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18 záznamů v PubMed Filtry

Článek

Protease resistance of porcine acidic mammalian chitinase under gastrointestinal conditions implies that chitin-containing organisms can be sustainable dietary resources

Tabata, Eri
Autor Tabata, Eri Department of Chemistry and Life Science, Kogakuin University, Hachioji, Tokyo, 192-0015, Japan
Kashimura, Akinori
Autor Kashimura, Akinori Department of Chemistry and Life Science, Kogakuin University, Hachioji, Tokyo, 192-0015, Japan
Wakita, Satoshi
Autor Wakita, Satoshi Department of Chemistry and Life Science, Kogakuin University, Hachioji, Tokyo, 192-0015, Japan
Ohno, Misa
Autor Ohno, Misa Department of Chemistry and Life Science, Kogakuin University, Hachioji, Tokyo, 192-0015, Japan
Sakaguchi, Masayoshi
Autor Sakaguchi, Masayoshi Department of Chemistry and Life Science, Kogakuin University, Hachioji, Tokyo, 192-0015, Japan
Sugahara, Yasusato
Autor Sugahara, Yasusato Department of Chemistry and Life Science, Kogakuin University, Hachioji, Tokyo, 192-0015, Japan
Imamura, Yasutada
Autor Imamura, Yasutada Department of Chemistry and Life Science, Kogakuin University, Hachioji, Tokyo, 192-0015, Japan
Seki, Shiro
Autor Seki, Shiro Department of Environmental Chemistry, Kogakuin University, Hachioji, Tokyo, 192-0015, Japan
Ueda, Hitoshi
Autor Ueda, Hitoshi Department of Integrative Biology, Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530, Japan
Matoska, Vaclav
Autor Matoska, Vaclav Laboratory of Molecular Diagnostics, Department of Clinical Biochemistry, Hematology and Immunology, Homolka Hospital, Roentgenova 37/2, Prague, 150 00, Czech Republic

Scientific reports. 2017 Oct 11 ; 7 (1) : 12963. [epub] 20171011

Sci Rep
ISSN 2045-2322
Zdroj

Chitin, a polymer of N-acetyl-D-glucosamine (GlcNAc), is a major structural component in chitin-containing organism including crustaceans, insects and fungi. Mammals express two chitinases, chitotriosidase (Chit1) and acidic mammalian chitinase (AMCase). Here, we report that pig AMCase is stable in the presence of other digestive proteases and functions as chitinolytic enzyme under the gastrointestinal conditions. Quantification of chitinases expression in pig tissues using quantitative real-time PCR showed that Chit1 mRNA was highly expressed in eyes, whereas the AMCase mRNA was predominantly expressed in stomach at even higher levels than the housekeeping genes. AMCase purified from pig stomach has highest activity at pH of around 2-4 and remains active at up to pH 7.0. It was resistant to robust proteolytic activities of pepsin at pH 2.0 and trypsin and chymotrypsin at pH 7.6. AMCase degraded polymeric chitin substrates including mealworm shells to GlcNAc dimers. Furthermore, we visualized chitin digestion of fly wings by endogenous AMCase and pepsin in stomach extract. Thus, pig AMCase can function as a protease resistant chitin digestive enzyme at broad pH range present in stomach as well as in the intestine. These results indicate that chitin-containing organisms may be a sustainable feed ingredient in pig diet.

MeSH
chitin metabolismus MeSH
chitinasy genetika izolace a purifikace metabolismus MeSH
chymotrypsin metabolismus MeSH
dieta * MeSH
Drosophila chemie MeSH
endopeptidasy metabolismus MeSH
gastrointestinální trakt metabolismus MeSH
křídla zvířecí chemie MeSH
messenger RNA genetika metabolismus MeSH
orgánová specificita MeSH
pepsinogen A metabolismus MeSH
prasata genetika MeSH
rozpustnost MeSH
substrátová specifita MeSH
Tenebrio MeSH
tkáňové extrakty MeSH
trypsin metabolismus MeSH
zvířata MeSH
Check Tag
zvířata MeSH
Publikační typ
časopisecké články MeSH
práce podpořená grantem MeSH
Názvy látek
chitin MeSH
chitinasy MeSH
chymotrypsin MeSH
endopeptidasy MeSH
messenger RNA MeSH
pepsinogen A MeSH
tkáňové extrakty MeSH
trypsin MeSH

Článek

Searching for New Biomarkers and the Use of Multivariate Analysis in Gastric Cancer Diagnostics

Anticancer research. 2016 Apr ; 36 (4) : 1967-71.

