Effect of citalopram and sertraline on the expression of miRNA- 124, 132, and 16 and their protein targets in patients with depression

Objectives This study aimed to evaluate the effect of SSRIs on the expression of miRNAs and their protein targets Materials and Methods In a 100 day open label study of citalopram n 25 and sertraline n 25 levels of miRNA 16 132 and 124 and glucocorticoid receptor GR Brain derived neurotrophic factor BDNF and serotonin transporter SERT protein expression were measured by QRT PCR and western blot in healthy control n 20 patients with depression at the baseline and same patients after 100 days of treatment Results Expression levels of GR and BDNF proteins were lower in the depressed group before treatment as compared with the healthy group i P lt i 0 0001 The SERT level was higher among the depressed group before treatment in comparison with the healthy group i P lt i 0 0001 The level of GR and BDNF significantly increased and SERT expression decreased after receiving sertraline i P lt i 0 05 When the depressed group received citalopram only SERT and GR were altered i P lt i 0 05 Among the microRNAs expression investigated mir 124 and mir 132 were higher and mir 16 was lower among the depressed compared with the healthy group i P lt i 0 0001 Individuals receiving citalopram only showed an increase in the expression of mir 16 while administration of sertraline led to a significant increase in the expression of mir 16 and a decrease in mir 124 and mir 132 i P lt i 0 05 Conclusion This elucidated the relationship between antidepressant treatment and the expression of different microRNA that control gene expression in various pathways involved in depressed patients Receiving SSRI can affect the level of these proteins and their relevant microRNA

A comparative investigation of marginal adaptation and surface defects of MTA and root MTA as two root end filling materials

Keywords: Marginal adaptation, Confocal microscope, Stereomicroscope, MTA, RMTA, Retrograde fillin

Development and characterization of a camelid single-domain antibody directed to human CD22 biomarker

CD22 is a B-cell-specific trans-membrane glycoprotein, which is found on the surface of the most B cells and modulates their function, survival, and apoptosis. Recently, targeting this cell surface biomarker in B-cell malignancies and disorders has attracted a lot of attention. The variable domain of camelid single-chain antibodies (VHH, nanobody) is a form of antibodies with novel properties including small size (15-17 kDa), thermal and chemical stability, high affinity and homology to human antibody sequences. In this study, a novel anti-CD22-specific VHH (Nb) has been developed and characterized by the screening of an immunized phage display library and its binding to CD22+ B cells is evaluated. Produced anti-CD22 VHH had a single protein band about 17 kDa of molecular size in Western blotting and its binding affinity was approximately 9 � 10-9 M. Also, this product had high specificity and it was able to recognize the natural CD22 antigen in CD22+ cell lysate as well as on the cell surface (93). This anti-CD22 VHH with both high affinity and specificity recognizes CD22 antigen well and can be used in diagnosis and treatment of B cell disorders and malignancies. © 2018 International Union of Biochemistry and Molecular Biology, Inc

Development and characterization of a camelid single-domain antibody directed to human CD22 biomarker

CD22 is a B-cell-specific trans-membrane glycoprotein, which is found on the surface of the most B cells and modulates their function, survival, and apoptosis. Recently, targeting this cell surface biomarker in B-cell malignancies and disorders has attracted a lot of attention. The variable domain of camelid single-chain antibodies (VHH, nanobody) is a form of antibodies with novel properties including small size (15-17 kDa), thermal and chemical stability, high affinity and homology to human antibody sequences. In this study, a novel anti-CD22-specific VHH (Nb) has been developed and characterized by the screening of an immunized phage display library and its binding to CD22+ B cells is evaluated. Produced anti-CD22 VHH had a single protein band about 17 kDa of molecular size in Western blotting and its binding affinity was approximately 9 � 10-9 M. Also, this product had high specificity and it was able to recognize the natural CD22 antigen in CD22+ cell lysate as well as on the cell surface (93). This anti-CD22 VHH with both high affinity and specificity recognizes CD22 antigen well and can be used in diagnosis and treatment of B cell disorders and malignancies. © 2018 International Union of Biochemistry and Molecular Biology, Inc