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Arslan Hande,Özdemir Meltem,Kavak Rasime Pelin,Keseroğlu Kemal,Mutlu Murad,Korkmaz Mehmet Hakan 대한청각학회 2024 Journal of Audiology & Otology Vol.28 No.1
Background and Objectives: Idiopathic sudden sensorineural hearing loss (ISSHL) is a rapid loss of hearing, exceeding 30 dB in at least 3 consecutive frequencies within 3 days, without any identifiable cause despite thorough investigations. Currently, the etiology and pathogenesis of ISSHL have not been fully elucidated. This study aimed to assess the size of the cochlear nerve in patients with ISSHL and explore its relationship with pretreatment audiograms and treatment response.Subjects and Methods: A total of 125 patients (59 [47.2%] women; mean age 47.7±13.8 years [minimum-maximum: 21-76]) and 60 healthy participants (27 [45%] women; mean age 45.7±16.8 years [minimum-maximum: 20-76]) as a control group were included in this study. The size of the cochlear nerve was assessed on the affected side, compared to the control group, as well as on the unaffected side. Pretreatment and posttreatment audiological values were also analyzed.Results: The cross-sectional area (CSA), vertical diameter (VD), and horizontal diameter (HD) of the CN were found to be smaller on the affected side of ISSHL patients compared to the control group (p<0.01; p=0.04; p=0.02, respectively). In the study group (affected side of ISSHL patients), there were no significant differences in VD, HD, and CSA values between pretreatment audiogram types (p=0.23; p=0.53; p=0.39, respectively), and initial hearing levels (p=0.16; p=0.22; p=0.23, respectively). Furthermore, there were no significant differences in VD, HD, and CSA values between the recovery groups according to Furuhashi criteria (p=0.18; p=0.37; p=0.27, respectively).Conclusions: The size of the CN may be a risk factor for ISSHL, but it does not affect the type of audiogram curves and was not prognostic in terms of treatment response.
Krisztina Szirák,Judit Keserű,Sándor Biró,Iván Schmelczer,György Barabás,András Penyige 한국미생물학회 2012 The journal of microbiology Vol.50 No.3
The SCO5461 gene of Streptomyces coelicolor A3(2) codes for an ADP-ribosyltransferase enzyme that is predicted to be a transmembrane protein with an extracellular catalytic domain. PCR-targeted disruption of the gene resulted in a mutant that differentiated normally on complex SFM medium; however, morphological differentiation in minimal medium was significantly delayed and this phenotype was even more pronounced on osmotically enhanced minimal medium. The mutant did not sporulate when it was grown on R5 medium, however the normal morphological differentiation was restored when the strain was cultivated beside the wild-type S. coelicolor M145 strain. Comparison of the pattern of ADP-ribosylated proteins showed a difference between the mutant and the wild type, fewer modified proteins were present in the cellular crude extract of the mutant strain. These results support our previous suggestions that protein ADP-ribosylation is involved in the regulation of differentiation and antibiotic production and secretion in Streptomyces.
Analysis and Identification of ADP-Ribosylated Proteins of Streptomyces coelicolor M145
András Penyige,Judit Keserű,Ferenc Fazakas,Iván Schmelczer,Krisztina Szirák,György Barabás,Sándor Biró 한국미생물학회 2009 The journal of microbiology Vol.47 No.5
Mono-ADP-ribosylation is the enzymatic transfer of ADP-ribose from NAD+ to acceptor proteins catalyzed by ADP-ribosyltransferases. Using m-aminophenylboronate affinity chromatography, 2D-gel electrophoresis, in-gel digestion and MALDI-TOF analysis we have identified eight in vitro ADP-ribosylated proteins in Streptomyces coelicolor, which can be classified into three categories: (i) secreted proteins; (ii) metabolic enzymes using NAD+/NADH or NADP+/NADPH as coenzymes; and (iii) other proteins. The secreted proteins could be classified into two functional categories: SCO2008 and SCO5477 encode members of the family of periplasmic extracellular solute-binding proteins, and SCO6108 and SCO1968 are secreted hydrolases. Dehydrogenases are encoded by SCO4824 and SCO4771. The other targets are GlnA (glutamine synthetase I., SCO2198) and SpaA (starvation-sensing protein encoded by SCO7629). SCO2008 protein and GlnA had been identified as ADP-ribosylated proteins in previous studies. With these results we provided experimental support for a previous suggestion that ADP-ribosylation may regulate membrane transport and localization of periplasmic proteins. Since ADP-ribosylation results in inactivation of the target protein, ADP-ribosylation of dehydrogenases might modulate crucial primary metabolic pathways in Streptomyces. Several of the proteins identified here could provide a strong connection between protein ADP-ribosylation and the regulation of morphological differentiation in S. coelicolor.