Function and expression study uncovered hepatocyte plasma membrane ecto-ATP synthase as a novel player in liver regeneration.

ATP synthase, canonically mitochondrially located, is reported to be ectopically expressed on the plasma membrane outer face of several cell types. We analysed, for the first time, the expression and catalytic activities of the ecto- and mitochondrial ATP synthase during liver regeneration. Liver regeneration was induced in rats by two-thirds partial hepatectomy.

Short-term type-1 diabetes differentially modulates 14-3-3 proteins in rat brain and liver.

Background: The 14-3-3 proteins family consists of seven proteins that are highly conserved molecular chaperones with roles in the regulation of metabolism, signal transduction, cell cycle control, protein trafficking and apoptosis. Their role in several pathologies has been reported. In this study, we investigated the mRNA and protein expression of the 14-3-3s in rat brain and liver in the early stage of Type-1 diabetes (T1D).

3,5-Diiodo-L-thyronine administration to hypothyroid rats rapidly enhances fatty acid oxidation rate and bioenergetic parameters in liver cells.

Growing evidence shows that, among triiodothyronine derivatives, 3,5 diiodo-L-thyronine (T(2)) plays an important role in energy metabolism and fat storage. In the present study, short-term effects of T(2) administration to hypothyroid rats on fatty acid oxidation rate and bioenergetic parameters were investigated. Within 1 h following T(2) injection, state 3 and state 4 respiration rates, which were reduced in hypothyroid mitochondria, were noticeably increased particularly in succinate- with respect to glutamate/malate-energized mitochondria.

Mitochondrial proteome analysis reveals depression of the Ndufs3 subunit and activity of complex I in diabetic rat brain.

Type-1 diabetes resulting from defective insulin secretion and consequent hyperglycemia, is associated with "diabetic encephalopathy." This is characterized by brain neurophysiological and structural changes resulting in impairment of cognitive function. The present proteomic analysis of brain mitochondrial proteins from streptozotocin-induced type-1 diabetic rats, shows a large decrement of the Ndufs3 protein subunit of complex I, decreased level of the mRNA and impaired catalytic activity of the complex in the diabetic rats as compared to controls.

3,5-diiodo-L-thyronine increases FoF1-ATP synthase activity and cardiolipin level in liver mitochondria of hypothyroid rats.

Short-term effects of 3,5-L-diiodothyronine (T(2)) administration to hypothyroid rats on F(o)F(1)-ATP synthase activity were investigated in liver mitochondria. One hour after T(2) injection, state 4 and state 3 respiration rates were noticeably stimulated in mitochondria subsequently isolated. F(o)F(1)-ATP synthase activity, which was reduced in mitochondria from hypothyroid rats as compared to mitochondria from euthyroid rats, was significantly increased by T(2) administration in both the ATP-synthesis and hydrolysis direction.

3,5-diiodo-L-thyronine upregulates rat-liver mitochondrial F(o)F(1)-ATP synthase by GA-binding protein/nuclear respiratory factor-2.

Besides triiodothyronine (T3), 3,5-diiodo-L-thyronine (T2) has been reported to affect mitochondrial bioenergetic parameters. T2 effects have been considered as independent of protein synthesis. Here, we investigated the effect of in vivo chronic T2 administration to hypothyroid rats on liver mitochondrial F(o)F(1)-ATP synthase activity and expression.

Effect of the ATPase inhibitor protein IF1 on H+ translocation in the mitochondrial ATP synthase complex.

The H(+) F(o)F(1)-ATP synthase complex of coupling membranes converts the proton-motive force into rotatory mechanical energy to drive ATP synthesis. The F(1) moiety of the complex protrudes at the inner side of the membrane, the F(o) sector spans the membrane reaching the outer side. The IF(1) component of the mitochondrial complex is a basic 10 kDa protein, which inhibits the F(o)F(1)-ATP hydrolase activity.

Structural and functional characterization of F(o)F(1)-ATP synthase on the extracellular surface of rat hepatocytes.

Extracellular ATP formation from ADP and inorganic phosphate, attributed to the activity of a cell surface ATP synthase, has so far only been reported in cultures of some proliferating and tumoral cell lines. We now provide evidence showing the presence of a functionally active ecto-F(o)F(1)-ATP synthase on the plasma membrane of normal tissue cells, i.e.

A two-dimensional electrophoresis and mass spectrometry protein analysis of the antibiotic producer Nonomuraea sp. ATCC 39727 in different growth conditions.

Nonomuraea sp. ATCC 39727 is an aerobic actinomycete, industrially important as a producer of the glycopeptide A40926, which is used as a precursor of the semi-synthetic antibiotic dalbavancin. Previous studies showed that the production of A40926 is depressed by calcium, but promoted by l-glutamine or l-asparagine.

Inhibitory and anchoring domains in the ATPase inhibitor protein IF1 of bovine heart mitochondrial ATP synthase.

The inhibitor protein IF1 is a basic protein of 84 residues which inhibits the ATPase activity of the mitochondrial FoF1-ATP synthase complex without having any effect on ATP synthesis. Results of cross-linking and limited proteolysis experiments are presented showing that in the intact FoF1 complex "in situ," in the inner membrane of bovine heart mitochondria, the central segment of IF1 (residues 42-58) binds to the alpha and beta subunits of F1 in a pH dependent process, and inhibits the ATPase activity. The C-terminal region of IF1 binds, simultaneously, to the OSCP subunit of Fo in a pH-independent process.

Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.

The protein IF(1) is a natural inhibitor of the mitochondrial F(o)F(1)-ATPase. Many investigators have been prompted to identify the shortest segment of IF(1), retaining its native activity, for use in biomedical applications. Here, the activity of the synthetic peptides IF(1)-(42-58) and IF(1)-(22-46) is correlated to their structure and conformational plasticity determined by CD and [1H]-NMR spectroscopy.