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1.
Int J Mol Sci ; 23(15)2022 Aug 02.
Artigo em Inglês | MEDLINE | ID: mdl-35955735

RESUMO

Abnormal glycosylation of cancer cells is considered a key factor of carcinogenesis related to growth, proliferation, migration and invasion of tumor cells. Many plant-based polyphenolic compounds reveal potential anti-cancer properties effecting cellular signaling systems. Herein, we assessed the effects of phenolic acid, p-coumaric acid and flavonoids such as kaempferol, astragalin or tiliroside on expression of selected cancer-related glycoforms and enzymes involved in their formation in AGS gastric cancer cells. The cells were treated with 80 and 160 µM of the compounds. RT-PCR, Western blotting and ELISA tests were performed to determine the influence of polyphenolics on analyzed factors. All the examined compounds inhibited the expression of MUC1, ST6GalNAcT2 and FUT4 mRNAs. C1GalT1, St3Gal-IV and FUT4 proteins as well as MUC1 domain, Tn and sialyl T antigen detected in cell lysates were also lowered. Both concentrations of kaempferol, astragalin and tiliroside also suppressed ppGalNAcT2 and C1GalT1 mRNAs. MUC1 cytoplasmic domain, sialyl Tn, T antigens in cell lysates and sialyl T in culture medium were inhibited only by kaempferol and tiliroside. Nuclear factor NF-κB mRNA expression decreased after treatment with both concentrations of kaempferol, astragalin and tiliroside. NF-κB protein expression was inhibited by kaempferol and tiliroside. The results indicate the rationality of application of examined polyphenolics as potential preventive agents against gastric cancer development.


Assuntos
Quempferóis , Neoplasias Gástricas , Ácidos Cumáricos , Flavonoides/farmacologia , Fucosiltransferases , Humanos , Quempferóis/farmacologia , NF-kappa B/metabolismo , Neoplasias Gástricas/patologia
2.
Nutrients ; 14(8)2022 Apr 07.
Artigo em Inglês | MEDLINE | ID: mdl-35458096

RESUMO

The ageing of the population is resulting in neurodegenerative diseases, including Alzheimer's disease (AD), which are an increasing social, economic and medical problem. Diet and physical activity are now considered as important modifiable factors that help prevent or delay the development of AD and other dementia-related diseases. The pyramid of healthy nutrition and lifestyle is a way of presenting the principles, the implementation of which gives a chance for proper development and a long healthy life. The basis of the pyramid, in the first place, is physical activity. Our review of the literature in the PubMed database supports the hypothesis that complementary factors, such as proper diet, physical exercise and mental activity, have a positive impact on the prevention of neurodegenerative diseases. The nutritional recommendations for healthy adults primarily include the consumption of vegetables, fruits, cereals, legumes, vegetable oils and fishes. Therefore, the introduction of Mediterranean and Asian diets may reduce the risk of the neurodegenerative diseases associated with dementia, whereas dairy products and meat-the main sources of L-carnitine-should be consumed in moderate amounts. The aim of our work is to provide up-to-date knowledge about the appropriate dietary model and healthy lifestyle elements and their impact on good health and the long life of people.


Assuntos
Doença de Alzheimer , Doença de Alzheimer/epidemiologia , Doença de Alzheimer/prevenção & controle , Dieta , Exercício Físico , Estilo de Vida Saudável , Humanos , Estilo de Vida , Verduras
3.
J Clin Med ; 10(6)2021 Mar 13.
Artigo em Inglês | MEDLINE | ID: mdl-33805796

RESUMO

L-carnitine plays an important role in the functioning of the central nervous system, and especially in the mitochondrial metabolism of fatty acids. Altered carnitine metabolism, abnormal fatty acid metabolism in patients with autism spectrum disorder (ASD) has been documented. ASD is a complex heterogeneous neurodevelopmental condition that is usually diagnosed in early childhood. Patients with ASD require careful classification as this heterogeneous clinical category may include patients with an intellectual disability or high functioning, epilepsy, language impairments, or associated Mendelian genetic conditions. L-carnitine participates in the long-chain oxidation of fatty acids in the brain, stimulates acetylcholine synthesis (donor of the acyl groups), stimulates expression of growth-associated protein-43, prevents cell apoptosis and neuron damage and stimulates neurotransmission. Determination of L-carnitine in serum/plasma and analysis of acylcarnitines in a dried blood spot may be useful in ASD diagnosis and treatment. Changes in the acylcarnitine profiles may indicate potential mitochondrial dysfunctions and abnormal fatty acid metabolism in ASD children. L-carnitine deficiency or deregulation of L-carnitine metabolism in ASD is accompanied by disturbances of other metabolic pathways, e.g., Krebs cycle, the activity of respiratory chain complexes, indicative of mitochondrial dysfunction. Supplementation of L-carnitine may be beneficial to alleviate behavioral and cognitive symptoms in ASD patients.

