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Phosphoproteomic analyses reveal that galectin-1 augments the dynamics of B-cell receptor signaling

ABSTRACT: we applied label-free quantitative phosphoproteomic analysis to delineate the dynamics of galectin-1-induced signaling in comparison with the first systematic phosphorylation-mediated signaling network in B cell activation by anti-IgM treatment.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): B Cell

SUBMITTER: Hsin-Yi Wu

LAB HEAD: Yu-Ju Chen

PROVIDER: PXD000762 | Pride | 2016-03-15

REPOSITORIES: Pride

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			Action	DRS
	F022814_IgM10m.dat	Other
	F022814_IgM10m.dat-pride.pride.mgf.gz	Mgf
	F022814_IgM10m.dat-pride.pride.mztab.gz	Mztab
	F022814_IgM10m.dat-pride.xml.gz	Xml
	F022814_Igm10min.xml	Xml

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Phosphoproteomic analyses reveal that galectin-1 augments the dynamics of B-cell receptor signaling.

Tsai Chih-Ming CM Wu Hsin-Yi HY Su Tseng-Hsiung TH Kuo Chu-Wei CW Huang Han-Wen HW Chung Cheng-Han CH Chen Chien-Sin CS Khoo Kay-Hooi KH Chen Yu-Ju YJ Lin Kuo-I KI

Journal of proteomics 20140403

B-cell activation is important for mounting humoral immune responses and antibody production. Galectin-1 has multiple regulatory functions in immune cells. However, the effects of galectin-1 modulation and the mechanisms underlying the coordination of B-cell activation are unclear. To address this issue, we applied label-free quantitative phosphoproteomic analysis to investigate the dynamics of galectin-1-induced signaling in comparison with that following anti-IgM treatment. A total of 3247 pho ...[more]

PMID: 24704852

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