Partial recovery from alloxan-induced diabetes by sodium phthalhydrazide in rats.

In the commonly used experimental model of diabetes, a cytotoxic glucose analogue alloxan can selectively destruct pancreatic β-cells, with characteristics similar to the type-1 diabetes (T1D) in humans. Treatment of diabetic rats with sodium phthalhydrazide partially reversed diabetogenic pathology in the alloxan-induced diabetes. The alloxan-treated rats with permanent hyperglycemia, which further received i.

Fermentation enzymes of Giardia intestinalis, pyruvate:ferredoxin oxidoreductase and hydrogenase, do not localize to its mitosomes.

It is becoming increasingly clear that the so-called remnant organelles of microaerophilic unicellular eukaryotes, hydrogenosomes and mitosomes, are significantly reduced versions of mitochondria. They normally lack most of the classic mitochondrial attributes, such as an electron transport chain and a genome. While hydrogenosomes generate energy by substrate-level phosphorylation along a hydrogen-producing fermentation pathway, involving iron-sulfur-cluster-containing enzymes pyruvate : ferredoxin oxidoreductase (PFO) and hydrogenase, whether mitosomes participate in ATP synthesis is currently unknown.

Mitochondrial porin VDAC 1 seems to be functional in rickettsial cells.

We have recently shown that Rickettsia prowazekii (typhus group rickettsiae) cells incorporate human mitochondrial porin VDAC1. Here, I report on the import of porin by rickettsiae of spotted fever group. It was shown that rickettsial cells of heavy band of Renografin density gradient, known as permeabilized rickettsiae, contain much more VDAC 1 compared to the cells of light band, that is, non-permeabilized rickettsiae.

A 29.5 kDa heat-modifiable major outer membrane protein of Rickettsia prowazekii, putative virulence factor, is a peptidyl-prolyl cis/trans isomerase.

Allelic genes from three Rickettsia prowazekii strains encoding parvulin-like protein (Plp), a heat-modifiable 29.5 kDa major outer membrane protein, were earlier cloned into expression vector pQE 30. In this work, recombinant proteins were overproduced in E.

Common evolutionary origin of mitochondrial and rickettsial respiratory chains.

Comprehensive phylogenetic analysis of the subunits of respiratory chain was carried out using a variety of mitochondrial and bacterial sequences including those from all unfinished alpha-proteobacterial genomes known to date. Maximum likelihood, neighbor-joining, and maximum parsimony consensus trees, based on four proton-translocating complexes, placed mitochondria as a sister group to the order Rickettsiales of obligate endosymbiotic bacteria to the exclusion of free-living alpha-proteobacteria. Thus, phylogenetic relationship of most eukaryotic respiratory enzymes conforms to canonical pattern of mitochondrial ancestry, prior established in analyses of ribosomal RNAs, which are encoded by residual mitochondrial genomes.

Phylogenetic affinity of a Giardia lamblia cysteine desulfurase conforms to canonical pattern of mitochondrial ancestry.

Among a few potential archezoan groups, only the Metamonada (diplomonads, retortamonads, and oxymonads) still retain the status of amitochondriate protists that diverged before the acquisition or retention of mitochondria. Indeed, finding that diplomonad genomes harbor a gene encoding a mitochondrial type chaperonin 60, the most compelling evidence for their secondarily amitochondriate nature, may be interpreted as an acquisition of this important general chaperone during some transient alpha-proteobacterial endosymbiosis. Recently published data on the cysteine desulfurase IscS demonstrated an alpha-proteobacterial origin of mitochondrial enzymes including a diplomonad Giardia lamblia homolog.

Mitochondrial connection to the origin of the eukaryotic cell.

Phylogenetic evidence is presented that primitively amitochondriate eukaryotes containing the nucleus, cytoskeleton, and endomembrane system may have never existed. Instead, the primary host for the mitochondrial progenitor may have been a chimeric prokaryote, created by fusion between an archaebacterium and a eubacterium, in which eubacterial energy metabolism (glycolysis and fermentation) was retained. A Rickettsia-like intracellular symbiont, suggested to be the last common ancestor of the family Rickettsiaceae and mitochondria, may have penetrated such a host (pro-eukaryote), surrounded by a single membrane, due to tightly membrane-associated phospholipase activity, as do present-day rickettsiae.

Phylogenetic relationships of organellar Hsp90 homologs reveal fundamental differences to organellar Hsp70 and Hsp60 evolution.

In agreement with endosymbiont theory for the origin of organelles, mitochondria and chloroplasts (plastids) are universally accepted to have monophyletically arisen from within alpha-proteobacteria and cyanobacteria, respectively. Convincing particular evidence in support of this theory emerged from phylogenetic analysis of highly conserved, ubiquitous heat shock proteins (Hsps) chaperonin 60 and Hsp70. These apparently indispensable general chaperones have proven to be highly useful molecular tracers of organellar origin.