Occurrence of a multimeric high-molecular-weight glyceraldehyde-3-phosphate dehydrogenase in human serum

Journal of Proteome Research
Rani KunjithapathamShanmugasundaram Ganapathy-Kanniappan

Abstract

Cellular glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a phylogenetically conserved, ubiquitous enzyme that plays an indispensable role in energy metabolism. Although a wealth of information is available on cellular GAPDH, there is a clear paucity of data on its extracellular counterpart (i.e., the secreted or extracellular GAPDH). Here, we show that the extracellular GAPDH in human serum is a multimeric, high-molecular-weight, yet glycolytically active enzyme. The high-molecular-weight multimers of serum GAPDH were identified by immunodetection on one- and two-dimensional gel electrophoresis using multiple antibodies specific for various epitopes of GAPDH. Partial purification of serum GAPDH by DEAE Affigel affinity/ion exchange chromatography further established the multimeric composition of serum GAPDH. In vitro data demonstrated that human cell lines secrete a multimeric, high-molecular-weight enzyme similar to that of serum GAPDH. Furthermore, LC-MS/MS analysis of extracellular GAPDH from human cell lines confirmed the presence of unique peptides of GAPDH in the high-molecular-weight subunits. Furthermore, data from pulse-chase experiments established the presence of high-molecular-weight subunits in the secreted, ex...Continue Reading

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Citations

Feb 6, 2018·Journal of Cellular and Molecular Medicine·Priya GajendiranShanmugasundaram Ganapathy-Kanniappan
Feb 1, 2019·Current Protocols in Protein Science·Shanmugasundaram Ganapathy-Kanniappan
Dec 4, 2019·Brain : a Journal of Neurology·Nicole J Van BergenJohn Christodoulou
Sep 15, 2017·Biophysics Reviews·César L AvilaRosana Chehín
Apr 18, 2021·BMC Molecular and Cell Biology·Carina Jägers, Henk Roelink
Nov 12, 2021·Frontiers in Physiology·Himanshi PanditaShanmugasundaram Ganapathy-Kanniappan

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