作者: Yeong Hee Ahn , Yong-Sam Kim , Eun Sun Ji , Ji Yeon Lee , Ji-Ae Jung
DOI: 10.1021/AC1001965
关键词: Matrix metalloproteinase 、 Protein tyrosine phosphatase 、 Molecular biology 、 Mass spectrometry 、 Lectin 、 Selected reaction monitoring 、 Tissue inhibitor of metalloproteinase 、 TIMP1 、 Glycoprotein 、 Chemistry
摘要: Lectin enrichment-coupled multiple-reaction monitoring (MRM) mass spectrometry was employed to quantitatively monitor the variation of aberrant glycoforms produced under pathological states. For this, tissue inhibitor metalloproteinase 1 (TIMP1) and protein tyrosine phosphatase κ (PTPκ), previously known target proteins for N-acetylglucosaminyltransferase-V (GnT-V), were enriched by phytohemagglutinin-L4 (L-PHA) lectin comparatively analyzed in conditioned medium WiDr colon cancer cell line its GnT-V-overexpressing transfectant cells. Enriched digested, resultant peptides quantified MRM analysis. quantitation data L-PHA-enriched samples revealed that abundance TIMP1 PTPκ greatly increased (11.7- 16.5-fold, respectively) GnT-V-treated cells compared control cells, although total slightly diff...