TY - JOUR
T1 - Quantification of Histone H1 Subtypes Using Targeted Proteomics
AU - Zamora, Lurdes
AU - Roque, Alicia
AU - Andrés, Marta
AU - López-Gómez, Jordi
AU - Ponte, Inma
AU - Vilaseca, Marta
AU - Villarreal, Laura
AU - Xicoy, Blanca
N1 - Publisher Copyright:
© 2024 by the authors.
PY - 2024/9/27
Y1 - 2024/9/27
N2 - Histone H1 is involved in the regulation of chromatin structure. Human somatic cells express up to seven subtypes. The variability in the proportions of somatic H1s (H1 complement) is one piece of evidence supporting their functional specificity. Alterations in the protein levels of different H1 subtypes have been observed in cancer, suggesting their potential as biomarkers and that they might play a role in disease development. We have developed a mass spectrometry-based (MS) parallel reaction monitoring (PRM) assay suitable for the quantification of H1 subtypes. Our PRM method is based on the quantification of unique peptides for each subtype, providing high specificity. Evaluation of the PRM performance on three human cell lines, HeLa, K562, and T47D, showed high reproducibility and sensitivity. Quantification values agreed with the electrophoretic and Western blot data, indicating the accuracy of the method. We used PRM to quantify the H1 complement in peripheral blood samples of healthy individuals and chronic myeloid leukemia (CML) patients. In CML, the first line of therapy is a tyrosine kinase inhibitor, imatinib. Our preliminary data revealed differences in the H1 complement in CML patients between imatinib responders and non-responders. These results support further research to determine if the H1 content or subtype composition could help predict imatinib response.
AB - Histone H1 is involved in the regulation of chromatin structure. Human somatic cells express up to seven subtypes. The variability in the proportions of somatic H1s (H1 complement) is one piece of evidence supporting their functional specificity. Alterations in the protein levels of different H1 subtypes have been observed in cancer, suggesting their potential as biomarkers and that they might play a role in disease development. We have developed a mass spectrometry-based (MS) parallel reaction monitoring (PRM) assay suitable for the quantification of H1 subtypes. Our PRM method is based on the quantification of unique peptides for each subtype, providing high specificity. Evaluation of the PRM performance on three human cell lines, HeLa, K562, and T47D, showed high reproducibility and sensitivity. Quantification values agreed with the electrophoretic and Western blot data, indicating the accuracy of the method. We used PRM to quantify the H1 complement in peripheral blood samples of healthy individuals and chronic myeloid leukemia (CML) patients. In CML, the first line of therapy is a tyrosine kinase inhibitor, imatinib. Our preliminary data revealed differences in the H1 complement in CML patients between imatinib responders and non-responders. These results support further research to determine if the H1 content or subtype composition could help predict imatinib response.
KW - histone H1
KW - functional differentiation
KW - parallel reaction monitoring
KW - imatinib resistance
KW - chronic myeloid leukemia
KW - cancer biomarker
UR - http://www.scopus.com/inward/record.url?scp=85207676030&partnerID=8YFLogxK
UR - https://portalrecerca.uab.cat/en/publications/15090207-3edf-494f-ab54-3987bff07360
U2 - 10.3390/biom14101221
DO - 10.3390/biom14101221
M3 - Article
C2 - 39456154
AN - SCOPUS:85207676030
SN - 2218-273X
VL - 14
JO - Biomolecules
JF - Biomolecules
IS - 10
M1 - 1221
ER -