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1.
J Cancer Res Ther ; 20(1): 25-32, 2024 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-38554294

RESUMO

OBJECTIVE: The aim of this study is to present the expressions of Calreticulin (CALR) and Glucagon-like peptide-1 (GLP-1) in high-grade gliomas and to further show the relation between the levels of these molecules and Ki-67 index, presence of Isocitrate dehydrogenase (IDH)-1 mutation, and tumor grade. PATIENTS AND METHODS: A total of 43 patients who underwent surgical resection due to high-grade gliomas (HGG) (grades III and IV) were included. The control group comprised 27 people who showed no gross pathology in the brain during the autopsy procedures. Adequately sized tumor samples were removed from each patient during surgery, and cerebral tissues were removed from the control subjects during the autopsy procedures. Each sample was stored at -80°C as rapidly as possible until the enzyme assay. RESULTS: Patients with high-grade gliomas showed significantly higher levels of CALR and significantly lower levels of GLP-1 when compared to control subjects (P = 0.001). CALR levels were significantly higher, GLP-1 levels were significantly lower in grade IV gliomas than those in grade III gliomas (P = 0.001). Gliomas with negative IDH-1 mutations had significantly higher CALR expressions and gliomas with positive IDH-1 mutations showed significantly higher GLP-1 expressions (P = 0.01). A positive correlation between Ki-67 and CALR and a negative correlation between Ki-67 and GLP-1 expressions were observed in grade IV gliomas (P = 0.001). CONCLUSIONS: Our results showed that higher CALR and lower GLP-1 expressions are found in HGGs compared to normal cerebral tissues.


Assuntos
Neoplasias Encefálicas , Glioma , Humanos , Neoplasias Encefálicas/patologia , Prognóstico , Antígeno Ki-67/genética , Antígeno Ki-67/metabolismo , Calreticulina/genética , Calreticulina/metabolismo , Glioma/patologia , Peptídeo 1 Semelhante ao Glucagon , Isocitrato Desidrogenase/genética , Mutação , Gradação de Tumores
2.
Turk Neurosurg ; 33(5): 799-803, 2023.
Artigo em Inglês | MEDLINE | ID: mdl-37715603

RESUMO

AIM: To compare tissue levels of the regulatory enzymes related to the Krebs cycle between low, and high-grade supratentorial gliomas. MATERIAL AND METHODS: Forty patients who underwent surgery for supratentorial gliomas (19 with low-grade and 21 with high-grade gliomas) were evaluated. The regulatory enzymes directly involved in the Krebs cycle, namely pyruvate dehydrogenase, citrate synthase, ?-ketoglutarate dehydrogenase, and isocitrate dehydrogenase, and two enzymes that indirectly regulate the Krebs cycle, namely glutamate dehydrogenase and glutaminase, were quantitatively studied in tumor tissues using ELISA. The results were compared between the two groups. RESULTS: The levels of all enzymes were higher in the high-grade glioma group but only pyruvate dehydrogenase, citrate synthase, and isocitrate dehydrogenase levels showed statistical significance. Moreover, all enzymes showed higher tissue levels in grade- II compared to grade-I gliomas, but only two enzymes, glutamate dehydrogenase and glutaminase, reached significantly higher levels. In the high-grade glioma group, all enzymes again showed higher tissue levels in grade-IV gliomas than in grade-III gliomas, but none showed statistical significance. CONCLUSION: Regulatory enzymes of the Krebs cycle are increased in high-grade gliomas compared to low-grade gliomas. Glutaminolysis enzymes, namely glutamate dehydrogenase and glutaminase, which are required for resupplying the Krebs cycle, are also increased in order to meet the high energy demand in high-grade gliomas.


Assuntos
Ciclo do Ácido Cítrico , Glioma , Humanos , Glutaminase , Citrato (si)-Sintase , Isocitrato Desidrogenase , Glutamato Desidrogenase , Glioma/cirurgia , Piruvatos
3.
J Med Biochem ; 41(3): 335-340, 2022 Jul 29.
Artigo em Inglês | MEDLINE | ID: mdl-36042906

RESUMO

Background: Alkaline phosphatase (ALP) enzymes are widely used as signal amplifiers in immunoenzymatic methods. Conditions that cause ALP elevations, such as bone or liver diseases, can cause interference in immunoenzymatic methods. We aimed to examine ALP's effect on immunoenzymatic assay by adding isolated pure ALP to the prepared serum pool. Methods: We prepared a serum pool and divided it into 4 groups. By adding isolated pure ALP at different concentrations to each group, we obtained sample groups containing ALP enzyme at concentrations of 85 U/L, 340 U/L, 870 U/L, and 1570 U/L. 20-repetition of bhCG, ferritin, FT4, TSH, troponin I, and Vit B12 tests were performed in each group. The coefficient of variation, bias, and total error was calculated. All groups were compared by using the Friedman test for paired samples. Results: After ALP addition, the calculated total error values of FT4, bhCG and troponin I tests were above the acceptable error limits. There were statistically significant differences in bhCG, FT4, troponin I, and Vit B12 tests compared to the baseline ALP level (P<0.0125). Conclusions: Isolated ALP elevations can be a source of interference for immunoenzymatic methods.