Anticancer Res
ISSN 1791-7530 | 0250-7005
Zdroj

AIM: The first aim of this study was to search for new biomarkers to be used in gastric cancer diagnostics. The second aim was to verify the findings presented in literature on a sample of the local population and investigate the risk of gastric cancer in that population using a multivariant statistical analysis. PATIENTS AND METHODS: We assessed a group of 36 patients with gastric cancer and 69 healthy individuals. We determined carcinoembryonic antigen, cancer antigen 19-9, cancer antigen 72-4, matrix metalloproteinases (-1, -2, -7, -8 and -9), osteoprotegerin, osteopontin, prothrombin induced by vitamin K absence-II, pepsinogen I, pepsinogen II, gastrin and Helicobacter pylori for each sample. RESULTS: The multivariate stepwise logistic regression identified the following biomarkers as the best gastric cancer predictors: CEA, CA72-4, pepsinogen I, Helicobacter pylori presence and MMP7. CONCLUSION: CEA and CA72-4 remain the best markers for gastric cancer diagnostics. We suggest a mathematical model for the assessment of risk of gastric cancer.

Klíčová slova
Gastric cancer, biomarkers, gastric cancer index, tumor markers,
MeSH
antigeny sacharidové asociované s nádorem krev MeSH
dospělí MeSH
Helicobacter pylori imunologie MeSH
imunoglobulin G krev MeSH
infekce vyvolané Helicobacter pylori imunologie MeSH
karcinoembryonální antigen krev MeSH
lidé středního věku MeSH
lidé MeSH
matrixová metaloproteinasa 7 krev MeSH
multivariační analýza MeSH
nádorové biomarkery krev MeSH
nádory žaludku krev diagnóza MeSH
pepsinogen A krev MeSH
protilátky bakteriální krev MeSH
rizikové faktory MeSH
senioři nad 80 let MeSH
senioři MeSH
teoretické modely * MeSH
Check Tag
dospělí MeSH
lidé středního věku MeSH
lidé MeSH
senioři nad 80 let MeSH
senioři MeSH
Publikační typ
časopisecké články MeSH
práce podpořená grantem MeSH
Názvy látek
antigeny sacharidové asociované s nádorem MeSH
CA-72-4 antigen MeSH Prohlížeč
imunoglobulin G MeSH
karcinoembryonální antigen MeSH
matrixová metaloproteinasa 7 MeSH
MMP7 protein, human MeSH Prohlížeč
nádorové biomarkery MeSH
pepsinogen A MeSH
protilátky bakteriální MeSH

Článek

Chicken and rabbit antibodies against porcine pepsinogen A

Prague medical report. 2015 ; 116 (1) : 16-23.

Prague Med Rep
ISSN 1214-6994
Zdroj

Isolated porcine pepsinogen A was used for the preparation of polyclonal rabbit and polyclonal chicken anti-pepsinogen A antibodies. Immunochemical properties of both immunoglobulin fractions were compared. The rabbit anti-serum was further purified using immobilized porcine pepsinogen A on magnetic cellulose beads and the resulting anti-pepsinogen A fraction proved to be applicable for the separation and the determination of porcine pepsinogen A. In contrary, antibodies prepared from chicken eggs by the same way have been found not suitable for the evaluation of the pepsinogen A level. Unexpectedly, the pre-immune fraction of chicken antibodies showed reactivity against porcine pepsinogen A and the affinity separation of specific polyclonal chicken anti-pepsinogen A antibodies on immobilized porcine pepsinogen A did not result in an enrichment of anti-pepsinogen A antibodies.

MeSH
ELISA MeSH
imunohistochemie MeSH
králíci MeSH
kur domácí MeSH
nádory žaludku imunologie metabolismus MeSH
pepsinogen A imunologie metabolismus MeSH
prasata MeSH
protilátky imunologie MeSH
skot MeSH
žaludeční sliznice imunologie metabolismus patologie MeSH
zvířata MeSH
Check Tag
králíci MeSH
skot MeSH
zvířata MeSH
Publikační typ
časopisecké články MeSH
práce podpořená grantem MeSH
Názvy látek
pepsinogen A MeSH
protilátky MeSH

Článek

Affinity chromatography of porcine pepsin and pepsinogen using immobilized ligands derived from the specific substrate for this enzyme

Journal of chromatography. B, Analytical technologies in the biomedical and life sciences. 2004 Feb 05 ; 800 (1-2) : 109-14.

