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In this research we have investigated the effects of mitochondrial peptide fraction bound to DNA on stationary rat hepatocyte cultures. The treatment with this peptide was responsible of cellular lysis, followed by significant proliferation after 46th day until 51st in which it is reestablished. In the present study it seems that peptides bound to hepatocyte mitochondrial DNA are involved in longer term cultural stabilization properties. Our results demonstrate that the peptide is a lysing factor activity at short terms.

A peptide fraction from the mitochondrial DNA of calf's liver was isolated using Drouin's method (1). This peptide fraction, which was extracted at pH 9.5 from an extensively purified mitochondrial DNA (2), has been shown to exert an in vitro regulatory role on the transcription and duplication activity of DNA (3). The same fraction also binds with mitochondrial DNA with a high affinity constant and stabilizes DNA from calf's thymus against thermal denaturation. The peptides from mitochondrial DNA have been subfractionated by fingerprinting-like techniques and one of them has been sequenced.

In this research the amino acidic composition of a peptide fraction from mitochondrial DNA has been determined, using HPLC and the fingerprinting technique. This peptide fraction has been shown to be composed of two sub-fractions with different reactivity to ninhydrin, and thus supplied with several N-substitute groups. The composition of the first fraction is Gln, Glu, Pro, Leu. The second fraction composition is Pro, Glu or Gln, Asp or Asn, Ser.

Authors tested "in vitro" action of a low molecular weight peptide fraction extracted by mitochondrial DNA from calf liver. The fraction acts upon duplication performed by E. Coli DNA polymerase I on poli dAT dAT template inhibiting chain elongation. The authors hypothesize that a similar role is exerted by this fraction "in vitro" on mitochondrial DNA template.

The authors verified the effect of a peptidic fraction from mitochondrial DNA on liver cell cultures. Primary cultures treated with the mitochondrial peptidic fraction (final concentration 0.025 O.D./ml) showed a higher viability after 48 hours with respect to cultures without mitochondrial peptidic fraction (p < 0.05). The results indicate a probable action of the mitochondrial peptidic fraction on liver cell viability.

In this paper the authors studied the effects of thyroid hormones and their structural analogues on the mitochondrial calcium transport activities. The thyroid hormones, 3,5,3' L-triiodothyronine (LT3) and 3,5,3'5' L-tetraiodothyronine (LT4) at physiological intracellular concentrations between 7.2 and 9 nM, decouple total Ca++ transport, as well as inhibit the passive transport of Ca++, either due to oxidation of pyruvate, malate or succinate or after inhibition with rotenone. The optical isomers 3,5,3' D-triiodothyronine (DT3) and 3,5,3',5' D-tetraiodothyronine (DT4) are less effective at all the used concentrations. Furthermore the structural analogues 3,3',5' L-triiodothyronine (LrT3), 3,5-dicloro, 3',5' L-diiodothyronine (LDiClT2) and 3,5 L-diiodothyronine (LT2) furnished even less effects on the same activities. The effect of the thyroid hormones and of their structural analogues has revealed that the mitochondrial calcium transport may be influenced both by a stereospecific interaction between hormones and protein ligands and by a lipophilic chaotropic action on the mitochondrial membranes lipids. In this context it is interesting to consider that both thyroid hormones and Ca++ transport activity are interacting with the energetic metabolism by means of phosphorylation and substrate oxidation mechanism.

The authors show the direct in vitro action of thyroid hormones on RNA-polymerase activity in rat liver mitochondria. 3,5,3' L-triiodothyronine (L-T3) and 3,5,3',5' L-tetraiodothyronine (L-T4) stimulate mitochondrial RNA synthesis without either increasing the permeability of preswollen mitochondria or stimulating the synthesis of the triphosphate ribonucleotides (NTP's). Thyroid hormones do not directly depress mitochondrial RNA hydrolysis. Studies carried out with structural analogues of thyroid hormones indicate the structural specifications of the regulating system of the mitochondrial RNA-polymerase. L-T3 and L-T4 are also effective 'in vitro' on mitochondria obtained from animals undergoing different hormonal and dietary treatments, with the exceptions of those fed with a hypoprotein diet. Thus, the authors suggest the possible intervention of a specific mitochondrial receptor for L-T3 and L-T4.