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1.
Molecules ; 26(4)2021 Feb 17.
Article in English | MEDLINE | ID: mdl-33671275

ABSTRACT

Oregano (Origanum vulgare L.) and thyme (Thymus vulgaris L.) have long been known for their organoleptic properties. Both plants are widely used in cuisine worldwide in fresh and dried form and as a pharmaceutical raw material. The study aimed to assess if the type of cultivation influenced chosen chemical parameters (total polyphenols by Folin-Ciocalteu method; carotenoids and chlorophyll content by Lichtenthaler method), antimicrobial activity (with chosen reference microbial strains) and shaped cytotoxicity (with L929 mouse fibroblasts cell line) in water macerates of dry oregano and thyme. Polyphenols content and antimicrobial activity were higher in water macerates obtained from conventional cultivation (independently from herb species), unlike the pigments in a higher amount in macerates from organic herbs cultivation. Among all tested macerates stronger antimicrobial properties (effective in inhibiting the growth of Pseudomonas aeruginosa, Bacillus cereus and Salmonella enteritidis) and higher cytotoxicity (abilities to diminish the growth of L929 fibroblasts cytotoxicity) characterized the conventionally cultivated thyme macerate.


Subject(s)
Agriculture , Carotenoids/analysis , Chlorophyll/analysis , Phenols/analysis , Water/chemistry , Animals , Anti-Infective Agents/pharmacology , Bacteria/drug effects , Cell Death/drug effects , Cell Line , Mice , Microbial Sensitivity Tests , Origanum/chemistry , Plant Extracts , Polyphenols/analysis , Thymus Plant/chemistry
2.
Skin Pharmacol Physiol ; 32(3): 125-131, 2019.
Article in English | MEDLINE | ID: mdl-30904911

ABSTRACT

BACKGROUND/AIMS: Analysis of the relationship between the estradiol blood concentration and the skin moisture, pore width, discoloration and smoothness in differently aged women on the 5th and 25th days of the menstrual cycle. METHODS: The study involved 57 women divided into 4 age groups. Measurements of skin moisture, pore width, discoloration and smoothness were performed using the Aramo SG Aram Huvis device. The estradiol serum concentration was determined by radioimmunoassay. RESULTS: In the luteal phase of the cycle, facial skin moisture increases from 93.5% of the correct standard moisture index in the youngest to 115.5% in the oldest group. A positive correlation (r2 = 0.45) between estradiol concentration and skin moisture was observed on the 5th day of the cycle in 40- to 50-year-olds. For women on the 25th day of the menstruation cycle, estrogen concentration below the normal range was more beneficial for skin smoothness and pore width for the oldest group. The difference was not statistically significant (p > 0.05); how-ever, in the 40- to 50-year age group, skin smoothness was much better (43.5 ± 6.7%) for low estradiol while it was 37.5 ± 4.7% in the 20- to 29-year age group. Similarly, in the 40- to 50-year age group, skin pore width was much smaller (35.2 ± 15.7%) for low estradiol while it was 54.3 ± 28.8% in the 20- to 29-year age group. CONCLUSIONS: Skin moisture was related to the concentration of estradiol only in the oldest examined group of women regardless of the phase of menstrual cycle. In the 40- to 50-year-old group of women, the low level of estradiol on the 25th day of the cycle is better used to maintain a good facial skin appearance and has a positive influence not only on skin moisture, but also on pore width and skin smoothness.


Subject(s)
Estradiol/blood , Menstrual Cycle/blood , Skin/chemistry , Adolescent , Adult , Color , Face , Female , Humans , Middle Aged , Porosity , Surface Properties , Water/analysis , Young Adult
3.
Acta Neuropsychiatr ; 28(1): 38-44, 2016 Feb.
Article in English | MEDLINE | ID: mdl-26286703

