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The aim of the study is to evaluate oxidant-antioxidant balance as well as lysosomal and anti-protease activities in ovarian cancer since it has been emphasized that the crucial inducing factor of carcinogenesis may be reactive oxygen/nitrogen species or, more precisely, oxidative stress-induced inflammation. The study involved 15 women with ovarian cancer, aged 59.9 ± 7.8 years, and 9 healthy women aged 56.3 ± 4.3 years (controls). The study material was venous blood collected from fasting subjects. In erythrocytes, the activities of superoxide dismutase, glutathione peroxidase, and catalase, as well as concentrations of conjugated dienes (CDs) and thiobarbituric acid reactive substances (TBARS), were investigated. CD, TBARS, and vitamins A and E plasma concentrations were also determined. Moreover, total antioxidant capacity and concentrations of 4-hydroxynonenal adducts and 8-iso-prostaglandin F2α, as well as activities of acid phosphatase, arylsulfatase, cathepsin D, and α 1 -antitrypsin, were studied in serum. The vitamin E and 8-iso-prostaglandin F2α concentrations as well as arylsulfatase activity were lower in the women with cancer compared to the controls ( p = 0.006, p = 0.03, p = 0.001, respectively). In contrast, cathepsin D activity was lower in the controls ( p = 0.04). In the peripheral blood of the women with cancer, oxidant-antioxidant and lysosomal disturbances were observed.

Deep electromagnetic stimulation (DEMS) and low-frequency ultrasound (US) are new physical therapy methods used in the rehabilitation of the musculoskeletal system and wound healing. They are applied locally to treat the injured tissues. The beneficial effects of these methods in supportive care have been documented, but accurate biochemical effects are not known. The goal was to assess the effect of single DEMS and US sessions on the oxidant-antioxidant equilibrium, as well as the activities of lysosomal hydrolases and α 1 -antitrypsin (AAT) in peripheral blood of juvenile injured amateur athletes. In the athletes with low back pain (DEMS treated, N = 16) and pain in the shoulder or ankle joint (US treated, N = 14), as well as in healthy control amateur athletes (DEMS treated, N = 14; US treated, N = 17), before the sessions and 30 minutes and 24 hours after them, the levels of the following parameters were determined: thiobarbituric acid reactive substances (TBARS) in erythrocytes and plasma, superoxide dismutase (SOD), glutathione peroxidase (GPx), and catalase (CAT) in erythrocytes, as well as acid phosphatase (AcP), arylsulfatase (ASA), cathepsin D (CTS D), and α 1 -antitrypsin (AAT) in serum. After both procedures, the levels of parameters changed in a negligible manner, excluding the cathepsin D activity, which was statistically significantly lower 30 min and 24 h after US in the control athletes compared to the baseline activity determined directly before the procedure (47.5% and 55.7% differences, respectively). Similar tendency was observed after DEMS ( p > 0.05). The procedures, especially low-frequency US, decrease lysosomal proteolytic activity and do not significantly disrupt the oxidant-antioxidant and lysosomal equilibriums in the peripheral blood both of healthy and injured athletes. No systemic acute-phase response of AAT was also detected in the athletes after both procedures. This trial is registered with CTRI/2018/01/011344., Competing Interests: The authors declare that they have no competing interests., (Copyright © 2020 Łukasz Sielski et al.)

Objective: To assess the activity of arylsulfatase (AS), acid phosphatase (ACP), cathepsin D (CAT-D) and alpha-1 antitrypsin (AAT) in blood serum and synovial fluid (SF) of patients with hip or knee osteoarthritis (OA)., Methods: The study included 43 subjects with OA (35 hip OA, 8 knee OA), submitted total joint replacement. The control group consisted of 58 subjects with no past history of musculoskeletal disorders., Results: The OA blood serum samples showed a significantly higher level of lysosomal enzymes activity than in the control group (AS by 17.8%, AAT by 42.4%); only the CAT-D activity decreased by 50%). AS, ACP and CAT-D activities were about two-fold higher in SF when compared with blood of OA patients. The differences between the genders were visible in the SF: Total protein concentration, activity of ACP (both higher in OA men) and activity of CAT-D (higher in OA women). Between the involved hip and knee, there were no significant differences in all estimated parameters in the blood serum of the OA group. In regard to the SF, only ACP activity was significantly higher in patients with a hip involved., Conclusions: The osteoarthritic SF enzymatic profile differs from that in normal joints. The OA in joints is not reflected in the systemic response. Our preliminary results suggest further studies on role of lysosomal enzymes (ACP and AS) as biomarkers for the detection of osteoarthritis.

