Detection and identification of plasma proteins that bind GlialCAM using ProteinChip arrays, SELDI-TOF MS, and nano-LC MS/MS

Proteomics
Linda Favre-KontulaBruno Antonsson

Abstract

In order to fully understand biological processes it is essential to identify interactions in protein complexes. There are several techniques available to study this type of interactions, such as yeast two-hybrid screens, affinity chromatography, and coimmunoprecipitation. We propose a novel strategy to identify protein-protein interactions, comprised of first detecting the interactions using ProteinChips and SELDI-TOF MS, followed by the isolation of the interacting proteins through affinity beads and RP-HPLC and finally identifying the proteins using nano-LC MS/MS. The advantages of this new strategy are that the primary high-throughput screening of samples can be performed with small amounts of sample, no specific antibody is needed and the proteins represented on the SELDI-TOF MS spectra can be identified with high confidence. Furthermore, the method is faster and less labor-intensive than other current approaches. Using this novel method, we isolated and identified the interactions of two mouse plasma proteins, mannose binding lectin C and properdin, with GlialCAM, a type 1 transmembrane glycoprotein that belongs to the Ig superfamily.

References

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Citations

Jun 1, 2011·Human Molecular Genetics·Tania López-HernándezRaúl Estévez
Mar 9, 2010·BMC Cancer·Yunfeng HeJie Lin
Feb 19, 2013·Expert Review of Proteomics·Mithilesh Kumar Jha, Kyoungho Suk
Aug 25, 2009·Best Practice & Research. Clinical Haematology·Jack M Lionberger, Derek L Stirewalt
Oct 11, 2008·Proteomics·Nicolas FavreChristian Pasquali
Sep 1, 2011·Mass Spectrometry Reviews·Peihong ZhuJohn G Marshall
Dec 30, 2009·Biotechnology Progress·Alex BerrillDaniel G Bracewell
Aug 11, 2012·PloS One·Tadeusz MajewskiBogdan Czerniak

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