4.
Biomed Rep ; 14(2): 19, 2021 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-33335725

RESUMO

Luteolin is a natural flavonoid possessing certain beneficial pharmacological properties, including anti-oxidant, anti-inflammatory, anti-microbial and anti-cancer properties. The majority of types of gastric cancer with chronic gastritis are caused by infection with Helicobacter pylori (H. pylori). The present study evaluated the effect of luteolin on a number of selected factors that are potentially involved in gastric cancer development. The study was performed using gastric cancer CRL-1739 cells treated with 30 µM luteolin and H. pylori alone or combined. ELISA and reverse transcription PCR were used to assess the expression levels of MUC1, GalNAcα-R (Tn antigen) and NeuAcα2-3Galß1-3GalNAc-R (sT antigen), ADAM-17, IL-8, IL-10 and NF-κB. H. pylori and luteolin independently and in combination significantly reduced the expression levels of the extracellular domain of MUC1 in gastric cancer cells compared with the untreated control cells. ADAM-17 expression was reduced by treatment with the pathogen and luteolin. Additionally, both factors reduced sT antigen expression. Treatment with 30 ≤M luteolin significantly induced IL-8 expression at the mRNA and protein level, and the mRNA expression levels of IL-10 and NF-κB compared with the control. Both H. pylori and luteolin induced IL-8 protein expression. The present preliminary results suggest that luteolin may be used to treat patients with gastric cancer.

5.
Nutrients ; 12(7)2020 Jul 03.
Artigo em Inglês | MEDLINE | ID: mdl-32635400

RESUMO

The prevention or alleviation of neurodegenerative diseases, including Alzheimer's disease (AD), is a challenge for contemporary health services. The aim of this study was to review the literature on the prevention or alleviation of AD by introducing an appropriate carnitine-rich diet, dietary carnitine supplements and the MIND (Mediterranean-DASH Intervention for Neurodegenerative Delay) diet, which contains elements of the Mediterranean diet and the Dietary Approaches to Stop Hypertension (DASH) diet. L-carnitine (LC) plays a crucial role in the energetic metabolism of the cell. A properly balanced diet contains a substantial amount of LC as well as essential amino acids and microelements taking part in endogenous carnitine synthesis. In healthy people, carnitine biosynthesis is sufficient to prevent the symptoms of carnitine deficiency. In persons with dysfunction of mitochondria, e.g., with AD connected with extensive degeneration of the brain structures, there are often serious disturbances in the functioning of the whole organism. The Mediterranean diet is characterized by a high consumption of fruits and vegetables, cereals, nuts, olive oil, and seeds as the major source of fats, moderate consumption of fish and poultry, low to moderate consumption of dairy products and alcohol, and low intake of red and processed meat. The introduction of foodstuffs rich in carnitine and the MIND diet or carnitine supplementation of the AD patients may improve their functioning in everyday life.


Assuntos
Doença de Alzheimer/prevenção & controle , Carnitina/administração & dosagem , Dieta Saudável/métodos , Suplementos Nutricionais , Ingestão de Alimentos/fisiologia , Idoso , Idoso de 80 Anos ou mais , Dieta Mediterrânea , Abordagens Dietéticas para Conter a Hipertensão , Feminino , Humanos , Masculino , Pessoa de Meia-Idade
6.
Adv Clin Exp Med ; 27(6): 807-811, 2018 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-29790696

RESUMO

BACKGROUND: The carbohydrates of gastric mucins and other sugar structures are involved in interactions with Helicobacter pylori (H. pylori) adhesins. The binding of bacteria to mucins can protect the epithelium from direct contact with the pathogen and from developing infection because of a specific barrier created by the mucus. The pathogen also interacts with other carbohydrate structures of the epithelium. Direct contact between the bacteria and the epithelial cells facilitates infection development. OBJECTIVES: The aim of this study was to assess the influence of Maackia amurensis (MAA), Lotus tetragonolobus (LTA), Ulex europaeus (UEA), and Arachis hypogaea (PNA) lectins on the binding of gastric carbohydrates with H. pylori adhesins. MATERIAL AND METHODS: Three patients' gastric juices and 12 H. pylori strains were included in the study. An ELISA test was used to assess the presence of MUC1 and MUC5AC mucins and the sugar structures recognized by all examined lectins. The binding of the bacterium to the sugar structures was analyzed by the ELISA method with and without the gastric juices pretreated with lectins. RESULTS: In the majority of the samples examined, MAA, LTA, UEA, and PNA lectins enhanced the binding of H. pylori to specific carbohydrate structures of gastric mucins. CONCLUSIONS: Substances which influence the binding of the pathogen with specific carbohydrate receptors on gastric epithelial cells can favor inflammation development. However, if H. pylori binds with mucins, the bacterium can have difficulty reaching the epithelium and progressing with infection.


