The phytase RipBL1 enables the assignment of a specific inositol phosphate isomer as a structural component of human kidney stones.

Details

Serval ID
serval:BIB_4A25E5BC13DE
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
The phytase RipBL1 enables the assignment of a specific inositol phosphate isomer as a structural component of human kidney stones.
Journal
RSC chemical biology
Author(s)
Liu G., Riemer E., Schneider R., Cabuzu D., Bonny O., Wagner C.A., Qiu D., Saiardi A., Strauss A., Lahaye T., Schaaf G., Knoll T., Jessen J.P., Jessen H.J.
ISSN
2633-0679 (Electronic)
ISSN-L
2633-0679
Publication state
Published
Issued date
05/04/2023
Peer-reviewed
Oui
Volume
4
Number
4
Pages
300-309
Language
english
Notes
Publication types: Journal Article
Publication Status: epublish
Abstract
Inositol phosphates (InsPs) are ubiquitous in all eukaryotes. However, since there are 63 possible different phosphate ester isomers, the analysis of InsPs is challenging. In particular, InsP <sub>1</sub> , InsP <sub>2,</sub> and InsP <sub>3</sub> already amass 41 different isomers, of which some occur as enantiomers. Profiling of these "lower" inositol phosphates in mammalian tissues requires powerful analytical methods and reference compounds. Here, we report an analysis of InsP <sub>2</sub> and InsP <sub>3</sub> with capillary electrophoresis coupled to electrospray ionization mass spectrometry (CE-ESI-MS). Using this method, the bacterial effector RipBL1 was analyzed and found to degrade InsP <sub>6</sub> to Ins(1,2,3)P <sub>3</sub> , an understudied InsP <sub>3</sub> isomer. This new reference molecule then aided us in the assignment of the isomeric identity of an InsP <sub>3</sub> while profiling human samples: in urine and kidney stones, we describe for the first time the presence of defined and abundant InsP <sub>3</sub> isomers, namely Ins(1,2,3)P <sub>3</sub> , Ins(1,2,6)P <sub>3</sub> and/or Ins(2,3,4)P <sub>3</sub> .
Keywords
Biochemistry, Genetics and Molecular Biology (miscellaneous), Molecular Biology, Biochemistry, Chemistry (miscellaneous)
Pubmed
Web of science
Open Access
Yes
Funding(s)
Swiss National Science Foundation / 182312
Swiss National Science Foundation / 183774
Create date
27/02/2023 12:20
Last modification date
17/11/2023 8:10
Usage data