[The role of forensic medical expertise of material evidence in the investigations into the cases of sexual offence].

The objective of the present study was to search for the methods for the enhancement of the effectiveness of forensic medical examination of material evidence during the investigations into the crimes against sexual immunity and personal sexual freedom. The work included the analysis of the relevant expert conclusions and copies of the decisions approving the performance of the forensic medical expertises. The study was carried out with the use of the following methods: the extraction of necessary data from the primary materials, their systematization and treatment by the methods of descriptive and analytical statistics.

Recruitment of Gβγ controls the basal activity of G-protein coupled inwardly rectifying potassium (GIRK) channels: crucial role of distal C terminus of GIRK1.

The G-protein coupled inwardly rectifying potassium (GIRK, or Kir3) channels are important mediators of inhibitory neurotransmission via activation of G-protein coupled receptors (GPCRs). GIRK channels are tetramers comprising combinations of subunits (GIRK1-4), activated by direct binding of the Gβγ subunit of Gi/o proteins. Heterologously expressed GIRK1/2 exhibit high, Gβγ-dependent basal currents (Ibasal) and a modest activation by GPCR or coexpressed Gβγ.

Two distinct aspects of coupling between Gα(i) protein and G protein-activated K+ channel (GIRK) revealed by fluorescently labeled Gα(i3) protein subunits.

G protein-activated K(+) channels (Kir3 or GIRK) are activated by direct interaction with Gβγ. Gα is essential for specific signaling and regulates basal activity of GIRK (I(basal)) and kinetics of the response elicited by activation by G protein-coupled receptors (I(evoked)). These regulations are believed to occur within a GIRK-Gα-Gβγ signaling complex.

G alpha(i) and G betagamma jointly regulate the conformations of a G betagamma effector, the neuronal G protein-activated K+ channel (GIRK).

Stable complexes among G proteins and effectors are an emerging concept in cell signaling. The prototypical G betagamma effector G protein-activated K(+) channel (GIRK; Kir3) physically interacts with G betagamma but also with G alpha(i/o). Whether and how G alpha(i/o) subunits regulate GIRK in vivo is unclear.

Divergent regulation of GIRK1 and GIRK2 subunits of the neuronal G protein gated K+ channel by GalphaiGDP and Gbetagamma.

G protein activated K+ channels (GIRK, Kir3) are switched on by direct binding of Gbetagamma following activation of Gi/o proteins via G protein-coupled receptors (GPCRs). Although Galphai subunits do not activate GIRKs, they interact with the channels and regulate the gating pattern of the neuronal heterotetrameric GIRK1/2 channel (composed of GIRK1 and GIRK2 subunits) expressed in Xenopus oocytes. Coexpressed Galphai3 decreases the basal activity (Ibasal) and increases the extent of activation by purified or coexpressed Gbegagamma.

[Peculiarities of sexual development in Caucasoids and Ural Mongoloids in Northern Russia].

A review of the domestic scientific literature concerning forensic medical aspects of the girls' pubertal development is presented. The interplay of various social factors is shown to influence the rate of sexual maturation and the age at which puberty begins. Racial differences of these parameters are demonstrated.

[Specific features of mineral and protein metabolism in patients with paranasal osteoma].

A comparative analysis of biochemical blood picture was made in 20 patients with osteoma of the paranasal sinuses before and after surgical treatment. A total of 17 tests characterizing metabolism and 680 biochemical examinations were made. Investigation of mineral and other kinds of metabolism may be important in diagnosis of osteomas, hyperostosis, exostosis and malignant tumors, determination of activity and tumor growth rate.

[Role of pectins in the complex treatment in patients in neurointensive care units].

Clinical and laboratory estimation of the efficacy of pectins in complex treatment of patients with intracranial hematoma was performed. It was shown that in the group of the patients treated with pectins vs the control group development of pyo-inflammatory infections was less frequent, the indices of the immunity status improved and a more rapid decrease of the intoxication and a more rapid normalization of the composition of various biotopes in the patients were observed.

Galphai1 and Galphai3 differentially interact with, and regulate, the G protein-activated K+ channel.

G protein-activated K(+) channels (GIRKs; Kir3) are activated by direct binding of Gbetagamma subunits released from heterotrimeric G proteins. In native tissues, only pertussis toxin-sensitive G proteins of the G(i/o) family, preferably Galpha(i3) and Galpha(i2), are donors of Gbetagamma for GIRK. How this specificity is achieved is not known.