Assuntos
Aderência Bacteriana/fisiologia , Mucinas Gástricas/metabolismo , Infecções por Helicobacter/metabolismo , Helicobacter pylori/metabolismo , Lectinas de Plantas/metabolismo , Arachis/metabolismo , Carboidratos/química , Mucosa Gástrica/química , Mucosa Gástrica/metabolismo , Interações Hospedeiro-Patógeno/fisiologia , Humanos , Lectinas/metabolismo , Maackia/metabolismo
7.
Adv Med Sci ; 63(1): 205-211, 2018 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-29197783

RESUMO

PURPOSE: Attachment of Helicobacter pylori to the mucous epithelial cells and the mucous layer is said to be a crucial step for infection development. Sugar antigens of gastric mucins (MUC5AC, MUC1) can act as receptors for bacterial adhesins. The aim of the study was to investigate if Lotus tetragonolobus and Maackia amurensis lectins influence the level of MUC1, MUC5AC, Lewis b, H type 1, sialyl Lewis x, phospho-IκBα and interleukin 8 in Helicobacter pylori infected gastric cancer cells. MATERIALS AND METHODS: The study was performed with one clinical H. pylori strain and CRL-1739 gastric cancer cells. To assess the levels of mentioned factors immunosorbent ELISA assays were used. RESULTS: Coculture of cells with bacteria had no clear effect on almost all examined structures. After coculture with H. pylori and lectins, a decrease of the level of both mucins, Lewis b and H type 1 antigens was observed. Lectins addition had no effect on sialyl Lewis x. Maackia amurensis caused slight increase of phospho-IκBα while interleukin 8 level was decreased. CONCLUSIONS: Lotus tetragonolobus and Maackia amurensis lectins can mediate in binding of Helicobacter pylori to gastric epithelium.


Assuntos
Antígenos Glicosídicos Associados a Tumores/metabolismo , Helicobacter pylori/fisiologia , Interleucina-8/metabolismo , Lectinas/uso terapêutico , Lotus/química , Maackia/química , Inibidor de NF-kappaB alfa/metabolismo , Neoplasias Gástricas/tratamento farmacológico , Neoplasias Gástricas/microbiologia , Linhagem Celular Tumoral , Helicobacter pylori/efeitos dos fármacos , Humanos , Lectinas/farmacologia , Mucinas/metabolismo , Fosforilação/efeitos dos fármacos
8.
Acta Biochim Pol ; 64(3): 465-470, 2017.
Artigo em Inglês | MEDLINE | ID: mdl-28742884

RESUMO

Cancer cells are characterized by an aberrant increase in protein N-glycosylation and by disruption of E-cadherin-mediated adherens junctions. However, the relationship between alterations in N-glycosylation process and loss of E-cadherin adhesion in cancer remains unclear. The mechanisms of altered expression of adhesive glycoproteins in cancer cells have not been fully elucidated. Thus, the aim of this study was to examine the expression of E-cadherin and sialyl Lewisa/x, NeuAcα2-3Gal, NeuAcα2-6Gal/GalNAc structures in the normal renal tissue and intermediate and cancerous tissues from patients with clear cell RCC. Moreover, we attempted to correlate the E-cadherin expression with some specific sugar residues of renal cancer tissue glycoproteins. The expression of E-cadherin was analysed using ELISA test and immunoblotting. Oligosaccharide structures and sialylation level were detected with ELISA test using specific biotinylated lectins or antibodies. A significant decrease of E-cadherin expression as well as a significant increase in sialylated oligosaccharides level in intermediate zone and renal cancer tissue in comparison to normal renal tissue are reported. Significant decrease in expression of cadherins and increase in sialylation of oligosaccharide structures in renal cancer tissue in comparison to normal renal tissue, and in renal cancer tissue in comparison to intermediate zone of renal tissue, are important for the future research concerning detection and quantification of cadherins and sialylated oligosaccharide structures in urine and cells of urinary sediment as possible non-invasive marker of early RCC.


