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[Activity of cytoplasmic proteinases from rat liver in Heren's carcinoma during tumor growth and treatment with medicinal herbs]

https://arctichealth.org/en/permalink/ahliterature20009
Source
Ukr Biokhim Zh. 2000 May-Jun;72(3):91-4
Publication Type
Article
Author
M M Marchenko
H P Kopyl'chuk
O V Hrygor'ieva
Author Affiliation
Yu. Fedkovich Chernivtsi State University, Ukraine.
Source
Ukr Biokhim Zh. 2000 May-Jun;72(3):91-4
Language
Ukrainian
Publication Type
Article
Keywords
Animals
Cytoplasm - enzymology
English Abstract
Hydrolysis
Liver - enzymology - pathology
Liver Neoplasms - enzymology
Organ Size - drug effects
Plant Extracts - pharmacology
Plants, Medicinal - chemistry
Rats
Abstract
The dynamics of the acid and neutral proteinases general enzymes activity change in the hepatocytes postnuclear fraction in the rats suffering from the Heren's carcinoma was investigated. It was determined that in the tumor development of the enzyme activity level of both the acid and neutral proteinases increased 2,6-fold. The natural preparation of the herbs (Calendula officinalis L., Echinacea purpurea L., Scorzonera humilis L., Aconitum moldavicum Hacq.) normalizes both the activity of the investigated enzymes and coefficients of the liver weights of the sick animals. The chemical medicinal preparation 5,6-benzcumarine-5-uracil normalizes the activity of the neutral cytoplasmatic proteinases and reduces the level of the proteolytic activity of the acid enzymes in comparison with the control group of the animals as well as increases of the liver weight coefficients.
PubMed ID
11200483 View in PubMed
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[Isoenzymic composition of glucose-6-phosphate dehydrogenase of subcellular fractions of rabbit tissues under alloxan diabetes]

https://arctichealth.org/en/permalink/ahliterature49029
Source
Ukr Biokhim Zh. 1975 May-Jun;47(3):339-41
Publication Type
Article
Author
N M Hula
Ia L Hermaniuk
Source
Ukr Biokhim Zh. 1975 May-Jun;47(3):339-41
Language
Ukrainian
Publication Type
Article
Keywords
Adrenal Glands - enzymology
Animals
Cytoplasm - enzymology
Diabetes Mellitus, Experimental - enzymology
English Abstract
Glucosephosphate Dehydrogenase - metabolism
Isoenzymes - metabolism
Liver - enzymology
Mitochondria - enzymology
Mitochondria, Liver - enzymology
Mitochondria, Muscle - enzymology
Muscles - enzymology
Myocardium - enzymology
Rabbits
Spleen - enzymology
Subcellular Fractions - enzymology
Abstract
The isoenzymes of glucose-6-phosphate dehydrogenase (G-6-PD, EC 1.1.1.49) was studied in hyaloplasm and mitochondria of the liver, myocardium, skeletal muscle, spleen and adrenals of alloxan diabetic rabbits. The most significant changes were found in the liver hyaloplasm: one of the minor isoenzymes, isoenzyme "C", disappears and the zone of the main isoenzyme "E" decreases significantly in comparison with the control. It was found that the intensity of these changes depends on the glycemia level in the diabetic animals.
PubMed ID
1216350 View in PubMed
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Matrix metalloproteinase-9 (MMP-9) immunoreactive protein in urinary bladder cancer: a marker of favorable prognosis.

