Dataset Information

PRM of UMR106 pY-IP

ABSTRACT: UMR106 cells were untreated or treated with 5 mM Pi or 100 ng/ml FGF2 for 15 min. The lysates were digested with trypsin, and tyrosine-phosphorylated peptides were enriched by anti-phosphotyrosine antibody. Several selected peptides including FGFR1 with phosphorylated tyrosine residues were measured by PRM. Time alignment and relative quantification of the transitions were performed with PinPoint version 1.4.

ORGANISM(S): Rattus Rattus (black Rat)

SUBMITTER: Hidetaka Kosako

PROVIDER: PXD010791 | JPOST Repository | Sun May 05 00:00:00 BST 2019

REPOSITORIES: jPOST

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Publications

Activation of unliganded FGF receptor by extracellular phosphate potentiates proteolytic protection of FGF23 by its O-glycosylation.

Takashi Yuichi Y Kosako Hidetaka H Sawatsubashi Shun S Kinoshita Yuka Y Ito Nobuaki N Tsoumpra Maria K MK Nangaku Masaomi M Abe Masahiro M Matsuhisa Munehide M Kato Shigeaki S Matsumoto Toshio T Fukumoto Seiji S

Proceedings of the National Academy of Sciences of the United States of America 20190516 23

Fibroblast growth factor (FGF) 23 produced by bone is a hormone that decreases serum phosphate (Pi). Reflecting its central role in Pi control, serum FGF23 is tightly regulated by serum Pi alterations. FGF23 levels are regulated by the transcriptional event and posttranslational cleavage into inactive fragments before its secretion. For the latter, O-glycosylation of FGF23 by <i>GALNT3</i> gene product prevents the cleavage, leading to an increase in serum FGF23. However, the molecular basis of ...[more]

PMID: 31097591

Similar Datasets

Project description:Targeted mass spectrometry (MS) approaches, which are powerful methods for uniquely and confidently quantifying a specific panel of proteins in complex biological samples, play a crucial role in validation and clinical translation of protein biomarkers discovered by global proteomic profiling. Common targeted MS methods, such as multiple reaction monitoring (MRM) and parallel-reaction monitoring (PRM), employ specific mass spectrometric technologies to quantify protein levels by comparing the transitions of specific endogenous (Endo) peptides with those of stable isotope labeled (SIL) peptide counterparts. These methods utilizing amino acid analyzed (AAA) SIL peptides warrants sensitive and precise measurements required for targeted MS assays. Compared to MRM, PRM provides higher experimental throughput by simultaneously acquiring all transitions of the target peptides and thereby compensate for different ion suppression among transitions of a target peptide. However, PRM still suffers different ion suppressions between Endo and SIL peptides due to poor spray stability as the Endo and SIL peptides were monitored at different liquid chromatography (LC) retention times. Here we introduce a new targeted MS method, termed as wideband PRM (WBPRM), designed for high-throughput targeted MS approach. WBPRM employs a wide isolation window for simultaneous fragmentations of both Endo and SIL peptides along with multiplexed single ion monitoring (SIM) scans for enhanced MS sensitivity of target peptides. Compared to PRM, WBPRM was demonstrated to provide increased sensitivity, precision, and accuracy of quantitative measurements of target peptides with increased throughput, allowing more target peptide measurements in a short experiment time. Its adaptability to a MS method provided by the manufacture makes it a facile method to implement for MS based assays, particularly in complex biological samples, where the needs for higher accuracy, sensitivity and efficiency are paramount.

			Action	DRS
	PRM_UMR106_pY_FGF2_1.raw	Raw
	PRM_UMR106_pY_FGF2_2.raw	Raw
	PRM_UMR106_pY_FGF2_3.raw	Raw
	PRM_UMR106_pY_Pi_1.raw	Raw
	PRM_UMR106_pY_Pi_2.raw	Raw