Assuntos
Caderinas/metabolismo , Carcinoma de Células Renais/metabolismo , Neoplasias Renais/metabolismo , Acetilglucosamina/metabolismo , Idoso , Antígenos CD , Carcinoma de Células Renais/patologia , Feminino , Glicoconjugados/metabolismo , Glicoproteínas/metabolismo , Humanos , Rim/metabolismo , Neoplasias Renais/patologia , Antígenos CD15/metabolismo , Masculino , Pessoa de Meia-Idade , Valores de Referência , Ácidos Siálicos/metabolismo
9.
Mol Cell Biochem ; 417(1-2): 35-47, 2016 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-27160935

RESUMO

Cancer cells have developed a number of adaptation mechanisms involving the signal activation of the transduction pathways, which promotes the progression and metastasis. Our results showed that the percentage of apoptotic MCF-7 cells incubated in the low glucose medium for 48 h was lower in comparison to those cultured in the high glucose medium, despite the high expression of the proapoptotic transcription factor-CHOP. Furthermore, the MCF-7 cells incubated in the low glucose medium for 48 h showed a higher expression of NF-κB p100/p52 subunits compared to cells incubated in the high glucose medium. Moreover, our findings demonstrated that the shortage of glucose strongly induces autophagy in MCF-7 cells. The activation of this process is not associated with the changes in the expression of mTOR kinase. We suggest, that the antiapoptotic chaperone ORP150 induction, transcription factor NF-κB2 activation, and increased autophagy constitute mechanisms protecting the MCF-7 cells against apoptosis.


Assuntos
Apoptose , Autofagia , Neoplasias da Mama/metabolismo , Glucose/metabolismo , Neoplasias da Mama/genética , Neoplasias da Mama/patologia , Feminino , Glucose/genética , Proteínas de Choque Térmico HSP70/genética , Proteínas de Choque Térmico HSP70/metabolismo , Humanos , Células MCF-7 , Subunidade p52 de NF-kappa B/genética , Subunidade p52 de NF-kappa B/metabolismo , Proteínas de Neoplasias/genética , Proteínas de Neoplasias/metabolismo , Serina-Treonina Quinases TOR/genética , Serina-Treonina Quinases TOR/metabolismo , Fator de Transcrição CHOP/genética , Fator de Transcrição CHOP/metabolismo
10.
Clin Exp Nephrol ; 19(4): 732-7, 2015 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-25091456

RESUMO

BACKGROUND: Changes in expression patterns of the sialyl Lewis antigens and MUC1 mucin can be considered as markers for the diagnosis of various cancers. However, there are no reports which have been devoted to analysis of differences in the sialyl Lewis antigens and MUC1 expression patterns as potential discrimination markers among different areas of clear cell renal cell carcinoma (ccRCC). The aim of this study was to determine the level of MUC1 and specific Lewis antigens on glycoproteins in three different areas: tumor (cancer tissue), intermediate zone (adjacent to tumor tissue) and normal renal cortex/medulla (uninvolved by tumor). METHODS: Study was performed on renal tissues taken from 30 patients with clear cell renal cell carcinoma. Relative amounts of sugar structures bound with proteins were determined by ELISA-like test with biotinylated lectins or monoclonal antibodies: anti-MUC1 and anti-sialyl Lewis(a/x). The study presented here provides novel information about relationship between MUC1 and sialyl Lewis antigens in the tumor, intermediate zone and noninvolved areas of normal renal tissue distant of tumor. RESULTS: We have found statistically significant increase of MUC1 and sialic acid linked by α-2,3 bond with galactose in cancer tissue and in intermediate zone comparing to normal renal tissue distant of tumor. Moreover, we observed statistically significant increase of sialic acid linked by α-2,6 bond with Gal/GalNAc and sialyl Lewis(a/x) antigens in cancer tissues only, comparing to normal ones. CONCLUSIONS: MUC1 and sialylated antigens can be involved in renal tumor development and can be considered as potential markers distinguishing normal renal tissue from intermediate zone and from cancer renal cells during ccRCC development.