J Chromatogr B Analyt Technol Biomed Life Sci
ISSN 1570-0232
Zdroj

Affinity chromatography of porcine protease and its zymogen was carried out on immobilized components of specific substrate used for the pepsin determination. For the immobilization of N-acetyl-L-phenylalanine and iodinated derivative of L-tyrosine, divinyl sulfone activated Sepharose was used. Ligands with blocked amino group and free carboxyl one were linked to Sepharose via ethylene diamine spacer using carbodiimide reaction. Conditions of affinity chromatography of porcine pepsin and pepsinogen on the prepared carriers were optimized: the effect of pH, ionic strength and a nature of the buffers used on adsorption of the enzyme and zymogen to an affinity carrier, as well as their elution was studied. The following parameters were taken into consideration: capacity of the prepared affinity matrices, reproducibility of experiments and the enzyme stability. Pepsin was adsorbed to both immobilized ligands at pH 3.5-4.0; for the elution of the enzyme it was necessary to increase ionic strength (up to 0.5 M). For the adsorption of pepsinogen pH 5.2 was found to be optimum, for its desorption, an increase of ionic strength was used.

Článek

Aromatic amino acids and their derivatives as ligands for the isolation of aspartic proteinases

Journal of chromatography. B, Analytical technologies in the biomedical and life sciences. 2002 Apr 25 ; 770 (1-2) : 121-8.

J Chromatogr B Analyt Technol Biomed Life Sci
ISSN 1570-0232
Zdroj

Affinity chromatography was used to study an interaction of aspartic proteinases with immobilized aromatic amino acids and their derivatives. The following ligands were used: L-tyrosine, 3-iodo-L-tyrosine, 3,5-diiodo-L-tyrosine, L-phenylalanine, p-iodo-L-phenylalanine and N-acetyl-L-phenylalanine. With the exception of the last one, ligands were coupled directly to divinyl sulfone activated Sepharose 4B. For the preparation of immobilized N-acetyl-L-phenylalanine, divinyl sulfone activated Sepharose 4-B with linked ethylene diamine was used. Porcine pepsin was used for the evaluation of the capacity of the prepared affinity carriers. The capacity of the immobilized amino acid derivatives significantly increased in comparison with the non-derivatized amino acids. The prepared immobilized ligands were further used for the separation of human pepsinogens.

MeSH
aminokyseliny aromatické metabolismus MeSH
aspartátové endopeptidasy izolace a purifikace metabolismus MeSH
lidé MeSH
ligandy MeSH
pepsin A izolace a purifikace MeSH
pepsinogen A izolace a purifikace MeSH
prasata MeSH
tyrosin metabolismus MeSH
zvířata MeSH
Check Tag
lidé MeSH
zvířata MeSH
Publikační typ
časopisecké články MeSH
práce podpořená grantem MeSH
Názvy látek
aminokyseliny aromatické MeSH
aspartátové endopeptidasy MeSH
ligandy MeSH
pepsin A MeSH
pepsinogen A MeSH
tyrosin MeSH

Článek

Immobilized-metal-ion affinity chromatography as a tool for the qualitative study of pepsinogen phosphorylation

Journal of biochemical and biophysical methods. 2001 Oct 30 ; 49 (1-3) : 523-31.

J Biochem Biophys Methods
ISSN 0165-022X
Zdroj

Affinity chromatography on immobilized Fe(3+) ions--immobilized-metal-ion affinity chromatography (IMAC) method--was used for the determination of pepsin and pepsinogen phosphorylation. IMAC is a very powerful method for detailed studies of proteins. Dephosphorylation of the pepsinogens and pepsins has no effect on their proteolytic ability. For this reason, the determination of proteolytic activity was used for the detection of pepsinogen (pepsin) presence in the collected fractions as a very suitable and specific method. Pepsins and their zymogens probably have the same amounts of phosphate ions in their molecule. The exact definition of conditions is very important for the prepurification of the proteinases and for their analysis.