The activity of α1-antitrypsin (AAT) and the lysosomal enzymes, cathepsin D (CTS D), arylsulfatase (ASA), and acid phosphatase, (AcP) was determined in patients with COPD (GOLD category A). Moreover, the diagnostic usefulness of these parameters in blood serum was assessed along with establishing whether smoking cessation affects these parameters. The study included 70 patients with COPD who ceased smoking (study group) and two control groups of 33 subjects each: nonsmokers without COPD (control I) and patients with COPD who continued smoking (control II). In control I, blood was taken once and in control II, at the start of the experiment and after the 1st, 2nd, and 3rd months. AAT in the patients exhibited higher activity than in the healthy subjects at all time points. AAT activity in the patients before the start of the experiment was ~80% higher (P < 0.001) than in control I. No statistically significant differences in CTS D, ASA, and AcP activity were found. COPD involves increased AAT activity and unchanged activities of the assessed lysosomal enzymes. Three-month tobacco abstinence does not affect these parameters in peripheral blood. Determining the AAT levels in blood serum can be used in the diagnostics of COPD.

To evaluate a possible mechanism of stress-induced lymphopenic effect we assessed the activity of lymphocyte lysosomal enzymes (LE) under immobilization. The effects of immobilization stress on LE (AP, acid phosphatase, cathepsin D and L, beta-N-acetyl-glucosamidase) activity in lymphocytes, number of lymphocytes and plasma cortisol (COR) level in the peripheral blood were examined in the cross-bred Pietrain pigs showing genotypic (presence or lack of RyR1 gene mutation) and phenotypic (reactivity to halothane) differences. It was found that immobilization stress evoked an increase in LE which was concomitant with lymphopenia and a rise of COR level. The most pronounced enhancement of LE, which may reflect a tendency to lymphocyte cytolysis, was found in the recessive homozygotes RyR1 (nn) phenotypically defined as stress/halothane susceptible as well as in the heterozygotes RyR1 (Nn) included in the group of stress/halothane resistant. Despite this individual variability the stress-induced increase in LE activity was present in all the animals. It seems that a possibility of destruction (lysis) of lymphocyte cells should not be excluded as one of the causes of stress lymphopenia.

Objectives: Observing the changes of activity of some lysosomal enzymes in blood serum of female rabbits subjected to injection of 10 microg of ghrelin/kg of body weight., Methods: In the blood serum the activity of cathepsins D and L, alanine aminopeptidase, acid phosphatase, lysosomal lipase and lysosomal esterase was determined., Results: As a result of ghrelin injection the activity of all the enzymes examined in blood serum increased markedly., Conclusion: Changes of lysosomal enzymes activities in the blood serum caused by the effects of ghrelin should be regarded as the response of the lysosomal system.

