
Our results demonstrate a novel role for NNT as a regulator of macrophage-mediated inflammatory responses
A normal Nnt allele can help with better cardiac function in MnSOD (zeige SOD2 Antikörper)-deficient mice during fetal development.
The presence of a truncated Nnt did not affect insulin (zeige INS Antikörper) secretion or glucose tolerance on the C57BL/6 background.
This gene encodes an integral protein of the inner mitochondrial membrane. The enzyme couples hydride transfer between NAD(H) and NADP(+) to proton translocation across the inner mitochondrial membrane. Under most physiological conditions, the enzyme uses energy from the mitochondrial proton gradient to produce high concentrations of NADPH. The resulting NADPH is used for biosynthesis and in free radical detoxification. Two alternatively spliced variants, encoding the same protein, have been found for this gene.
Nicotinamide Nucleotide Transhydrogenase family member (nnt-1)
, nicotinamide nucleotide transhydrogenase
, NAD(P) transhydrogenase, mitochondrial
, pyridine nucleotide transhydrogenase
, Nicotinamide nucleotide transhydrogenase (NAD(P)+ transhydrogenase)