Assuntos
Carcinoma de Células Renais/metabolismo , Neoplasias Renais/metabolismo , Antígenos CD15/metabolismo , Mucina-1/metabolismo , Idoso , Biomarcadores Tumorais/metabolismo , Feminino , Humanos , Rim/metabolismo , Masculino , Pessoa de Meia-Idade , Antígeno Sialil Lewis X
11.
Biomed Res Int ; 2014: 196249, 2014.
Artigo em Inglês | MEDLINE | ID: mdl-24605321

RESUMO

The 26S proteasome inhibitor, bortezomib, selectively induces apoptosis in some cancer cells. However, the nature of its selectivity remains unknown. The study presented here provides novel information on cellular effects of bortezomib in normal fibroblasts. We have found that in normoxic conditions the percent of apoptotic cells did not change significantly, independently on incubation time and examined concentration of bortezomib (25 nmol/L or 50 nmol/L). In hypoxic conditions we did not observe any effect of bortezomib on apoptosis of fibroblasts incubated for 24 h and 48 h in comparison to control. Only in the case of fibroblasts incubated for 12 hours in hypoxia significant increase in apoptosis, dependent on concentration of bortezomib, was observed. Our study has shown that bortezomib causes a time-dependent increase in senescence of normal fibroblasts, especially of these incubated in hypoxic conditions. Moreover, we demonstrated that oxygen regulated protein 150 (ORP150) expression was induced in fibroblasts in hypoxia conditions only, suggesting that this protein may play an important role in the cytoprotective response to environmental stress.


Assuntos
Ácidos Borônicos/farmacologia , Senescência Celular/efeitos dos fármacos , Fibroblastos/citologia , Inibidores de Proteassoma/farmacologia , Pirazinas/farmacologia , Pele/citologia , Apoptose/efeitos dos fármacos , Western Blotting , Bortezomib , Hipóxia Celular/efeitos dos fármacos , Sobrevivência Celular/efeitos dos fármacos , Fibroblastos/efeitos dos fármacos , Fibroblastos/enzimologia , Proteínas de Choque Térmico HSP70/metabolismo , Humanos , Subunidade alfa do Fator 1 Induzível por Hipóxia/metabolismo , beta-Galactosidase/metabolismo
12.
Mol Cell Biochem ; 389(1-2): 177-85, 2014 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-24385108

RESUMO

The cellular and molecular effects of the proteasome inhibitor-bortezomib-on breast cancer cells are as yet poorly characterised. Bortezomib selectively induces apoptosis in some cancer cells. However, the nature of its selectivity remains unknown. Previously, we demonstrated that: there was no effect of bortezomib action on apoptosis and a time-dependent increase in senescence of human skin fibroblasts. The study presented here provides novel information on cellular effects of bortezomib in breast cancer cells line MDA-MB-231. Our findings demonstrated that in contrast to normal fibroblasts, bortezomib treatment evoked a strong effect on apoptosis in breast cancer cells incubated in hypoxic and normoxic conditions. We observed a time-dependent increase up to 70 % in apoptosis of MDA-MB-231 cells in hypoxic and normoxic conditions. There was no effect of bortezomib action on senescence of these cells. We suggest that bortezomib may be candidates for further evaluation as chemotherapeutic agents for human breast cancer.


Assuntos
Apoptose/efeitos dos fármacos , Ácidos Borônicos/farmacologia , Neoplasias da Mama/tratamento farmacológico , Complexo de Endopeptidases do Proteassoma/metabolismo , Inibidores de Proteassoma/farmacologia , Pirazinas/farmacologia , Antineoplásicos/farmacologia , Bortezomib , Neoplasias da Mama/metabolismo , Linhagem Celular , Linhagem Celular Tumoral , Sobrevivência Celular/efeitos dos fármacos , Feminino , Fibroblastos/efeitos dos fármacos , Fibroblastos/metabolismo , Proteínas de Choque Térmico HSP70/metabolismo , Humanos , Hipóxia/tratamento farmacológico , Hipóxia/metabolismo , beta-Galactosidase/metabolismo
13.
Adv Clin Exp Med ; 22(3): 347-53, 2013.
Artigo em Inglês | MEDLINE | ID: mdl-23828675