ABSTRACT

BACKGROUND: It has been reported that lithium may inhibit lipid peroxidation and protein oxidation. Lithium salts also appear to stimulate cell proliferation, increase neurogenesis, and delay cell death. Oxidative stress and neurodegeneration may play an important role in the pathophysiology of bipolar disorder and the disease course thereof. The aim of this research is to estimate the influence of lithium (alone and in combination with haloperidol) on the parameters of oxidative stress and viability of SH-SY5Y cell lines in neutral and pro-oxidative conditions. METHODS: The evaluated oxidative stress parameter was lipid peroxidation. The viability of the cell lines was measured utilising the MTT test. RESULTS: In neutral conditions, higher levels of thiobarbituric acid reactive substances were observed in those samples which contained both haloperidol and lithium than in other samples. However, these differences were not statistically significant. Cell viability was significantly higher in therapeutic lithium samples than in the controls; samples of haloperidol alone as well as those of haloperidol with lithium did not differ from controls. CONCLUSIONS: The results of our study may indicate that lithium possess neuroprotective properties that may be partly due to antioxidative effects. The combination of lithium and haloperidol may generate increased oxidative stress.


Subject(s)
Antipsychotic Agents/pharmacology , Haloperidol/pharmacology , Lithium Compounds/pharmacology , Oxidative Stress/drug effects , Animals , Bipolar Disorder/drug therapy , Bipolar Disorder/metabolism , Bipolar Disorder/physiopathology , Cell Death/drug effects , Cell Line, Tumor , Cell Survival/drug effects , Humans , Lipid Peroxidation/drug effects , Neuroblastoma/metabolism , Neuroblastoma/pathology , Neurogenesis/drug effects , Oxidation-Reduction , Thiobarbituric Acid Reactive Substances/metabolism
4.
Redox Rep ; 21(1): 45-49, 2016 Jan.
Article in English | MEDLINE | ID: mdl-26193071

ABSTRACT

OBJECTIVES: Lithium may inhibit lipid peroxidation (LP) and protein oxidation, stimulate cell proliferation, increase neurogenesis, and delay cell death. Oxidative stress (OxS) is a state of imbalance between oxidative processes and antioxidant defenses, which may play an important role in the pathophysiology and disease course of bipolar disorder (BD). The aim of this study was to estimate the influence of lithium, administered alone or in combination with haloperidol, on selected OxS parameters in human plasma in vitro. METHODS: The OxS parameters evaluated were thiobarbituric acid reactive substances (TBARS) and total antioxidant capacity (TAC). Plasma samples from healthy volunteers were incubated with drug concentrations used in psychiatry. RESULTS: Incubation of plasma with lithium or haloperidol alone did not produce statistically significant changes of TBARS levels in comparison with control samples. However, significantly higher TBARS levels were observed in samples incubated with haloperidol plus lithium compared to control, haloperidol, or lithium samples. The TAC value did not differ between samples. CONCLUSIONS: Lithium does not influence OxS parameters in human plasma in vitro during short-term observation when applied at concentrations used in psychiatry. However, lithium increased the TBARS level in the samples when given in combination with haloperidol, which may be one of the mechanisms behind the neurotoxicity associated with combined lithium and haloperidol administration.

5.
Protein J ; 34(5): 338-48, 2015 Oct.
Article in English | MEDLINE | ID: mdl-26341972

ABSTRACT

Proteases are essential for tumour progression and many are over-expressed during this time. The main focus of research was the role of these proteases in degradation of the basement membrane and extracellular matrix (ECM), thereby enabling metastasis to occur. Cancer procoagulant (CP), a protease present in malignant tumours, but not normal tissue, is a known activator of coagulation factor X (FX). The present study investigated the function of CP in cancer progression by focussing on its enzymatic specificity. FX cleavage was confirmed using SDS-PAGE and MALDI-TOF MS and compared to the proteolytic action of CP on ECM proteins, including collagen type IV, laminin and fibronectin. Contrary to previous reports, CP cleaved FX at the conventional activation site (between Arg-52 and Ile-53). Additionally, degradation of FX by CP occurred at a much slower rate than degradation by conventional activators. Complete degradation of the heavy chain of FX was only visible after 24 h, while degradation by RVV was complete after 30 min, supporting postulations that the procoagulant function of CP may be of secondary importance to its role in cancer progression. Of the ECM proteins tested, only fibronectin was cleaved. The substrate specificity of CP was further investigated by screening synthetic peptide substrates using a novel direct CP assay. The results indicate that CP is not essential for either cancer-associated blood coagulation or the degradation of ECM proteins. Rather, they suggest that this protease may be required for the proteolytic activation of membrane receptors.