Background: The paper compares the effects of ozone therapy and conventional balneological methods on health condition of patients with obliterative atheromatosis and on serum activity of three lysosomal enzymes., Material/methods: Sixty-four patients with lower limb ischaemia in the course of obliterative atheromatosis (without diabetes) were enrolled in the study. Thirty-two patients were treated with ozone administered by intravenous infusions and 30-minute aerosol oxygen-ozone baths. A comparative group was formed of 32 patients treated with traditional balneology. There was also a control group made up of 30 healthy subjects. Ozone therapy as well as traditional balneology were administered daily for the period of 10 days, excluding Saturdays and Sundays. Blood for biochemical analysis was collected from elbow vein in the following time intervals: 24 hours before ozone therapy or classical balneology, one hour after therapy and on the 10th day of treatment. The activity of cathepsin D, acid phosphatase and arylsulphatase as well as the levels of a-1-antitrypsin (protease inhibitor) were determined in blood serum of patients with obliterative atheromatosis., Results: In patients who received ozone therapy the activity of analysed lysosomal hydrolases returned to the values typical for healthy subjects. Patients' general condition also improved. The use of traditional balneological methods did not result in any significant change either in the activity of lysosomal hydrolases, the level of a-1-antitrypsin or general condition of patients., Conclusions: Ozone therapy administered by intravenous infusions and aerosol oxygen-ozone baths of lower extremities yields much better therapeutic results in comparison with classical balneology.

The aim of the study was an assessment of some lysosomal enzymes activity in serum and in tumors of patients with lung cancer histopathologically confirmed as squamous cell lung carcinoma. The first group constisted of 10 patients with stage II of the disease and the second group consisted of 11 patients with stage III of the disease. Lysosomal enzymes activities were assayed in serum before surgery and on the 10th day after surgery in serum and in tumors. Arylsuphatase, cathepsin D and acid phosphatase activities were higher in the patients serum than in that of the control group. The decrease of arylsulphatase and cathepsin D activities after surgery was statistically significant in both groups of patients, but the cathepsin D activity was still 3 times higher in patients than in those from the control group. The decrease of acid phosphatase activity after surgery was about 50% in both groups of patients and this decrease was statistically significant. The arylsulphatase and acid phosphatase activity in tumors was nearly 3 times higher in stage III patients than it was in stage II patients, but the cathepsin D activity was nearly the same in both patient groups. Higher lysosomal enzyme activity may be a useful factor in diagnosing and monitoring of lung cancer. However, further investigations are needed.

Unspecific inflammatory lesions of the urinary tract are known to be a vital question in urology and nephrology of our country and in foreign ones. Used in experiments were rats of mixed population. Lysosomal enzymes were studied in homogenates of the liver and contralateral kidney tissues and in the blood serum as well 1, 3, 6 days after simulation of the pathology experimental model. Activities were measured of such lysosomal enzymes as acid DNA-ase and RNA-ase, cathepsin, and acid phosphatase. Results of the studies made showed that in unspecific purulent affection of the kidneys there occurs an activation of acid blood hydrolases followed by their activation in the liver. The contralateral kidney, because of it being linked in functioning with the liver, remains relatively "inert" with respect to activation of lysosomal enzymes.

Cardiac and plasma activities of marker lysosomal enzymes were studied in Wistar rats with metabolic (epinephrine) and occlusion (ligation of coronary arteries) myocardial infarction. Activity of all examined lysosomal enzymes significantly increased in the myocardium and blood plasma starting from the first day after ligation of the coronary arteries and was accompanied by leukocytic infiltration of the myocardium. Enzyme activity gradually decreased to postoperation day 14. In metabolic infarction leukocytic infiltration and specific activity of lysosomal enzymes rose gradually and attained maximum to postoperation day 14, while the signs of labilization of lysosomal membranes appeared from the first postoperation day. Plasma activity of lysosomal enzymes in metabolic infarction increased smoothly and peaked on day 14.