RESUMO

BACKGROUND: Helicobacter pylori is responsible for gastroduodenal diseases such as chronic gastritis, gastric and duodenal ulcers and also gastric malignances. During an infection, gastric mucins, especially secretory MUC5AC, are said to participate in interactions with bacterial adhesins. Recently, epithelial MUC1 mucin has also been proposed to be engaged in infection development. H. pylori surface possesses lipopolisaccharides with Lewis antigens whose role in interactions with gastric mucins has not been elucidated thoroughly so far. OBJECTIVES: To check the involvement of Lewis b and H type 1 structures of H. pylori in adhesion of bacteria to MUC1 mucin. MATERIAL AND METHODS: The study was performed on gastric juices taken from 10 clinical patients and 4 H. pylori strains. Bacteria were assessed for the presence of Lewis b and H type 1 structures by ELISA test. Interactions of H. pylori with MUC1 were analyzed by sandwich ELISA method with bacteria pretreated or not with Lewis b - HSA or H type 1 - HSA glycoconjugates. RESULTS: In the majority of the patients, the slight increase of adhesion of H. pylori to MUC1, after pretreatment of bacteria with H type 1 glycoconjugate was observed. A statistically significant difference was revealed in one strain with a dose of conjugate 50µg/mL (P = 0.05). The influence of Lewis b on adhesion is considered to be contradictory. CONCLUSIONS: H type 1 antigens are suggested to be involved in carbohydrate - carbohydrate interactions of H. pylori with MUC1 mucin.


Assuntos
Aderência Bacteriana , Helicobacter pylori/fisiologia , Antígenos do Grupo Sanguíneo de Lewis/metabolismo , Mucina-1/metabolismo , Adulto , Anticorpos Antibacterianos/imunologia , Feminino , Helicobacter pylori/imunologia , Humanos , Antígenos do Grupo Sanguíneo de Lewis/química , Masculino , Pessoa de Meia-Idade , Ligação Proteica , Adulto Jovem
14.
Acta Biochim Pol ; 60(2): 223-6, 2013.
Artigo em Inglês | MEDLINE | ID: mdl-23772422

RESUMO

Sialic acid and sialyl Lewisa/x are found on N- and O-glycans of many human malignant cells. Carbohydrate antigens can be used as tumor markers, and an increase of their levels in cancer cells is associated with tumor progression. The aim of this study was to assess the level of some Lewis blood group antigens on glycoproteins in tumor (cancer tissue), intermediate zone (adjacent to tumor tissue), and normal renal cortex/medulla (uninvolved by tumor). The study was performed on tissues taken from 30 patients. Relative amounts of sugar structures of proteins with molecular masses above 30 kDa were determined by ELISA-like test with biotinylated lectins: MAA (Maackia amurensis), SNA (Sambucus nigra), and monoclonal antibodies anti-sialyl Lewisa/x.∙ Higher expression of all examined structures was revealed in cancer tissues. Significant increases were observed for sialic acid linked α 2-3 in cancer tissues when compared to healthy ones and also among intermediate and healthy tissues. The sialic acid linked α 2-6 and sialyl Lewisx structures were significantly increased in cancerous cells when compared to normal and intermediate renal tissue. In case of sialyl Lewisa antigen, a significant difference was discovered between normal and intermediate tissue. Our results confirm that the examined Lewis antigens can be involved in tumor development. Their increase in cancer tissues can suggest their specific role in the process.


Assuntos
Biomarcadores Tumorais/biossíntese , Carcinoma de Células Renais/fisiopatologia , Neoplasias Renais/imunologia , Neoplasias Renais/fisiopatologia , Antígenos do Grupo Sanguíneo de Lewis/biossíntese , Idoso , Antígeno CA-19-9 , Feminino , Glicoproteínas/imunologia , Glicoproteínas/metabolismo , Humanos , Rim/metabolismo , Masculino , Pessoa de Meia-Idade , Oligossacarídeos/biossíntese
15.
Folia Histochem Cytobiol ; 50(4): 599-604, 2012.
Artigo em Inglês | MEDLINE | ID: mdl-23264225

RESUMO

Cancer development is associated with the improper glycosylation of proteins. There are alterations in the synthesis and expression of sugar structures. These changes can be important not only in the early stages of tumour development, but also in the next stages connected with cancer invasiveness and its ability to form metastases. Oligosaccharide structures of glycans in tumours deviate from normal cells. Relatively increased degrees of branching and sialylation of N-glycans, enhanced presentation of short-chain mucin-type O-glycans with sialylation, and alterations in the expression of blood group ABO and Lewis epitopes can be observed. The main aim of our study was to assess changes in the glycosylation of proteins in clear cell renal cell carcinoma. This study was performed on tissues taken from 15 patients. The relative amounts of sugar structures of proteins with molecular mass above 30 kDa in tumour (cancer tissue), intermediate zone i.e. tumour-adjacent tissue, and normal tissue uninvolved by tumour, were determined by ELISA-like test with biotinylated lectins highly specific to examined sugar antigens. A higher expression of all examined structures was revealed in cancer tissue. Increased levels of sialic acid, fucose, T and Tn antigens, compared to healthy renal tissue, were characteristic for clear cell renal cell carcinoma.