Subject(s)
Cysteine Endopeptidases/metabolism , Neoplasm Proteins/metabolism , Neoplasms/metabolism , Amino Acid Sequence , Collagen Type IV/metabolism , Cysteine Endopeptidases/chemistry , Enzyme Activation , Extracellular Matrix/metabolism , Fibronectins/chemistry , Fibronectins/metabolism , Humans , Kinetics , Laminin/metabolism , Molecular Sequence Data , Neoplasm Metastasis , Neoplasm Proteins/chemistry , Neoplasms/enzymology , Neoplasms/pathology , Proteolysis , Substrate Specificity
6.
Contemp Oncol (Pozn) ; 19(2): 108-12, 2015.
Article in English | MEDLINE | ID: mdl-26034387

ABSTRACT

THE AIM OF THE STUDY: To analyze human breast cancer cell line MCF-7 and human malignant melanoma cell line WM-115 in order to characterize the cellular expression of CP and to evaluate whether ATO may affect this activity, as well as the viability of the cells. MATERIAL AND METHODS: The inhibitory effect of arsenic trioxide on the proliferation of MCF-7 and WM-115 cells were measured with MTT test. The activity of cancer procoagulant after ATO exposure was determined by a specific three-stage chromogenic assay. RESULTS: ATO decreased the CP activity in a dose- and time-dependent manner in MCF-7 cells with no effect on cell proliferation at the same time. However, it affected the CP activity of WM-115 cells in a different way. Reduction in CP activity was followed by an increase after 48 h incubation. The cells viability results showed dose-and time-correlated response within high arsenic concentrations. CONCLUSIONS: Arsenic trioxide downregulates the CP expression in human breast cancer and melanoma cells.

7.
Postepy Hig Med Dosw (Online) ; 67: 817-27, 2013 Aug 06.
Article in Polish | MEDLINE | ID: mdl-24018447

ABSTRACT

Arsenic trioxide (As2O3) has recently been identified as an effective drug in different types of cancer therapy. It is a useful pharmacological agent in acute promyelocytic leukemia (APL) treatment, especially the form that is resistant to conventional chemotherapy with all-trans retinoic acid (ATRA). What is more, laboratory data suggest that As2O3 is also active when it comes to several solid tumor cell lines. However, the mechanism of action is not fully understood. As2O3 in high doses triggers apoptosis, while in lower concentrations it induces partial differentiation. The As2O3 mechanism of action involves effects on mitochondrial transmembrane potential which lead to apoptosis. It also acts on the activity of JNK kinase, glutathione, caspases, NF-ĸB nuclear factor or pro- and antiapoptotic proteins. This publication presents the current knowledge about the influence of arsenic trioxide in cancer cells.


Subject(s)
Antineoplastic Agents/pharmacology , Arsenicals/pharmacology , Leukemia, Promyelocytic, Acute/drug therapy , Neoplasms/drug therapy , Oxides/pharmacology , Apoptosis/drug effects , Apoptosis Regulatory Proteins/drug effects , Apoptosis Regulatory Proteins/metabolism , Arsenic Trioxide , Caspases/drug effects , Caspases/metabolism , Cell Differentiation/drug effects , Cell Line, Tumor , Drug Resistance, Neoplasm , Humans , Leukemia, Promyelocytic, Acute/pathology , MAP Kinase Kinase 4/drug effects , MAP Kinase Kinase 4/metabolism , Mitochondria/drug effects , NF-kappa B/drug effects , NF-kappa B/metabolism , Neoplasms/pathology
8.
Postepy Hig Med Dosw (Online) ; 64: 284-90, 2010 Jun 09.
Article in Polish | MEDLINE | ID: mdl-20558866

ABSTRACT

Retinoids are useful pharmacological agents in therapy and prevention of cancer. All-trans retinoic acid (ATRA) is applied in chemoprevention and differentiation therapy of some cancers with particularly impressive results in the management of acute promyelocytic leukemia (APL). ATRA plays a major role in regulating growth and differentiation of a wide variety of normal and malignant cell types. ATRA mediates these effects by regulating gene transcription. Nuclear retinoic acid receptors (RARs) are considered to be the mediators of most of the effects of ATRA on gene expression. We present a current state of knowledge on the effects of ATRA on cell growth and differentiation as well as describe RARs and their role in the cellular mechanism of ATRA action. A particular attention was paid to the effects of ATRA on proliferation and differentiation of cancer cells.


