What question did this study set out to answer?

Identify post-translational modifications of plasma proteins associated with pancreatic cancer using high-throughput mass spectrometry.

August 21, 2009Journal of Biological ChemistryOpen Access

Prolyl 4-Hydroxylation of α-Fibrinogen

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Identify post-translational modifications of plasma proteins associated with pancreatic cancer using high-throughput mass spectrometry.
Screened plasma samples from 38 pancreatic cancer patients and 39 healthy controls using the label-free 2DICAL liquid chromatography-mass spectrometry platform.
Developed a novel monoclonal antibody (11A5) to measure prolyl-hydroxylated alpha-fibrinogen levels and identify the modifying enzyme.
Analyzed 685 clinical blood samples via competitive enzyme-linked immunosorbent assay to evaluate biomarker fluctuations across patient health states.
Identified novel prolyl hydroxylation on alpha-fibrinogen, which is specifically mediated by the key enzyme prolyl 4-hydroxylase A1.
Demonstrated marked elevation of prolyl-hydroxylated alpha-fibrinogen in pancreatic cancer plasma compared with healthy controls.
Observed dynamic, state-dependent variations in prolyl-hydroxylated alpha-fibrinogen concentrations across 685 clinical blood samples.

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Implication

Comparative proteomic analysis reveals elevated prolyl-hydroxylated alpha-fibrinogen in pancreatic cancer patients, highlighting its dynamic regulation across clinical states.

Cite This Study

Ono et al. (2009) studied this question.

synapsesocial.com/papers/6a6df28e2163a0a01bc3065f https://doi.org/10.1074/jbc.m109.041749

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Implication

Comparative proteomic analysis reveals elevated prolyl-hydroxylated alpha-fibrinogen in pancreatic cancer patients, highlighting its dynamic regulation across clinical states.

Prolyl 4-Hydroxylation of α-Fibrinogen

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Discussion

Implication

Cite This Study

Prolyl 4-Hydroxylation of α-Fibrinogen

Key Points

Discussion

Implication

Cite This Study

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