Assuntos
Saúde , Neoplasias Renais/metabolismo , Neoplasias Renais/patologia , Rim/metabolismo , Rim/patologia , Proteínas/metabolismo , Idoso , Feminino , Glicosilação , Humanos , Lectinas/metabolismo , Masculino , Pessoa de Meia-Idade , Estadiamento de Neoplasias , Estatísticas não Paramétricas , Carga Tumoral
16.
Contemp Oncol (Pozn) ; 16(2): 154-8, 2012.
Artigo em Inglês | MEDLINE | ID: mdl-23788869

RESUMO

BACKGROUND: Lysosomal exoglycosidases, such as α-mannosidases (MAN) and ß-galactosidases (GAL), are found in different glycoside hydrolase sequence-based families. Considerable research has proved plays the role of MAN, which play a key role in the modification and diversification of hybrid N-glycans, processes with strong cellular links to cancer. Therefore the study aim was to investigate the activities of MAN and GAL in larynx cancer compared to controls. MATERIAL AND METHODS: Larynx cancer (n = 21) and normal healthy tissue (n = 21) were collected from patients during total laryngectomy. A biopsy of macroscopically healthy tissue in the area of the lower 1/3 of omohyoid muscle was taken for frozen sections in each case and these served as controls. The release of p-nitrophenol from p-nitrophenol derivatives of MAN and GAL was used. RESULTS: In all specimens we observed significantly higher activity of investigated enzymes in larynx cancer compared with controls. The mean release of MAN from activated cells was 3.702 ±1.3245 nkat/g wet tissue compared to controls (1.614 ±0.8220 nkat/g wet tissue). The mean release of GAL from the activated cells was 3.383 ±2.1980 nkat/g wet tissue compared to controls (2.137 ±1.3685 nkat/g wet tissue). Differences in observed activity were statistically significant. CONCLUSION: The present data indicate that MAN and GAL are significantly and consistently elevated in larynx cancer growth. It also means that catabolic reactions involving glycoproteins, glycolipids and proteoglycans may play a role in larynx cancer. Further research should also evaluate the relative importance of these particular exoglycosidases in indicating the progress of the disease in considering the spectrum of identified marker mediators.

17.
Clin Chem Lab Med ; 49(5): 885-9, 2011 May.
Artigo em Inglês | MEDLINE | ID: mdl-21288176

RESUMO

BACKGROUND: In cancer tissue, altered glycosylation of proteins is observed. There are some typical changes; for example, sialyl-Lewis(a/x) glycoforms are more abundant in many types of cancers. The current study investigated the differences in glycosylation of proteins between neoplastic and healthy human salivary glands. METHODS: Sugar structures on proteins with a molecular mass above 30 kDa were determined by enzyme-linked immunosorbent assay (ELISA) with biotinylated lectins. RESULTS: The expression of sialic acid in cancer tissues was higher in comparison with healthy ones. The same observations were revealed for Fuc α1-6, α1-2, T, Tn antigens and α1-6 mannose. CONCLUSIONS: Glycosylation of proteins in cancer salivary gland tissues is altered in comparison with healthy tissue.


Assuntos
Ensaio de Imunoadsorção Enzimática/métodos , Neoplasias das Glândulas Salivares/metabolismo , Glândulas Salivares/metabolismo , Proteínas e Peptídeos Salivares/metabolismo , Adulto , Idoso , Feminino , Glicosilação , Humanos , Masculino , Pessoa de Meia-Idade , Peso Molecular , Lectinas de Plantas/metabolismo , Neoplasias das Glândulas Salivares/patologia , Glândulas Salivares/citologia , Glândulas Salivares/patologia , Proteínas e Peptídeos Salivares/química
18.
Clin Exp Med ; 11(2): 81-8, 2011 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-20953890

RESUMO

It is suggested that gastric mucins, and in particular some specific glycan structures that can act as carbohydrate receptors, are involved in the interactions with Helicobacter pylori adhesins. The main aim of our study was to evaluate glycosylation pattern of glycoproteins of gastric juice before and at the end of eradication therapy. Gastric juices were taken from 13 clinical patients and subjected to analysis. Pooled fractions of the void volume obtained after gel filtration were subjected to ELISA tests. To assess the relative amounts of carbohydrate structures, lectins and monoclonal antibodies were used. Changes in the level of MUC 1 and MUC 5AC mucins and of carbohydrate structures, which are suggested to be receptors for Helicobacter pylori adhesins, were observed by the end of the eradication treatment. Our results support the idea about the involvement of MUC 5AC and MUC 1 with some specific sugar structures in the mechanism of Helicobacter pylori infection.


