Glycocapture based proteomics for secretome analysis英文电子书.pdf

512 DOI 10.1002/pmic.201200414 Proteomics 2013, 13, 512–525 REVIEW Glycocapture-based proteomics for secretome analysis 1 2 1,3 Zon W. Lai , Edouard C. Nice and Oliver Schilling 1 Institute for Molecular Medicine and Cell Research, University of Freiburg, Freiburg, Germany 2 Department of Biochemistry and Molecular Biology, Monash University, VIC, Australia 3 BIOSS Centre for Biological Signaling Studies, University of Freiburg, Freiburg, Germany Protein glycosylation represents the most abundant extracellular posttranslational modifi- Received: September 7, 2012 cation in multicellular organisms. These glycoproteins unequivocally comprise the major Revised: October 19, 2012 biomolecules involved in extracellular processes, such as growth factors, signaling proteins Accepted: November 6, 2012 for cellular communication, enzymes, and proteases for on- and off-site processing. It is now known that altered protein glycosylation is a hallmark event in many different pathologies. Glycoproteins are found mostly in the so-called secretome, which comprises classically and nonclassically secreted proteins and protein fragments that are released from the cell surface through ectodomain shedding. Due to biological complexity and technical difficulty, compara- bly few studies have taken an in-depth investigation of cellular secretomes using system-wide approaches. The cellular secretomes are considered to be a valuable source of therapeutic targets and novel biomarkers. It is not surprising that many existing biomarkers, including biomark- ers for breast, ovarian, prostate, and colorectal cancers are glycoproteins. Focused analysis of secreted glycoproteins could thus provide valuable information for ear