Uncovering the glutamate carboxypeptidase II microenvironment using a multi-labeling proteomic approach
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F25%3A00642428" target="_blank" >RIV/61388963:_____/25:00642428 - isvavai.cz</a>
Alternative codes found
RIV/61389013:_____/25:00642428 RIV/00216208:11110/25:10507474
Result on the web
<a href="https://doi.org/10.1038/s41598-025-28826-5" target="_blank" >https://doi.org/10.1038/s41598-025-28826-5</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41598-025-28826-5" target="_blank" >10.1038/s41598-025-28826-5</a>
Alternative languages
Result language
angličtina
Original language name
Uncovering the glutamate carboxypeptidase II microenvironment using a multi-labeling proteomic approach
Original language description
Glutamate carboxypeptidase II (GCPII) is a membrane-bound metallopeptidase predominantly expressed in neural and prostatic tissues, with significantly elevated levels in prostate carcinoma that increase with tumor grade. Despite its significance as a target for imaging and therapy in prostate cancer, its physiological function in this tissue remains poorly understood. To help fill this knowledge gap, we developed an integrated approach combining proximity labeling technologies for proteomic profiling (horseradish peroxidase, µMap, and riboflavin tetraacetate labeling) with our previously established iBody platform, which targets GCPII with a small-molecule specific inhibitor with proven efficacy as a chemical probe. Proximity labeling proteomic experiments on U251 MG–GCPII cells were followed by mass spectrometry and statistical analysis of protein abundances obtained by label-free quantification. Additionally, selected identified proteins were further validated through Western blot analyses and GCPII pulldown assays using cell lysates. This work identifies a network of GCPII-associated proteins that are potentially involved in cancer metabolism, migration, invasiveness, progression, and immune evasion. Our novel proximity proteomics labeling strategy provides a low-background framework, efficient biotinylation, and enhanced target binding via the avidity effect. Among the approaches tested, riboflavin tetraacetate-based iBody labeling exhibited the highest precision, underscoring its potential for membrane protein interactome mapping.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Scientific Reports
ISSN
2045-2322
e-ISSN
2045-2322
Volume of the periodical
15
Issue of the periodical within the volume
November
Country of publishing house
GB - UNITED KINGDOM
Number of pages
10
Pages from-to
45461
UT code for WoS article
001651032800004
EID of the result in the Scopus database
2-s2.0-105026374410