Proteomics of Ishikawa endometrial cancer cells: impact of liposomal backbone.
Endometrial cells
LC-MS/MS
Liposomes
Phosphatidylcholine
Proteomics
Journal
BMC research notes
ISSN: 1756-0500
Titre abrégé: BMC Res Notes
Pays: England
ID NLM: 101462768
Informations de publication
Date de publication:
02 Sep 2024
02 Sep 2024
Historique:
received:
12
05
2024
accepted:
01
08
2024
medline:
3
9
2024
pubmed:
3
9
2024
entrez:
2
9
2024
Statut:
epublish
Résumé
The Ishikawa cell line is the most widely used model system for investigating implantation and endometrial cancer. Understanding the biology of this cell line is essential for developing effective interventional strategies. To gain a deeper understanding of its cellular protein profile, we extracted cellular proteins from Ishikawa cells and analyzed the peptides using mass spectrometry. Our goal was to create a proteomic resource specifically tailored for Ishikawa cells. This data set is of particular significance in the realm of targeted drug delivery. Liposomes are synthetic spherical vesicles composed of hydrophobic bilayer phospholipids and have received immense recognition as highly effective carriers for the delivery of pharmaceutical drugs and essential nutrients to the endometrium. Phosphatidylcholine and phosphatidylethanolamine are often combined to create functional liposomal systems. To discern any potential interfering effects originating from the liposome backbone, our investigation involved direct effects of phospholipid liposomes on endometrial epithelial cells. The data set includes peptide spectra derived from the intracellular proteomes of Ishikawa endometrial cancer cell isolates and their phospholipid-treated counterparts. Representing a proteome-wide profile, this dataset aims to contribute to a broader understanding of the physiology of endometrial epithelial cells. Proteomic analysis identified key proteins involved in the intricate regulation of cellular metabolism, cell cycle progression, and signaling. Between-group analysis revealed no differentially expressed proteins after adjusting for multiple testing using the applied thresholds (p-value < 0.05 and |logFC| > 1). Data are available via ProteomeXchange with identifier PXD050871.
Identifiants
pubmed: 39223611
doi: 10.1186/s13104-024-06885-7
pii: 10.1186/s13104-024-06885-7
doi:
Substances chimiques
Liposomes
0
Proteome
0
Phosphatidylethanolamines
0
Phosphatidylcholines
0
phosphatidylethanolamine
39382-08-6
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
239Informations de copyright
© 2024. The Author(s).
Références
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