Objective and Design: The role of a tetrapeptide derivative PEP 1261 {Boc-Lys(Boc)-Arg-Asp-Ser(tBu)-OtBu}, corresponding to residues 39-42 of human lactoferrin, has been tested in vitro in the modulation of neutrophil function., Material and Subjects: The level of non-enzymatic mediators of inflammation such as reactive oxygen species (ROS), enzymatic mediators such as myeloperoxidase (MPO) and lysosomal enzymes have been assessed in the presence or absence of PEP 1261 in phorbol 12-myristate 13 acetate (PMA) stimulated human neutrophils (n = 6) and also in neutrophils isolated from adjuvant induced arthritic rats (AIA) (n = 4)., Treatment: PEP 1261, at a concentration of 0.14 mM, was added to the neutrophil cultures., Statistical Method: The results were analysed by nonparametric statistics using Mann Whitney U test., Results: Addition of PEP 1261 effectively blocked the H2O2 and O2*- release, decreased the levels of MPO levels (p< 0.01) and lysosomal enzymes (p < 0.05) as compared to PMA stimulated human neutrophils. PEP 1261 was also observed to inhibit the levels of H2O2, O2*-, MPO and lysosomal enzymes (p < 0.05) as compared to PMA stimulated control rat neutrophils and neutrophils from arthritic rats., Conclusions: The results of this study indicate that PEP 1261 could serve as an excellent antiinflammatory agent.

Lysosomal acid hydrolases are thought to play an important role in inflammation associated with rheumatoid arthritis. A Siddha preparation of Semecarpus anacardium nut extract called Serankottai Nei was tested for its capacity to stabilize lysosomes obtained from liver and kidney of adjuvant-induced arthritic animals. Lysosomal membrane stability was measured by determining the release of acid hydrolases from the lysosomes. The drug was administered at a dose level of 150 mg/kg body weight for 14 days to arthritic animals after the adjuvant injection. The total and free activity of lysosomal enzymes were significantly increased in arthritic rats with concomitant increase in plasma levels of protein-bound carbohydrates. Significantly increased lysosomal membrane fragility as observed in arthritic condition was reduced in drug-treated animals. Antiarthritic activity of the drug through its stabilizing action on lysosomal membranes could be inferred from this study.

Lysosomal cathepsins D (CD), B (CB), and L (CL) serum levels were determined by immunoassays in patients with chronic (CHP) or acute (AP) pancreatitis and in patients with ductal pancreatic carcinoma (DPC) and correlated with some biological and clinical parameters of this tumor. CB serum concentrations significantly higher than those measured in healthy subjects (NS) were observed in CHP, AP, and DPC patients (p < 0.01). However, no significant difference was noted among these groups. Increased CL serum levels were evident only in cancer patients compared to NS, AP, or CHP groups (p < 0.05), while no difference was observed among these groups. Elevated CD serum values were observed in CHP and AP patients compared to healthy subjects or cancer patients (p < 0.01). In cancer patients no correlation between CD, CB, and CL and clinical stage or tumor size was found. However, significant correlations were observed only between serum CD and CA50 (p < 0.02) and between CD and CL (p < 0.05). No further relationship among the biochemical parameters examined was observed. The present data suggest that the different serum patterns of CD, CB, and CL in patients with pancreatitis and pancreatic cancer may be of clinical interest as additional biochemical parameters for the differential diagnosis of these diseases. However, further prospective clinical studies are needed to assess better their potential value as prognostic parameters to identify patients with pancreatitis at increased risk to develop pancreatic cancer.

Activity of lysosomal and nonlysosomal proteases and contents of protein and its degradation products in the blood serum of rats with methylcholantrene fibrosarcoma were evaluated. Activity of lysosomal proteases and prolidase and prolinase as well in the blood serum of rats with methylcholanthrene tumour did not differ from the activity of these enzymes in the blood serum of control rats. Only the activity of elastase and collagenase in the blood serum of rats with methylcholanthrene tumour especially with tumour of intermediate and big mass was increased. Content of total protein was decreased in the blood serum of rats with tumour of intermediate and big mass and contents of glycoproteins and alfa-amin nitrogen were increased in comparison to the blood serum of control rats.