[Protein content in blood plasma and its changes in patients of the neurological critical care unit].

Twelve blood plasma proteins were studied in 120 patients with isolated traumatic and nontraumatic cerebral hemorrhage. At all stages of the study a marked imbalance of blood proteins occurred which was independent of the etiological factor. Patients with craniocerebral trauma exhibited the phenomenon of the atypical response manifesting with low concentration of acute-phase proteins.

Mapping the Gbetagamma-binding sites in GIRK1 and GIRK2 subunits of the G protein-activated K+ channel.

G protein-activated K+ channels (Kir3 or GIRK) are activated by direct binding of Gbetagamma. The binding sites of Gbetagamma in the ubiquitous GIRK1 (Kir3.1) subunit have not been unequivocally charted, and in the neuronal GIRK2 (Kir3.

Na+ promotes the dissociation between Galpha GDP and Gbeta gamma, activating G protein-gated K+ channels.

G protein-gated K(+) channels (GIRK, or Kir3) are activated by the direct binding of Gbetagamma or of cytosolic Na(+). Na(+) activation is fast, Gbetagamma-independent, and probably via a direct, low affinity (EC(50), 30-40 mm) binding of Na(+) to the channel. Here we demonstrate that an increase in intracellular Na(+) concentration, [Na(+)](in), within the physiological range (5-20 mm), activates GIRK within minutes via an additional, slow mechanism.

G(alpha)(i) controls the gating of the G protein-activated K(+) channel, GIRK.

GIRK (Kir3) channels are activated by neurotransmitters coupled to G proteins, via a direct binding of G(beta)(gamma). The role of G(alpha) subunits in GIRK gating is elusive. Here we demonstrate that G(alpha)(i) is not only a donor of G(beta)(gamma) but also regulates GIRK gating.

A novel long N-terminal isoform of human L-type Ca2+ channel is up-regulated by protein kinase C.

Human L-type voltage-dependent Ca(2+) channels (alpha(1C), or Ca(v)1.2) are up-regulated by protein kinase C (PKC) in native tissues, but in heterologous systems this modulation is absent. In rat and rabbit, alpha(1C) has two N-terminal (NT) isoforms, long and short, with variable initial segments of 46 and 16 amino acids, respectively.

[Homeostasis and its correction in burn patients with gastrointestinal erosive-ulcerative diseases].

Acute erosive ulcerative hemorrhage (EUH) is one of the most grave complications of burn disease, caused by impaired blood rheology, clotting, and protein status. Twenty-three patients with burns of 12-70% body surface were examined, 17-25% of burns being deep. The most pronounced changes in blood rheology and clotting with formation of erythrocyte aggregations, fibrin precipitation and imbalance of visceral proteins were observed during the shock stage (days 1-3), particularly pronounced in patients with acute EUH.

[Early evaluation of blood loss by the profile of blood proteins in patients with injuries].

The concentrations of positive (C-reactive protein, orosomucoid, haptoglobin, ceruloplasmin) and negative (transtiretine, alpha 2-macroglobulin, transferrin) markers of acute phase response were measured in 55 victims with injuries to hollow organs on day 1 of hospitalization. By visual intraoperative evaluation of blood loss, the patients were divided in 2 groups: with blood loss under 1 liter (n = 32, group 1) and more than 1 liter (n = 23, group 2). Acute phase response was more manifest in group 1.

Modulation of L-type Ca2+ channels by gbeta gamma and calmodulin via interactions with N and C termini of alpha 1C.

Neuronal voltage-dependent Ca(2+) channels of the N (alpha(1B)) and P/Q (alpha(1A)) type are inhibited by neurotransmitters that activate G(i/o) G proteins; a major part of the inhibition is voltage-dependent, relieved by depolarization, and results from a direct binding of Gbetagamma subunit of G proteins to the channel. Since cardiac and neuronal L-type (alpha(1C)) voltage-dependent Ca(2+) channels are not modulated in this way, they are presumed to lack interaction with Gbetagamma. However, here we demonstrate that both Gbetagamma and calmodulin directly bind to cytosolic N and C termini of the alpha(1C) subunit.

