[Ultrasound-guided percutaneous cryoablation of renal tumors].

INTRODUCTION: Surgery remains the gold-standard curative treatment for localized (T1) renal carcinoma. However, recent medical-technological advances have led to the development of new minimally invasive treatment options, one of which is percutaneous cryoablation. AIM: To assess the effectiveness and safety of ultrasound-guided percutaneous cryoablation of renal tumors. MATERIALS AND METHODS: The study comprised 12 patients aged 52 to 76 years who underwent ultrasound-guided percutaneous cryoablation of renal tumors from 2015 to 2017. In 11 patients, the size of the renal mass was 3.0 cm (T1a), in 1 patient 4.5 cm (T1b). A Doppler ultrasound, contrast-enhanced MSCT and computer 3D modeling were performed in all patients pre-operatively and 6 months after surgery to assess the tumors size and extent and the spatial location of the tumor internal surface to the pelvicalyceal system. In all patients, the tumors were located along the posterior or lateral surface of the kidney, in the lower or middle segment and without sinus invasion. We used a 3rd generation Galil Medicals SeedNet Gold Cryotherapy System and IceSeed and IceRod cryoprobes. Intraoperatively, immediately before cryoablation, the tumor was biopsied. In all patients the diagnosis of renal cell carcinoma was confirmed morphologically. RESULTS: Mean duration of cryoablation was 60 minutes. Endotracheal, spinal, local and intravenous anesthesia was used in 1, 6, 5 and 1 patients, respectively. Doppler ultrasound at 6 months after surgery showed that in 11 patients (T1a) the tumor size decreased on average by 8 mm, with no blood flow in the tumors. MSCT with 3D modeling also revealed a decrease in tumor size and total absence of contrast agent accumulation, or accumulation gradient not exceeding 10 HU (initially it was about 200 HU). In the patient with T1b stage renal carcinoma, MSCT showed a decrease in tumor size from 4.5 to 3.7 cm, however, there was a mass up to 1.5 cm with a high gradient of contrast agent accumulation. The patient underwent kidney resection. No intra- and postoperative complications were observed. CONCLUSION: The accumulated experience allows to confirm the effectiveness and safety of ultrasound-guided percutaneous cryoablation and to consider it a method of choice for patients with stage T1a renal carcinoma located along the posterior or lateral surface of the kidney in the lower or middle segment, without sinus invasion.

[Time course of morphological changes in humoral renal allograft rejection in ABO incompatibility between donor and recipient].

One hundred and five biopsy specimens taken in different periods after 34 ABO-incompatible mismatched related kidney transplantations were examined to establish the patterns of humoral activity from the morphological changes and expression of C4d deposits in the peritubular capillaries. Severe reversible forms of acute humoral rejection (AHR) (2 patients) and minimal morphological manifestations (13 patients) were observed in the biopsy specimens taken as long as 2 months later in Group 1 (C4d+). In the early period, the minimal manifestations of AHR did not cause organ dysfunction; but in the late period, 5 of them developed chronic humoral rejection in persistent humoral activity; 4 grafts were removed 531,720, 1019, and 1252 days later. Group 2 (C4d-) (n = 19) showed no graft losses or significant chronic changes; the late minimal manifestations of AHR had no impact on the duration of organ function in 3 recipients. The timely detection of early humoral activity and minimal manifestations of AHR is needed for the measures taken to reduce a risk for late function loss of the grafted organ.

[Liver resection after neoadjuvant colorectal chemotherapy: short-term results].

The conducted survey proves, that surgical tactics by liver resections after the neoadjuvant chemotherapy should not differ, regarding the volume of liver resection. Hystologic hepatic parenchyma reactions to the action of chemotherapy were predominately the steatosis and fibrosis.

[Effect of Ca2+ ions on hydrodynamic properties of pentamer and decamer of C-reactive protein in solution]. / Vliianie ionov Ca2+ na gidrodinamicheskie svoistva pentamera i dekamera C-reaktivnogo belka v rastvore.

The molecular mass and sedimentation coefficient of native C-reactive protein in solution were determined by analytical ultracentrifugation in the presence and absence of calcium ions. Pentameric C-reactive protein was shown to be the major macroscopic form of this protein in solution. The removal of calcium ions from solution caused decompaction of the protein accompanied by changes in its hydrodynamic parameters. The sedimentation coefficient s20(0), w of pentameric C-reactive protein in solution containing 2 mM--Ca2+ (6.6S) exceeded that for C-reactive protein in solution containing 2 mM EDTA (6.4S). Analysis of average molecular masses Mw and Mz obtained from sedimentation data demonstrated that the solution of highly purified protein was not homogeneous. As shown by intermolecular crosslinking, the solution also contained the 241-kDa decamer of C-reactive protein (9.5S) as a separate macroscopic form, whose share hardly reached 10% in the presence of 2 mM Ca2+ and increased after removal of calcium ions. The decamers were shown to result from intermolecular association of the pentamers.

[Aggregation of C-reactive protein in solutions at acid pH]. / Agregatsiia C-reaktivnogo belka v rastvorakh pri kislom znachenii pH.

