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1.
Eur J Transl Myol ; 33(2)2023 Jun 15.
Article in English | MEDLINE | ID: mdl-37325930

ABSTRACT

This report presents socio-demographic data of gender incongruent patients, searching for gender affirming medical care (GAMC) in Russia by retrospective medical records analysis of patients. Data of 1117 patients were included in the analysis. Over the period from 2014 to 2021, there was a significant increase in the number of applications (+123.2%). Among all transgender individuals 44.01% were trans femine (MtF) and 55.99% (n=630) were trans masculine (FtM), 1.2% was non-binary persons. The average age for GAMC application in MtF was 26 years and in FtM was 23 years. Majority of patients experienced gender incongruence (GI) since pre-pubertal age (median 11.0). Age of acceptance oneself as a "transgender " was 17.0 years, earlier in FtM, later in MtF. The first coming-out was made at 20 (22 for MtF, 19 for FtM). Depression was diagnosed in 82,4% cases,12.6% of patients have suicide attempts. 53.6%, were already taking hormonal therapy (76.7% MtF, 32.3% FtM). The Russian transgender population is big, stigmatized, ethnically and culturally heterogeneous group, that has little visibility. Further research is essentials for formation of professional attitude in the medical environment.

2.
Am J Physiol Cell Physiol ; 286(4): C848-56, 2004 Apr.
Article in English | MEDLINE | ID: mdl-14656720

ABSTRACT

Many xenobiotics are detoxified through the mercapturate metabolic pathway. The final product of the pathway, mercapturic acids (N-acetylcysteine S-conjugates), are secreted predominantly by renal proximal tubules. Mercapturic acids may undergo a transformation mediated by aminoacylases and cysteine S-conjugate beta-lyases that leads to nephrotoxic reactive thiol formation. The deacetylation of cysteine S-conjugates of N-acyl aromatic amino acids is thought to be mediated by an aminoacylase whose molecular identity has not been determined. In the present study, we cloned aminoacylase III, which likely mediates this process in vivo, and characterized its function and structure. The enzyme consists of 318 amino acids and has a molecular mass (determined by SDS-PAGE) of approximately 35 kDa. Under nondenaturing conditions, the molecular mass of the enzyme is approximately 140 kDa as determined by size-exclusion chromatography, which suggests that it is a tetramer. In agreement with this hypothesis, transmission electron microscopy and image analysis of aminoacylase III showed that the monomers of the enzyme are arranged with a fourfold rotational symmetry. Northern analysis demonstrated an approximately 1.4-kb transcript that was expressed predominantly in kidney and showed less expression in liver, heart, small intestine, brain, lung, testis, and stomach. In kidney, aminoacylase III was immunolocalized predominantly to the apical domain of S1 proximal tubules and the cytoplasm of S2 and S3 proximal tubules. The data suggest that in kidney proximal tubules, aminoacylase III plays an important role in deacetylating mercapturic acids. The predominant cytoplasmic localization of aminoacylase III may explain the greater sensitivity of the proximal straight tubule to the nephrotoxicity of mercapturic acids.


Subject(s)
Acetylcysteine/metabolism , Amidohydrolases/genetics , Kidney Tubules, Proximal/enzymology , Amidohydrolases/chemistry , Amidohydrolases/metabolism , Amino Acid Sequence , Animals , Cell Line , Cloning, Molecular , Gene Expression , Humans , Kinetics , Mice , Microscopy, Electron , Molecular Sequence Data , Protein Structure, Quaternary
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