Subject(s)
Antineoplastic Agents/pharmacology , Neoplasms/drug therapy , Neoplasms/prevention & control , Tretinoin/pharmacology , Antineoplastic Agents/therapeutic use , Humans , Tretinoin/therapeutic use
9.
Thromb Res ; 124(3): 364-7, 2009 Jul.
Article in English | MEDLINE | ID: mdl-19419757

ABSTRACT

Neoplastic cells produce procoagulants responsible for hypercoagulation states frequently observed in cancer patients. It is accepted that two major procoagulants from malignant tissue are tissue factor (TF) and a direct activator of coagulation factor X called cancer procoagulant (CP). Direct factor X-activating activity of cultured human malignant melanoma WM 115 cells has been analyzed in the cell extracts, whole cells and in the medium after the cell culture. The factor X-activating activity was detected in the malignant cell lysates but not in the cultured medium or intact malignant cells. The lysates contained no TF as determined by Western blotting and enzyme-linked immunosorbent assay (ELISA) using anti-TF monoclonal antibody. The enzymatic characteristics of the activity was typical for CP. The results suggest that cancer procoagulant is an intracellular protein.


Subject(s)
Cysteine Endopeptidases/metabolism , Factor X/metabolism , Melanoma/metabolism , Neoplasm Proteins/metabolism , Thromboplastin/metabolism , Animals , Cell Line, Tumor
10.
Blood Coagul Fibrinolysis ; 20(5): 315-20, 2009 Jul.
Article in English | MEDLINE | ID: mdl-19448531

ABSTRACT

Additional carboxylation of glutamic acid by vitamin K-dependent gamma-carboxylase is a common posttranslational modification of many proteins, including some of blood clotting factors. Vitamin K-antagonists, such as warfarin, are often included in the therapy of malignant disease, decreasing the blood coagulation potential. Cancer procoagulant, a direct blood coagulation factor X activator from malignant tissue, is considered as a vitamin K-dependent protein, so it could serve as one of possible targets for the therapy with warfarin. However, there is still no experimental data demonstrating directly the presence of gamma-carboxyglutamic acid (Gla) in a cancer procoagulant molecule. The presence of Gla in cancer procoagulant isolated from human amnion-chorion membranes and from human malignant melanoma WM 115 cell line was analyzed directly, using specific anti-Gla monoclonal antibodies. There was no detectable amount of Gla in cancer procoagulant isolated from fetal or malignant tissue. Cancer procoagulant from human tissues does not contain Gla-rich domain. The finding indicates that cancer procoagulant is rather a poor target for warfarin therapy of malignant disease.


Subject(s)
1-Carboxyglutamic Acid/analysis , Amnion/enzymology , Chorion/enzymology , Cysteine Endopeptidases/chemistry , Melanoma/enzymology , Neoplasm Proteins/chemistry , 1-Carboxyglutamic Acid/immunology , Antibodies, Monoclonal/immunology , Anticoagulants/pharmacology , Cell Line, Tumor/enzymology , Cysteine Endopeptidases/pharmacology , Enzyme Activation/drug effects , Factor X/drug effects , Female , Humans , Melanoma/pathology , Neoplasm Proteins/pharmacology , Pregnancy , Warfarin/pharmacology
11.
Comp Med ; 58(3): 282-6, 2008 Jun.
Article in English | MEDLINE | ID: mdl-18589871

ABSTRACT

Two common procoagulant activities associated with tumors are tissue factor and cancer procoagulant (CP), an activator of coagulation factor X. We have identified a convenient source of CP in transplanted Lobund-Wistar rat PA3 prostate tumors. CP activity was purified from 5 independent transplanted prostate tumors by column chromatography. The protein activated factor X in the absence of TF and factor VII. An antihuman CP antibody recognized rat CP in an ELISA and inactivated CP activity in a chromogenic assay. Lobund-Wistar prostate tumors may provide a convenient animal model useful in determining the role of CP in cancer development.


