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A number of effects of weak combined (static and alternating) magnetic fields with an alternating component of tens and hundreds nT at a collinear static field of 42 microT, which is equivalent to the geomagnetic field, have been found: the activation of fission and regeneration of planarians Dugesia tigrina, the inhibition of the growth of the Ehrlich ascites carcinoma in mice, the stimulation of the production of the tumor necrosis factor by macrophages, a decrease in the protection of chromatin against the action of DNase 1, and the enhancement of protein hydrolysis in systems in vivo and in vitro. The frequency and amplitude ranges for the alternating component of weak combined magnetic fields have been determined at which it affects various biological systems. Thus, the optimal amplitude at a frequency of 4.4 Hz is 100 nT (effective value); at a frequency of 16.5 Hz, the range of effective amplitudes is broader, 150-300 nT; and at a frequency of 1 (0.5) Hz, it is 300 nT. The sum of close frequencies (e.g., 16 and 17 Hz) produces a similar biological effect as the product of the modulating (0.5 Hz) and carrying frequencies (16.5 Hz), which is explained by the ratio A = A0sin omega1t + A0sin omega2t = A0sin(omega1 + omega2)t/2cos(omega1 - omega2)t/2. The efficiency of magnetic signals with pulsations (the sum of close frequencies) is more pronounced than that of sinusoidal frequencies. These data may indicate the presence of several receptors of weak magnetic fields in biological systems and, as a consequence, a higher efficiency of the effect at the simultaneous adjustment to these frequencies by the field. Even with consideration of these facts, the mechanism of the biological action of weak combined magnetic fields remains still poorly understood.

Due to its role in dopamine system functioning in brain, angiotensin-1-converting enzyme (ACE) gene insertion-deletion (I/D) polymorphism is reportedly studied for association with major psychosis. The present study aimed at searching for I/D allele and genotype distribution in patients with major psychosis and healthy subjects and for an association between ACE gene polymorphism and clinical presentations of these disorders. One hundred and ninety-eight patients with schizophrenia (144) and affective disorders (54), 100 male, aged 36.3 +/- 12.8 years, and 247 controls, 87 male, aged 49.6 +/- 13.5 years, have been genotyped. No association was found between ACE gene polymorphism and major psychosis. In the group of males with schizophrenia, genotype distribution differed significantly from that in the male control group (chi2 = 6.24; p = 0.04), with frequencies of the DD genotype and the D allele being higher comparing to the II genotype and the I allele frequency (p = 0.04 and p = 0.01 respectively). It is suggested that in schizophrenia as well as in some other polygenic diseases ACE gene polymorphism might be rather considered as a modifying than a causal factor.

The action of two earlier isolated highly purified spleen thiol proteinases on angiotensins I and II, bradykinin and kallidin was investigated. It was demonstrated that proteinase I which is apparently cathepsin L from bovine spleen brings about rapid inactivation of angiotensin II with a splitting of the Tyr-Ile bond and a formation of two tetrapeptides. Proteinases I also split angiotensin I. Proteinase I partially inactivates bradykinin and kallidin by splitting the Gly4-Phe5 bond. The activity of proteinase I toward angiotensin II is about 50 times higher than that toward bradykinin. The corresponding values of Km and V are 7.5 X 10(-5) M and 10.0 mumole/min/mg. The possible role of proteinase I in angiotensin II inactivation under physiological conditions is discussed. Proteinase II converts kallidin to bradykinin by splitting off the N-terminal lysine. Proteinase II causes partial inactivation of bradykinin by splitting of the Gly4-Phe5 and Phe5-Ser6 bonds of this peptide. Proteinase II possesses both aminopeptidase and endopeptidase activities and is therefore cathepsin H from spleen. Proteinase II does not split either angiotensin I or angiotensin II.