The hydrodynamic properties of the C-reactive protein (CRP) at different pH were studied using quasi-elastic light scattering, size-exclusion liquid chromatography, and nonreducing gel electrophoresis. It was shown that a CRP solution at pH 5.0-7.2 presents a polydisperse system the major component of which is the native pentameric CRP. At pH 4.0-4.5, CRP exists in two states having different hydrodynamic properties: the native pentameric form with a molecular mass of 120 kDa and with the hydrodynamic radius of 4.03 nm and high-molecular-weight aggregates with a wide range of their molecular weight distribution. The interaction of the C-reactive protein with monoclonal antibodies to it indicates that conformation-dependent surface epitopes of the protein lose the native structure at pH 5.0-5.5. The aggregation of CRP is an irreversible process, which begins in a narrow pH range of pH 5.0-4.5 and is not accompanied by the dissociation into subunits but is determined by intermolecular interactions of its quasi-native pentamers.

[Hydrodynamic parameters of native C-reactive protein molecule in a solution]. / Gidrodinamicheskie parametry molekuly nativnogo C-reaktivnogo belka v rastvore.

The hydrodynamic properties of the C-reactive protein in solution (pH 6.8) were studied using quasi-elastic light scattering and size-exclusion liquid chromatography. It was shown that the solution containing the C-reactive protein represents a polydisperse system. The values of the translation diffusion coefficient and the apparent molecular weight of the C-reactive protein in solution at pH 6.8 were determined. The values of the translation diffusion coefficient, molecular weight and the hydration radius obtained suggest that the native pentameric C-reactive protein is the major form of the protein in solution at pH 6.8.

[Malignant central nervous system tumors are susceptible to specific antibodies]. / Zlokachestvennye opukholi tsentral'noi nervnoi sistemy mogut byt' dostupny dlia ataki spetsificheskimi antitelami.

The binding of circulating specific IgG to glioblastoma cells from brain tumor biopsies was shown using fluorescence conjugate Protein A-FITC and Western blotting. Blood-brain barrier permeability for antitumor antibodies in vivo in glioblastoma patients is suggested.

Human immunoglobulin light chains lambda form amyloid fibrils and granular aggregates in solution.

Myeloma nephropathy is a disorder characterized by deposition of monoclonal immunoglobulin light chains in the kidneys. The chains deposited form either amyloid fibrils or granular (amorphous) aggregates. Distinct molecular mechanisms leading to the formation of different aggregate types in kidney of patients with multiple myeloma are poorly understood. Here we describe the self-association kinetics of human monoclonal immunoglobulin light chains lambda (GRY) isolated from urine of a patient with multiple myeloma. Under physiological conditions, the isolated light chain exists predominantly in a form of covalent dimer with apparent molecular mass of 50.1 kD. Spectral probe binding, analytical gel filtration, Western blot analysis, and electron microscopy indicate that GRY dimer aggregation occurs via two different pathways producing either amyloid fibrils or amorphous aggregates depending on microenvironment. Incubation of GRY (25 microM) for 4-14 days at 37 degrees C in phosphate buffered saline (PBS), pH 7.0, or in PBS containing urea (0.8 M), pH 6.5, leads to amyloid fibril formation. Under electron microscopy, the fibrils show unbranched thread-like structures, approximately 60-80 x 1000 A in size, which can bind thioflavin T and Congo Red. GRY maintained in acetate buffer, pH 3.5, forms granular aggregates. The structure of GRY oligomers formed during the early stage of amyloid fibril formation (1-4 days) has been examined by means of protein cross-linking with homobifunctional reagents. These oligomers are predominantly trimers and tetramers.

Thermodynamic stability and functional activity of tumor-associated antibodies.

Tumor-associated antibodies of human IgG1 subclass were eluted from cell-surface antigens of human carcinoma cells and studied by differential scanning calorimetry and binding to local conformational probes, protein A from Staphylococcus aureus and a monoclonal antibody targeted to the CH2 domain of the Fc fragment. At pH 2.0-7.0, we observed virtually identical enthalpies of thermal unfolding for IgG1 from normal human sera and tumor-associated IgG1. The exact values of calorimetric enthalpy (Delta h) at pH 7.0 were 6.1 and 6.2-6.3 cal/g for IgG1 from normal serum and IgG1 from carcinoma cells, respectively. The affinity constants of protein A binding to the CH2--CH3 domain interface demonstrated differences between serum IgG1 and tumor associated IgG1 that did not exceed 3-8-fold. The binding affinity toward the anti-CH2 monoclonal antibody determined for serum IgG1 and IgG1 from carcinoma cells differed not more than 2.5-fold. The thermodynamic parameters of IgG1 from carcinoma cells strongly suggest that protein conformational stability was essentially unaltered and that the Fc fragment of the tumor-derived IgG1 preserved its structural integrity.

Anti-plasminogen autoantibodies from plasma of patients with systemic lupus erythematosus having anti-phospholipid antibody syndrome: isolation and some immunochemical properties.

Blood plasma samples from patients with systemic lupus erythematosus having the anti-phospholipid antibody syndrome were found to contain anti-plasminogen antibodies of the IgG class. The titers of anti-plasminogen autoantibodies of the IgG class were elevated in these patients compared with normal controls. Part of the pool of IgG anti-plasminogen antibodies reacts with an epitope in the lysine-binding sites of plasminogen. Anti-plasminogen IgG isolated from patients' blood plasma is specific only for a native epitope of human plasminogen passively adsorbed on immunosorbent micro-titration plate. As shown by enzyme immunoassay, autoantibodies to plasminogen of the IgG class cross-react with human fibrinogen.