The relationship between nutrition screenings and nutritional status determined by malnutrition in hemodialysis patients

Objective: It is aimed to evaluate the relationship of food consumptions, biochemical blood parameters, and some anthropometrics with the screening tests using in the nutritional status of hemodialysis patients with end stage renal failure. Materials and Methods: The survey were conducted with 110 hemodialysis patients who hospitalized at the Nephrology Clinic in Akdeniz University Hospital. The routine biochemical blood parameters of the patients were analyzed and their anthropometric measurements were performed. The food consumptions were recorded by the dietician and Nutritional Risk Screening 2002 (NRS 2002), Malnutrition Universal Screening Tool (MUST) and Subjective Global Assessment (SGA)has screening tests using were performed. Results: The average age of the patients participating in the study was 55 ± 19 years. In MUST, 42.7% of the patients were at high risk, 18.2% of them at moderate risk by malnutrition. Statistically significant relationship was also negatively determined between body weight, dry weight, BMI, the waist circumference, and MUST and SGA (p<0.05). A negatively significant relationship was statistically found among albumin, creatinine, hemoglobin and calcium readouts by NRS2002, among albumin, BUN, calcium and phosphorus readouts by MUST, among albumin, hemoglobin and calcium readouts by SGA (p<0.05). Conclusion: It was observed that the dialysis patients could not get the advised nutritional quantities, thence malnutrition progressed. It is concluded that anthropometric measurements are more concordant with MUST and the biochemical symptoms with NRS2002, and therefore both must be taken into consideration in the assessment of nutritional status correctly of the end-stage renal patients undergoing hemodialysis

Evaluation of the effect of gluten-free diet and Mediterranean diet on autoimmune system in patients with Hashimoto's thyroiditis

Hashimoto's thyroiditis is an autoimmune disease in which thyroid cells are attacked through cell-and antibody-mediated immune processes. A gluten-free diet reduces antibody concentration and regulates thyroid autoimmunization. Mediterranean diet reduces oxidative stress. This study evaluates the short-term effects of Mediterranean, gluten-free, and Mediterranean gluten-free dietary patterns on thyroid function and autoantibody levels of patients. The 40 patients with Hashimoto's thyroiditis included in the study were randomly divided into four groups (defined as gluten-free, Mediterranean, Mediterranean gluten-free, and controls) for 12 weeks. Thyroid function tests, autoantibody levels, and food consumption were recorded at the beginning and end of the study. There was no statistically significant difference in TSH levels of the groups before the intervention, but a statistically significant difference was found afterward (p 0.05). In addition, body weight, body mass index, waist and hip circumference averages decreased significantly in all intervention groups compared with controls (p < 0.05). The study achieved an increase in Free T-3 hormone levels in the intervention groups. The most marked difference was seen in the Mediterranean gluten-free diet model, which may be due to the anti-inflammatory effect of both Mediterranean and gluten-free diets and the loss of body weight as a result of the intervention

Evaluation of the ICT Tuberculosis test for the routine diagnosis of tuberculosis

BACKGROUND: Rapid and accurate diagnosis of tuberculosis (TB) is crucial to facilitate early treatment of infectious cases and thus to reduce its spread. To improve the diagnosis of TB, more rapid diagnostic techniques such as antibody detection methods including enzyme-linked immunosorbent assay (ELISA)-based serological tests and immunochromatographic methods were developed. This study was designed to evaluate the validity of an immunochromatographic assay, ICT Tuberculosis test for the serologic diagnosis of TB in Antalya, Turkey. METHODS: Sera from 72 patients with active pulmonary (53 smear-positive and 19 smear-negative cases) and eight extrapulmonary (6 smear-positive and 2 smear-negative cases) TB, and 54 controls from different outpatient clinics with similar demographic characteristics as patients were tested by ICT Tuberculosis test. RESULTS: The sensitivity, specificity, and negative predictive value of the ICT Tuberculosis test for pulmonary TB were 33.3%, 100%, and 52.9%, respectively. Smear-positive pulmonary TB patients showed a higher positivity rate for antibodies than smear-negative patients, but the difference was not statistically significant. Of the eight patients with extrapulmonary TB, antibody was detected in four patients. CONCLUSION: Our results suggest that ICT Tuberculosis test can be used to aid TB diagnosis in smear-positive patients until the culture results are available

Cytosolic Guanine Nucledotide Binding Deficient Form of Transglutaminase 2 (R580a) Potentiates Cell Death in Oxygen Glucose Deprivation

Transglutaminase 2 (TG2) is a hypoxia-responsive protein that is a calcium-activated transamidating enzyme, a GTPase and a scaffolding/linker protein. Upon activation TG2 undergoes a large conformational change, which likely affects not only its enzymatic activities but its non-catalytic functions as well. The focus of this study was on the role of transamidating activity, conformation and localization of TG2 in ischemic cell death. Cells expressing a GTP binding deficient form of TG2 (TG2-R580A) with high basal transamidation activity and a more extended conformation showed significantly increased cell death in response to oxygen-glucose deprivation; however, targeting TG2-R580A to the nucleus abrogated its detrimental role in oxygen-glucose deprivation. Treatment of cells expressing wild type TG2, TG2-C277S (a transamidating inactive mutant) and TG2-R580A with Cp4d, a reversible TG2 inhibitor, did not affect cell death in response to oxygen-glucose deprivation. These findings indicate that the pro-cell death effects of TG2 are dependent on its localization to the cytosol and independent of its transamidation activity. Further, the conformational state of TG2 is likely an important determinant in cell survival and the prominent function of TG2 in ischemic cell death is as a scaffold to modulate cellular processes