https://arctichealth.org/en/permalink/ahliterature85620
Source
Anticancer Res. 2008 May-Jun;28(3B):1757-61
Publication Type
Article
Author
Vasala Kaija
Pääkko Paavo
Turpeenniemi-Hujanen Taina
Author Affiliation
Department of Oncology and Radiotherapy, Oulu University Hospital, Oulu, Finland. kaija.vasala@oulu.fi
Source
Anticancer Res. 2008 May-Jun;28(3B):1757-61
Language
English
Publication Type
Article
Keywords
Carcinoma, Transitional Cell - enzymology - pathology
Cytoplasm - enzymology
Disease Progression
Disease-Free Survival
Female
Follow-Up Studies
Humans
Immunohistochemistry
Male
Matrix Metalloproteinase 9 - metabolism
Neoplasm Staging
Survival Rate
Tumor Markers, Biological - metabolism
Urinary Bladder Neoplasms - enzymology - pathology
Abstract
BACKROUND: The purpose of this study was to explore whether changes in matrix metalloproteinase-9 (MMP-9) are involved in the progression of urinary bladder cancer and whether they have any prognostic value. PATIENTS AND METHODS: Overexpression of MMP-9 was evaluated in the primary tumor of 87 urinary bladder cancer cases with immunohistochemical staining. RESULTS: Of the urinary bladder carcinomas, 38% showed an overexpression (>25%) of MMP-9 immunoreactive protein. Increased positivity for MMP-9 correlated with favorable overall survival of the urinary bladder cancer patients. The 5-year overall survival and relapse-free survival was 68% and 36% in patients showing high MMP-9 expression and 48% and 19% in patients with low (
PubMed ID
18630455 View in PubMed
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The tumour-associated carbonic anhydrases CA II, CA IX and CA XII in a group of medulloblastomas and supratentorial primitive neuroectodermal tumours: an association of CA IX with poor prognosis.

https://arctichealth.org/en/permalink/ahliterature144172
Source
BMC Cancer. 2010;10:148
Publication Type
Article
Date
2010
Author
Kristiina Nordfors
Joonas Haapasalo
Miikka Korja
Anssi Niemelä
Jukka Laine
Anna-Kaisa Parkkila
Silvia Pastorekova
Jaromir Pastorek
Abdul Waheed
William S Sly
Seppo Parkkila
Hannu Haapasalo
Author Affiliation
Department of Pathology, Tampere University Hospital, Tampere, Finland. kristiina.nordfors@gmail.com
Source
BMC Cancer. 2010;10:148
Date
2010
Language
English
Publication Type
Article
Keywords
Adolescent
Adult
Aged
Antigens, Neoplasm - analysis
Apoptosis
Carbonic Anhydrase II - analysis
Carbonic Anhydrases - analysis
Cerebellar Neoplasms - blood supply - enzymology - pathology - therapy
Chi-Square Distribution
Child
Child, Preschool
Cytoplasm - enzymology
Endothelial Cells - enzymology
Female
Finland
Humans
Immunohistochemistry
Infant
Infant, Newborn
Kaplan-Meier Estimate
Male
Medulloblastoma - blood supply - enzymology - pathology - therapy
Middle Aged
Neuroectodermal Tumors, Primitive - blood supply - enzymology - pathology - therapy
Odds Ratio
Proportional Hazards Models
Supratentorial Neoplasms - blood supply - enzymology - pathology - therapy
Time Factors
Treatment Outcome
Tumor Markers, Biological - analysis
Young Adult
Abstract
Medulloblastomas (MBs) and supratentorial primitive neuroectodermal tumours (PNETs) are the most common highly aggressive paediatric brain tumours. In spite of extensive research on these tumours, there are only few known biomarkers or therapeutic target proteins, and the prognosis of patients with these tumours remains poor. Our aim was to investigate whether carbonic anhydrases (CAs), enzymes commonly overexpressed in various tumours including glioblastomas and oligodendrogliomas, are present in MBs and PNETs, and whether their expression can be correlated with patient prognosis.
We determined the expression of the tumour-associated carbonic anhydrases CA II, CA IX and CA XII in a series of MB/PNET specimens (n = 39) using immunohistochemistry.
Endothelial CA II, cytoplasmic CA II, CA IX and CA XII were expressed in 49%, 73%, 23% and 11% of the tumours, respectively. CA II was detected in the neovessel endothelium and the tumour cell cytoplasm. CA IX was mainly expressed in the tumour cells located in perinecrotic areas. CA XII showed the most homogenous distribution within the tumours. Importantly, CA IX expression predicted poor prognosis in both univariate (p = 0.041) and multivariate analyses (p = 0.016).
We suggest that CA IX should be considered a potential prognostic and therapeutic target in MBs and PNETs.
Notes
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PubMed ID
20398423 View in PubMed
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8 records – page 1 of 1.