4.
Leuk Res Rep ; 17: 100293, 2022.
Artigo em Inglês | MEDLINE | ID: mdl-35242525

RESUMO

We aimed to examine the efficiency for prediction of prognosis and response in non-APL AML cases of the "Samatya-predicting score". A total of 213 patients diagnosed between January 2010-December 2020 were examined. Of the 158 patients included in the study, the median value of risk score was determined as 2,5. The sensitivity for mortality was 88% and the specificity was 42%. In terms of being non-responder to induction therapy, the sensitivity was 90,1%, the specificity was 25,3%. OS was shorter in those with high risk scores. This study makes an important contribution to the literature in terms of creating a different perspective to predict prognosis in AML.

5.
Turk Neurosurg ; 31(2): 282-289, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-33575999

RESUMO

AIM: To assess and compare the antioxidant capacities of high-grade gliomas (HGG) according to their grades and the presence of isocitrate dehydrogenase 1 (IDH1) mutation using tissue thiol level measurement. MATERIAL AND METHODS: Tissue thiol concentrations were measured in 41 HGG samples and 21 healthy brain tissues obtained from autopsy procedures, which were performed within the first 4 hours of death. All samples were stored at ?80°C, and a thiol quantification kit was used in evaluating tissue thiol levels. The Number Cruncher Statistical System was used for statistical analyses to detect the differences between the control group and the HGG group, which was also divided into subgroups according to their grade and IDH1 mutation presence. RESULTS: The tissue thiol levels of HGGs were found to be higher than the control group (p=0.001). Although the median thiol levels of Grade 4 gliomas were higher than those of Grade 3, no statistically significant difference was noted (p=0.076). When all tumors were compared according to the IDH1 mutation presence, IDH1-negative (IDH1-) HGGs had higher thiol contents than IDH1 mutant (IDH1+) HGGs (p=0.001). The thiol levels of Grade 4 IDH1- gliomas were statistically significantly higher than of Grade 3 gliomas (p=0.023), but no statistically significant difference between the thiol levels of Grade 3 and Grade 4 IDH1+ tumors was noted (p=0.459). CONCLUSION: We have demonstrated the higher thiol concentrations of HGGs, particularly IDH1- ones. The sulfhydryl contents of gliomas as an indicator of tumoral antioxidant capacity may be responsible for the treatment resistance of IDH1- gliomas, the mechanism of which is not clear. Thiols can be a novel target for treatment, considering the unsatisfactory results of current modalities for HGGs.


Assuntos
Antioxidantes/metabolismo , Neoplasias Encefálicas/metabolismo , Glioma/metabolismo , Isocitrato Desidrogenase , Mutação , Compostos de Sulfidrila/metabolismo , Adulto , Idoso , Encéfalo/metabolismo , Encéfalo/patologia , Neoplasias Encefálicas/genética , Neoplasias Encefálicas/patologia , Contagem de Células/métodos , Feminino , Glioma/genética , Glioma/patologia , Humanos , Isocitrato Desidrogenase/genética , Masculino , Pessoa de Meia-Idade , Mutação/genética , Adulto Jovem
6.
World Neurosurg ; 137: e554-e563, 2020 05.
Artigo em Inglês | MEDLINE | ID: mdl-32068173

RESUMO

BACKGROUND: MIR17 host gene (MIR17HG) is a potential therapeutic target for some cancer types. The aim of this study was to assess MIR17HG protein levels in patients with meningioma who had not been reported previously in the literature and comparing with normal meninges tissues. METHODS: MIR17HG protein levels were measured in 46 samples including 25 meningioma tissues procured during surgery and 21 normal meninges tissues obtained within 4 hours of death during autopsy procedures. Each sample was stored at -80°C until the evaluation of MIR17HG protein using a sandwich enzyme-linked immunoassay principle. Results were compared between the groups. RESULTS: MIR17HG protein levels were significantly higher in meningioma tissues compared with controls and difference was statistically significant (P = 0.012). Both World Health Organization grade I and grade II meningiomas had higher MIR17HG protein levels compared with controls and differences were statistically significant (P = 0.026 for grade I and P = 0.042 for grade II). Receiver operating characteristic curve analysis was performed to determine the cutoff of MIR17HG protein value in differentiating meningioma and control groups. At the cutoff value for MIR17HG protein of >0.0998 ng/mL, the sensitivity was 73.91%, 71.43%, and 77.78% and area under the curve was 0.756, 0.753, and 0.761 for meningioma group, grade I, and grade II subgroups, respectively, and specificity was 69.23% for each group. CONCLUSIONS: MIR17HG protein expression was found to have a higher level in meningiomas than in normal meninges tissues in our study. Considering the recurrence and irresectability for some meningiomas, which require further treatment, MIR17HG may be a new target for treatment in meningiomas and our study will shed light on further studies.


Assuntos
Neoplasias Meníngeas/metabolismo , Meninges/metabolismo , Meningioma/metabolismo , MicroRNAs/metabolismo , Adulto , Idoso , Feminino , Humanos , Masculino , Neoplasias Meníngeas/genética , Neoplasias Meníngeas/patologia , Meninges/patologia , Meningioma/genética , Meningioma/patologia , MicroRNAs/genética , Pessoa de Meia-Idade
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