The Role of Transglutaminase 2 in Ischemic Cell Death

Thesis (Ph.D.)--University of Rochester. School of Medicine & Dentistry. Dept. of Pharmacology and Physiology, 2011.Transglutaminase 2 (TG2) is an enzyme that catalyzes Ca2+ dependent transamidation reactions. TG2 plays a role in many biological functions such as growth, differentiation and inflammation. Intriguingly, TG2 can contribute to both cell survival and cell death. Increased transamidation activity of cytosolic TG2 is proposed to be detrimental, while nuclear localization of TG2 is critical for its prosurvival effects. However, it is still not clear what determines the pro-death and prosurvival roles of TG2 in the cells. Our goal in this study was to examine the role of TG2 in ischemic cell death. In the first part, we used a constitutive transamidation active (R580A) point mutant of TG2 to analyze the role of transamidation activity in ischemic cell death. R580A significantly induced cell death in response to OGD, however this effect was independent of its high transamidation activity. The detrimental affect of R580A was fully abrogated when the protein was translocated to the nucleus. These experiments also indicated that the open conformation of R580A might induce cell death in response to ischemic stress. Finally, our results show that the detrimental role of TG2 is mainly cytosolic, dependent on its conformational state and independent of its transamidation activity. In the second part of this study, we investigated the role of endogenous TG2 in ischemic cell death. Previously, we showed that neuronal selective TG2 overexpressor mice were protected against ischemic stroke. In this study, we used complete embryonic TG2 knock out (TG2-/-) mice. Interestingly, TG2-/- mice were also protected against ischemic stroke. Neurons isolated from TG2-/- mice showed diminished cell viability, however TG2-/- astrocytes were resistant to OGD-induced cell death. Further, wild type and TG2-/- neurons were both protected against OGDinduced cell death when they were co-cultured with TG2-/- astrocytes. These data suggest that the increased viability of TG2-/- astrocytes may contribute to reduction in stroke volumes in TG2-/- mice. TG2-/- astrocytes might also promote the survival of neurons after ischemic insult through neuron-astrocyte cross talk. In conclusion, our study shows that TG2 can be both detrimental and prosurvival in ischemic cell death depending on its conformational state, cellular localization and the cell type

Transglutaminase 2: A molecular Swiss army knife

AbstractTransglutaminase 2 (TG2) is the most widely distributed member of the transglutaminase family with almost all cell types in the body expressing TG2 to varying extents. In addition to being widely expressed, TG2 is an extremely versatile protein exhibiting transamidating, protein disulphide isomerase and guanine and adenine nucleotide binding and hydrolyzing activities. TG2 can also act as a protein scaffold or linker. This unique protein also undergoes extreme conformational changes and exhibits localization diversity. Being mainly a cytosolic protein; it is also found in the nucleus, associated with the cell membrane (inner and outer side) and with the mitochondria, and also in the extracellular matrix. These different activities, conformations and localization need to be carefully considered while assessing the role of TG2 in physiological and pathological processes. For example, it is becoming evident that the role of TG2 in cell death processes is dependent upon the cell type, stimuli, subcellular localization and conformational state of the protein. In this review we discuss in depth the conformational and functional diversity of TG2 in the context of its role in numerous cellular processes. In particular, we have highlighted how differential localization, conformation and activities of TG2 may distinctly mediate cell death processes

Transglutaminase 2 facilitates or ameliorates HIF signaling and ischemic cell death depending on its conformation and localization

AbstractTransglutaminase 2 (TG2) is a widely expressed and multifunctional protein that modulates cell death/survival processes. We have previously shown that TG2 binds to hypoxia inducible factor 1β (HIF1β) and decreases the upregulation of HIF responsive genes; however, the relationship between these observations was not investigated. In this study, we investigated whether endogenous TG2 is sufficient to suppress HIF activity and whether the interaction between TG2 and HIF1β is required for this suppression. shRNA-mediated silencing of TG2 significantly enhanced HIF activation in response to hypoxia. In addition, nuclear localization of TG2 is required for its suppressive effect on HIF activity, with TG2 being recruited to HIF responsive promoters in hypoxic conditions. These observations suggest that TG2 directly regulates hypoxic transcriptional machinery; however, its interaction with HIF1β was not required for this regulation. We also examined whether TG2's effect on cell death/survival processes in ischemia is due to its effects on HIF signaling. Our results indicate that TG2 mediated HIF suppression can be separated from TG2's effect on cell survival in hypoxic/hypoglycemic conditions. Lastly, here we show that nuclear TG2 in the closed conformation and non-nuclear TG2 in the open conformation have opposing effects on hypoxic/hypoglycemic cell death, which could explain previous controversial results. Overall, our results further clarify the role of TG2 in mediating the cellular response to ischemia and suggest that manipulating the conformation of TG2 might be of pharmacological interest as a therapeutic strategy for the treatment of ischemia-related pathologies