Your browser doesn't support javascript.
loading
A coupled enzyme assay for detection of selenium-binding protein 1 (SELENBP1) methanethiol oxidase (MTO) activity in mature enterocytes.
Philipp, Thilo Magnus; Will, Andreas; Richter, Hannes; Winterhalter, Patrick Rainer; Pohnert, Georg; Steinbrenner, Holger; Klotz, Lars-Oliver.
Afiliación
  • Philipp TM; Institute of Nutritional Sciences, Nutrigenomics Section, Friedrich Schiller University Jena, Jena, Germany.
  • Will A; Institute of Nutritional Sciences, Nutrigenomics Section, Friedrich Schiller University Jena, Jena, Germany.
  • Richter H; Institute for Inorganic and Analytical Chemistry, Friedrich Schiller University Jena, Jena, Germany.
  • Winterhalter PR; Department of Cardiac Surgery, Martin Luther University Halle-Wittenberg, Halle, Germany.
  • Pohnert G; Institute for Inorganic and Analytical Chemistry, Friedrich Schiller University Jena, Jena, Germany.
  • Steinbrenner H; Institute of Nutritional Sciences, Nutrigenomics Section, Friedrich Schiller University Jena, Jena, Germany.
  • Klotz LO; Institute of Nutritional Sciences, Nutrigenomics Section, Friedrich Schiller University Jena, Jena, Germany. Electronic address: lars-oliver.klotz@uni-jena.de.
Redox Biol ; 43: 101972, 2021 07.
Article en En | MEDLINE | ID: mdl-33901808
Methanethiol, a gas with the characteristic smell of rotten cabbage, is a product of microbial methionine degradation. In the human body, methanethiol originates primarily from bacteria residing in the lumen of the large intestine. Selenium-binding protein 1 (SELENBP1), a marker protein of mature enterocytes, has recently been identified as a methanethiol oxidase (MTO). It catalyzes the conversion of methanethiol to hydrogen sulfide (H2S), hydrogen peroxide (H2O2) and formaldehyde. Here, human Caco-2 intestinal epithelial cells were subjected to enterocyte-like differentiation, followed by analysis of SELENBP1 levels and MTO activity. To that end, we established a novel coupled assay to assess MTO activity mimicking the proximity of microbiome and intestinal epithelial cells in vivo. The assay is based on in situ-generation of methanethiol as catalyzed by a bacterial recombinant l-methionine gamma-lyase (MGL), followed by detection of H2S and H2O2. Applying this assay, we verified the loss and impairment of MTO function in SELENBP1 variants (His329Tyr; Gly225Trp) previously identified in individuals with familial extraoral halitosis. MTO activity was strongly enhanced in Caco-2 cells upon enterocyte differentiation, in parallel with increased SELENBP1 levels. This suggests that mature enterocytes located at the tip of colonic crypts are capable of eliminating microbiome-derived methanethiol.
Asunto(s)
Palabras clave
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Enterocitos / Proteínas de Unión al Selenio Tipo de estudio: Diagnostic_studies / Prognostic_studies Límite: Humans Idioma: En Revista: Redox Biol Año: 2021 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Países Bajos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Enterocitos / Proteínas de Unión al Selenio Tipo de estudio: Diagnostic_studies / Prognostic_studies Límite: Humans Idioma: En Revista: Redox Biol Año: 2021 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Países Bajos