Significance of Biochemical Difference between Childhood Nephrotic Syndrome with UTI and without UTI

Background: Nephrotic syndrome is one of most common renal disease in childhood and infection is one of the most important complication in this disease. Infection increase the mortality and morbidity of this type of patients. Most common infection is UTI. So through this study we can able to determine biochemical difference between childhood nephrotic syndrome with Urinary Tract Infection (UTI) and with out UTI patients and its clinical significance. Objective: To determine the biochemical different in childhood nephrotic syndrome patients and its relation with urinary tract infection. Materials and Methods: It is prospective study done in pediatric department in Rajshahi Medical College Hospital, 60 patient of both sex age between 1-12 years, diagnosed as idiopathic nephrotic syndrome with and without UTI were included in this study. Data collection ware done by history taking, clinical examination, laboratory investigations and followed up. Patients were followed up till cure of UTI and remission of proteinuria. After data collection statistical analysis were done by computerized software. Results: In our study we found there were biochemical difference between childhood nephrotic syndrome with UTI and without UTI patients. In patients of nephrotic syndrome with UTI serum albumin decrease significantly and serum cholesterol increase significantly than nephritic syndrome without UTI patients. Conclusion: Child with nephrotic with UTI patients had lower serum albumin and higher serum cholesterol than nephrotic syndrome without UTI patients and it effect the morbidity mortality of this patients. KYAMC Journal.2021;12(1): 22-25

Brain positron emission tomography with 2-18F-2-deoxi-D-glucose of patients with dystonia and essential tremor detects differences between these disorders

We studied patients with dystonia (D) and essential tremor (ET) using positron emission tomography (PET) equipped with Cortex ID software. This allowed PET brain visualisation to be compared to scans of a control group by means of the z-score. The study revealed hypo-metabolism in both D and ET groups, and additionally revealed a difference between these two groups of patients in certain areas of the brain. These two nosological forms overlap in clinical features and are difficult to differentiate. The PET picture may help to provide a differential diagnosis in addition to the biochemical difference in dopamine exchange previously revealed by us in this group of patients.

A Sequence of the CIS Gene Promoter Interacts Preferentially with Two Associated STAT5A Dimers: a Distinct Biochemical Difference between STAT5A and STAT5B

ABSTRACT Two distinct genes encode the closely related signal transducer and activator of transcription proteins STAT5A and STAT5B. The molecular mechanisms of gene regulation by STAT5 and, particularly, the requirement for both STAT5 isoforms are still undetermined. Only a few STAT5 target genes, among them the CIS (cytokine-inducible SH2-containing protein) gene, have been identified. We cloned the human CIS gene and studied the human CIS gene promoter. This promoter contains four STAT binding elements organized in two pairs. By electrophoretic mobility shift assay studies using nuclear extracts of UT7 cells stimulated with erythropoietin, we showed that these four sequences bound to STAT5-containing complexes that exhibited different patterns and affinities: the three upstream STAT binding sequences bound to two distinct STAT5-containing complexes (C0 and C1) and the downstream STAT box bound only to the slower-migrating C1 band. Using nuclear extracts from COS-7 cells transfected with expression vectors for the prolactin receptor, STAT5A, and/or STAT5B, we showed that the C1 complex was composed of a STAT5 tetramer and was dependent on the presence of STAT5A. STAT5B lacked this property and bound with a stronger affinity than did STAT5A to the four STAT sequences as a homodimer (C0 complex). This distinct biochemical difference between STAT5A and STAT5B was confirmed with purified activated STAT5 recombinant proteins. Moreover, we showed that the presence on the same side of the DNA helix of a second STAT sequence increased STAT5 binding and that only half of the palindromic STAT binding sequence was sufficient for the formation of a STAT5 tetramer. Again, STAT5A was essential for this cooperative tetrameric association. This property distinguishes STAT5A from STAT5B and could be essential to explain the transcriptional regulation diversity of STAT5.