Subject(s)
Cysteine Endopeptidases/metabolism , Factor X/metabolism , Neoplasm Proteins/metabolism , Prostatic Neoplasms/metabolism , Animals , Enzyme-Linked Immunosorbent Assay , Male , Prostatic Neoplasms/pathology , Rats , Rats, Wistar
12.
Cancer Lett ; 222(1): 89-94, 2005 May 10.
Article in English | MEDLINE | ID: mdl-15837545

ABSTRACT

Cancer procoagulant (CP) is a cysteine protease produced by fetal and malignant tissues, activating in vitro blood coagulation factor X. It has been demonstrated that CP is able to stimulate blood platelet adhesion to fibrinogen and collagen. The pro-adhesive properties of CP could play an important role in metastatic spread of cancer as well as in primary tumor growth. Effects of anti-CP antibody on the growth of MCF-7 breast cancer cells and on the cells adhesion to vitronectin have been analyzed in vitro. Addition of polyclonal anti-CP antibody to MCF-7 cell culture resulted in 16-18% (P < 0.001) decrease in the cells viability as compared with the control (other antibody or no antibody in the culture). Preincubation of MCF-7 cells with anti-CP antibody reduced the cells adhesion to vitronectin. Further addition of purified CP (0.5-8 microg/ml) to the MCF-7 cells preincubated with anti-CP antibody resulted in complete recovery of adhesive properties of the cells. However, when high concentration (16 microg/ml) of CP was added to the sample, only partial recovery of the adhesive properties by the cells was observed. Results of the experiments support the hypothesis that CP is involved in the growth of cancer cells, but its pro-coagulative properties are of secondary importance. One of the possible mechanisms of the interactions between CP and malignant cell could be the regulation of the cell adhesion processes.


Subject(s)
Antibodies/pharmacology , Cell Adhesion/drug effects , Cell Survival/drug effects , Cysteine Endopeptidases/immunology , Growth Inhibitors/pharmacology , Neoplasm Proteins/immunology , Vitronectin/metabolism , Cell Adhesion/immunology , Cell Line, Tumor , Cell Survival/immunology , Humans , Vitronectin/immunology
13.
Arch Biochem Biophys ; 428(2): 131-5, 2004 Aug 15.
Article in English | MEDLINE | ID: mdl-15246868

ABSTRACT

Cancer procoagulant (CP) and tissue factor (TF; only in complex with Factor VIIa (FVIIa)) can activate FX to FXa. Controversy still exists whether or not CP is an entity different from TF, or whether CP activity is due to contamination of CP preparations with TF/FVIIa complex. We therefore looked for proteins in CP preparations that were detected by anti-TF antibodies and then sequenced these proteins. One- and two-dimensional gels of CP and TF were used to identify proteins immunoreactive to monoclonal anti-CP and anti-TF antibodies (Mabs). Those proteins in the CP preparation recognized by anti-TF antibodies were sequenced. Angiotensinogen precursor, alpha-1-antitrypsin precursor, and vitamin D-binding protein were identified along with one so far unidentified sequence; however, no TF-sequences were identified. Also, no proteins with the correct molecular weight for TF were identified using anti-TF antibodies. It seems possible that CP preparations contain proteins that have some epitopes similar to the epitopes recognized in TF by anti-TF Mab. However, these proteins do neither have the molecular weight nor the amino acid sequence of TF.


Subject(s)
Coagulants/pharmacology , Cysteine Endopeptidases/pharmacology , Neoplasm Proteins/pharmacology , Proteins/chemistry , Thromboplastin/immunology , Angiotensinogen/chemistry , Antibodies, Monoclonal/chemistry , Blotting, Western , Chromatography , Electrophoresis, Gel, Two-Dimensional , Electrophoresis, Polyacrylamide Gel , Factor X/chemistry , Humans , Recombinant Proteins/chemistry , Thromboplastin/chemistry , Vitamin D-Binding Protein/chemistry , alpha 1-Antitrypsin/chemistry , alpha 1-Antitrypsin/metabolism
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