Assuntos
Carboidratos/análise , Suco Gástrico/química , Mucina-5AC/análise , Mucina-1/análise , Adulto , Cromatografia em Gel , Ensaio de Imunoadsorção Enzimática , Feminino , Glicosilação , Infecções por Helicobacter/tratamento farmacológico , Helicobacter pylori/isolamento & purificação , Humanos , Masculino , Pessoa de Meia-Idade
19.
Hepatogastroenterology ; 57(98): 367-71, 2010.
Artigo em Inglês | MEDLINE | ID: mdl-20583445

RESUMO

BACKGROUND/AIMS: Helicobacter pylori resides primarily in the gastric mucus layer composed of carbohydrate-rich glycoproteins, mucins. Carbohydrates of the secretory MUC 5AC mucin are one of the proved receptors for H. pylori adhesins. A participation of the membrane-associated MUC 1 in the mechanism of infection is also suggested. The main aim of the study was to support the participation of the membrane associated MUC 1 mucin in the mechanism of infection. METHODOLOGY: 13 gastric juices were included in the study. The presence of MUC 5AC and MUC 1 mucins as well as H. pylori bindings were performed using ELISA tests. RESULTS: MUC 1 and MUC 5AC mucins were present in all the examined juices. H. pylori adhered to both glycoproteins. CONCLUSIONS: H. pylori bind to the secretory MUC 5AC mucin as well as to the epithelial MUC 1. This supports the idea that the membrane-associated mucin is involved in the mechanism of H. pylori infection.


Assuntos
Suco Gástrico/metabolismo , Infecções por Helicobacter/metabolismo , Helicobacter pylori/metabolismo , Mucina-5AC/metabolismo , Mucina-1/metabolismo , Adulto , Ensaio de Imunoadsorção Enzimática , Feminino , Humanos , Masculino , Pessoa de Meia-Idade
20.
Hepatogastroenterology ; 56(94-95): 1287-98, 2009.
Artigo em Inglês | MEDLINE | ID: mdl-19950779

RESUMO

BACKGROUND/AIMS: Evaluation of N-acetyl-beta-D-hexosaminidase (HEX), and its isoenzymes A (HEX A) and B (HEX B) activity in blood serum and urine as potential markers of colorectal cancer. METHODOLOGY: The study was performed in blood serum and urine of 32 patients with adenocarcinoma, 6 with adenocarcinoma mucinosum of the colon, and 20 healthy people. The activity of HEX, HEX A and HEX B was determined in blood serum and urine by spectrophotometric method of Marciniak et al. The concentration of CEA was determined in blood serum by immunoenzymatic method (MEIA). The concentration of protein was assessed by the Lowry method, whereas the concentration of creatinine in urine by the Jaffe method (without deproteinization). RESULTS: A significant increase in the concentration of HEX, HEX A and HEX B activity was proved in serum and urine of patients with colon adenocarcinoma. In patients with colon adenocarcinoma mucinosum, the higher activity of HEX was revealed in blood serum compared to healthy people, and the significantly higher activity of HEX and HEX B expressed as pKat/mg of creatinine, was found in urine. We observe a significant increase in the activity of HEX, HEX A and HEX B expressed in pKat/mg of creatinine was found in urine of patients bearing tumor of diameter 6.0-7.0 cm in comparison to patients with tumor of diameter 4.0-5.0 cm. CONCLUSIONS: The present study results suggest that determination of HEX, HEX A and HEX B activity in blood serum and urine may be used to detect colon cancer in its early stages. However, the use of HEX, HEX A and HEX B activity in oncological diagnostics requires further studies on a larger group of patients.


Assuntos
Biomarcadores Tumorais/análise , Neoplasias do Colo/diagnóstico , Hexosaminidase A/análise , Hexosaminidase B/análise , beta-N-Acetil-Hexosaminidases/análise , Adulto , Idoso , Idoso de 80 Anos ou mais , Biomarcadores Tumorais/sangue , Biomarcadores Tumorais/urina , Antígeno Carcinoembrionário/sangue , Feminino , Hexosaminidase A/sangue , Hexosaminidase A/urina , Hexosaminidase B/sangue , Hexosaminidase B/urina , Humanos , Masculino , Pessoa de Meia-Idade , beta-N-Acetil-Hexosaminidases/sangue , beta-N-Acetil-Hexosaminidases/urina
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