hosnie hoseini; Parichehreh Yaghmaei; Gholamreza Bahari; Saeed Aminzadeh
Volume 22, Issue 11 , 2020
Abstract
Background: The activities of programmed cell death 1 (PD-1) and programmed death ligand-1 (PD-L1) have already been identified in various cancers. However, in non-Hodgkin?s lymphoma (NHL), the prognostic value of PD-1/PD-L1 gene polymorphisms and expression levels remains unclear.
Objectives: The present ...
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Background: The activities of programmed cell death 1 (PD-1) and programmed death ligand-1 (PD-L1) have already been identified in various cancers. However, in non-Hodgkin?s lymphoma (NHL), the prognostic value of PD-1/PD-L1 gene polymorphisms and expression levels remains unclear.
Objectives: The present study aimed to investigate the relationship between the genetic polymorphisms of PD-1/PD-L1 genes and NHL in the Iranian population.
Methods: Four single-nucleotide polymorphisms (SNPs) of PD-1/PD-L1 genes were examined in 134 NHL patients and 134 healthy controls using polymerase chain reaction-restriction fragment length polymorphism. The expression levels of PD-1/PD-L1 genes were analyzed using real-time polymerase chain reaction.
Results: The obtained results of the current study demonstrated that PD-L1 rs2890685 (A>C) SNP (P<0.0001) was significantly associated with the increased risk of NHL. The AA genotype of PD-L1 rs2890685 polymorphism was observed to be more prevalent in the NHL patients, compared to that reported for the healthy controls. There was no significant association between PD-L1 rs4143815, PD-1 rs11568821, and PD-1rs2227981 SNPs with the risk of NHL. Furthermore, the obtained findings showed that the messenger ribonucleic acid transcription levels of both PD-1 and PD-L1 were significantly higher in the NHL patients than those reported for the healthy controls (P<0.001).
Conclusion: According to the results of the current study, there was an association between functional PD-L1 rs2890685 polymorphism and risk of NHL, suggesting that the genetic variant of PD-L1 might be a possible prognostic marker for the prediction of the risk and development of NHL.
Pooneh Amini-Geram; Fatemeh Goshadrou; Azadeh Ebrahim-Habibi; Parichehreh Yaghmaei; Saeed Hesami-Tackallou
Volume 19, Issue 3 , March 2017, , Pages 1-8
Abstract
Background: Glucose is an essential element in the supply of body’s energy. In diseases such as diabetes, glucose increase is associated with disturbance in metabolism.Cortisol is an important hormone in the regulation of glucose metabolism, and human serum albumin (HSA) is one of the most important ...
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Background: Glucose is an essential element in the supply of body’s energy. In diseases such as diabetes, glucose increase is associated with disturbance in metabolism.Cortisol is an important hormone in the regulation of glucose metabolism, and human serum albumin (HSA) is one of the most important glucose and cortisol transmitters in blood. Interaction between albumin and these ligands could affect HSA secondary structure and its stability.Objectives: The aim of this study was to investigate HSA secondary structure in the presence of different concentrations of glucose and cortisol.Methods: This was an in vitro (analytical/descriptive) study in which, completely randomized design was used to study the interaction between human serum albumin at 37°C at different glucose concentrations of 0, 80, 180, 240, and 400 mg/dL and cortisol at concentrations of 0, 10, 20, and 40µg/dL. Intrinsic fluorescence spectroscopy and Circular dichroism (CD) were performed to obtain data.Results: HSA secondary structure underwent changes in the presence of different concentrations of cortisol and glucose. P values less than 0.01 were considered to be statistically significant. Fluorescence spectroscopy and CD results showed that at normal glucose concentrations, HSA was very flexible, beta-sheet content reduced, andthe maximum increase in fluorescence and blue-shift happened. At higher concentrations of glucose, HSA became rigid. Also, HSA in presence of 10 µg/dL cortisol was very flexible; but a cortisol concentration of 40 µg/dL caused stability in HSA structure in presence of different glucose concentrations.Conclusions: Under normal glucose conditions, very low cortisol concentrations create large changes in HSA secondary structure. At normal glucose concentrations, some of the binding sites of HSA that are all occupied by glucose at higher concentrations become available to cortisol. Cortisol structure is very hydrophobic, which causes large changes in HSA secondary structure and significant increases in quenching and blue shift. In conclusion, binding of compounds such as medicines to HSA sites may be affected by competitive bindings of glucose, depending on its concentration in the blood.