Adult male Wistar rats were divided in 3 groups. In the first group, infrarenal abdominal aorta was occluded for 6 hours and reperfused thereafter. In the second group, the reperfusion was not made, and the third group underwent a sham operation. Lysosomal enzymatic activities were assessed in serum tissues. Lysosomal membrane fragilities were estimated also in these tissues. Finally, 14C-aminopyrine breath test (ABT) was studied to define the possible liver dysfunction caused by limb ischemia. As a result, release of lysosomal enzymes from ischemic muscle was confirmed in vitro experiments, and the increase in the serum was statistically significant in the first and second groups as compared to the third group. Particularly prominent was a marked elevation of cathepsin-D in the first group which was observed immediately after the release of occlusion. Results of liver lysosomal enzymes and ABT revealed significant cellular damages and depression of microsomal function of the liver both in the first and second groups. These studies suggest that lysosomal enzymes derived from ischemic muscle exert a possible toxicity on the liver, and liver damage thus resulted may play a roll on the pathogenesis of whole body injury associated with acute and critical lower limb ischemia.

Impairments in structural integrity of liver, heart and skeletal muscle lysosomes followed by necrotic and necrobiotic alterations in the tissues and secretion of active hydrolases in blood were detected under conditions of exhaustive physical exercises in rats when dose-dependent physical loading was studied. At the same time, in patients with hypertrophic cardiomyopathy physical loading, carried out as stepwise spiroveloergometry up to the submaximal heart rate, led to release of lysosomal enzymes into blood, which was not observed in healthy persons under similar conditions. The higher level of enzymes was found in circulation of the patients with most severe forms of the disease.

The dynamics of activity of lysosomal enzymes in the blood, morphometric indices in the parietal peritoneum was studied in 217 patients with acute diffuse peritonitis depending on the severity of the process. It was established that patients suffering of acute diffuse peritonitis through showing to a certain extent similar clinical picture differ, however, by their morphochemical indices. Comparing the activity of catepsin-D, relative specific volume of erythrocytes (V), density of distribution of polymorphonuclear leucocytes (N) it may be suggested that catepsin values over 16.9 ast. un (min, mg), V--over 0.4 conv. un., N over 4.04 conv. un indicate irreversible changes in the tissues.

Activities of acid and alkaline phosphatases, cathepsin B, leucine aminopeptidase, N-acetyl-beta-D-hexosaminidases, beta-D-galactosidase and beta-D-glucuronidase were studied in leukocytes of two groups of patients with normal and pathological healing of wounds after surgical treatment of scar stenosis of larynx. Analysis of the enzymatic activity, calculated by means of Student's test using the data of a single estimation of the activity in leukocytes before surgical treatment, did not exhibit any distinct differences in these two groups of patients. The study of interrelationship between the activities of individual enzymes by means of principles of regression analysis enabled to show that the enzymes studied were in the positive regressive relation. Pattern of enzymatic activity in leukocytes of patients with pathological wound healing was distinctly different from that of patients with normal healing in the shape of regression and, especially, in relaxation of the interrelations between phosphatases and other enzymes. The principle of regression enabled to evaluate the prognosis of postoperative development of wound healing using the preliminary estimation of enzymatic activity in leukocytes of patients with scar stenosis of larynx.

Casein-induced amyloidosis in hamsters was found to be of the AA-type, as shown by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and amino acid analysis of the major low-molecular weight component of the amyloid fibrils. Levels of serum amyloid A (SAA) and the activities of cathepsin D, beta-N-glucosaminidase, serine esterase, lactate dehydrogenase (LDH) and gamma glutamyl transpeptidase (GGT) were measured in the blood plasma during induction of amyloidosis. During the pre-amyloid phase an increase was observed in all these parameters. During the deposition of amyloid, an increase was observed in the activities of the lysosomal enzymes cathepsin D and beta-N-glucosaminidase, which was significantly correlated with amyloid deposition. Serine esterase activities did not show any relationship to amyloid deposition. LDH and GGT activities were normal in the amyloid phase. SAA levels were lower during amyloid deposition than during the pre-amyloid phase. These findings indicate that a specific release of lysosomal contents from mononuclear phagocytic cells is involved in the pathogenesis of AA-amyloidosis. Amyloid deposition may be the result of: (i) extrusion of intralysosomal protein AA or pre-amyloid, followed by extracellular formation of amyloid fibrils; (ii) secretion of lysosomal enzymes, followed by extracellular cleavage of SAA and subsequent aggregation of protein AA with other components.