Expression cloning of KCRF, a potassium channel regulatory factor.

By functional coexpression screening of a rat cDNA library in Xenopus oocytes, we have cloned a protein (KCRF: K Channel Regulatory Factor) that reduces currents of several K(+) channels: G protein-activated GIRK1/4 (K(ir)3.1/K(ir)3.4), inward rectifier IRK1 (K(ir)2.

Expression of GIRK (Kir3.1/Kir3.4) channels in mouse fibroblast cells with and without beta1 integrins.

G protein-activated K+ channel (GIRK) subunits possess a conserved extracellular integrin-binding motif (RGD) and bind directly to beta1 integrins. We expressed GIRK1/GIRK4 channels labeled with green fluorescent protein in fibroblast cell lines expressing or lacking beta1 integrins. Neither plasma membrane localization nor agonist-evoked GIRK currents were affected by the absence of beta1 integrins or by incubation with externally applied RGD-containing peptide.

The N terminus of the cardiac L-type Ca(2+) channel alpha(1C) subunit. The initial segment is ubiquitous and crucial for protein kinase C modulation, but is not directly phosphorylated.

The first 46 amino acids (aa) of the N terminus of the rabbit heart (RH) L-type cardiac Ca(2+) channel alpha(1C) subunit are crucial for the stimulating action of protein kinase C (PKC) and also hinder channel gating (Shistik, E., Ivanina, T., Blumenstein, Y.

Regulation of cardiac L-type Ca2+ channel by coexpression of G(alpha s) in Xenopus oocytes.

Activation of G(alpha s) via beta-adrenergic receptors enhances the activity of cardiac voltage-dependent Ca2+ channels of the L-type, mainly via protein kinase A (PKA)-dependent phosphorylation. Contribution of a PKA-independent effect of G(alpha s) has been proposed but remains controversial. We demonstrate that, in Xenopus oocytes, antisense knockdown of endogenous G(alpha s) reduced, whereas coexpression of G(alpha s) enhanced, currents via expressed cardiac L-type channels, independently of the presence of the auxiliary subunits alpha2/delta or beta2A.

Crucial role of N terminus in function of cardiac L-type Ca2+ channel and its modulation by protein kinase C.

The role of the cytosolic N terminus of the main subunit (alpha1C) of cardiac L-type voltage-dependent Ca2+ channel was studied in Xenopus oocyte expression system. Deletion of the initial 46 or 139 amino acids (a.a.

[Acute phase response and plasma proteins in acute cholecystitis].

Changes in the levels of plasma proteins albumin, transtiretine, transferrin, C-reactive protein, orosomucoid, and alpha 1-antitrypsin were followed up in patients with acute cholecystitis. Acute-phase response develops in acute cholecystitis; its development is most accurately characterized by the concentrations of C-reactive protein. The content of this protein together with the concentrations of transtiretine, orosomucoid, and alpha 1-antitrypsin can be regarded as an indicator of the severity of inflammation of the gallbladder and helps predict the disease course and define the terms of an intervention by the least invasive methods of treatment.

Ca2+ current enhancement by alpha 2/delta and beta subunits in Xenopus oocytes: contribution of changes in channel gating and alpha 1 protein level.

1. A combined biochemical and electrophysiological approach was used to determine the mechanism by which the auxiliary subunits of Ca2+ channel enhance the macroscopic Ca2+ currents. Xenopus oocytes were injected with RNA of the main pore-forming subunit (cardiac: alpha 1C), and various combinations of RNAs of the auxiliary subunits (alpha 2/delta and beta 2A).

Inhibition of function in Xenopus oocytes of the inwardly rectifying G-protein-activated atrial K channel (GIRK1) by overexpression of a membrane-attached form of the C-terminal tail.

Coexpression in Xenopus oocytes of the inwardly rectifying guanine nucleotide binding (G)-protein-gated K channel GIRK1 with a myristoylated modification of the (putative) cytosolic C-terminal tail [GIRK1 aa 183-501 fused in-frame to aa 1-15 of p60src and denoted src+ (183-501)] leads to a high degree of inhibition of the inward G-protein-gated K+ current. The nonmyristoylated segment, src- (183-501), is not active. Although some interference with assembly is not precluded, the evidence indicates that the main mechanism of inhibition is interference with functional activation of the channel by G proteins.