Profiling of the cell surface proteome.
The in depth-mining of the proteome necessitates the comprehensive analysis of proteins in individual subcellular compartments to uncover interesting patterns of protein expression that include assessment of protein location, trafficking and of post-translational modifications that are location specific. One of the compartments of substantial interest from a diagnostic and therapeutic point of view is the plasma membrane which contains intrinsic membrane proteins and other proteins expressed on the cell surface. Technologies are currently available for the comprehensive profiling of the cell surface proteome that rely on protein tagging of intact cells. Studies are emerging that point to unexpected patterns of expression of specific proteins on the cell surface, with a common occurrence of proteins previously considered to occur predominantly in other compartments, notably the endoplasmic reticulum. The profiling of the cell surface and plasma membrane proteomes will likely provide novel insights and uncover disease related alterations.
Jang
Jun Ho
JH
University of Michigan, Department of Pediatrics, Ann Arbor, MI 48109, USA.
Hanash
Samir
S
D036541:ADP-ribosyl Cyclase / Q000032:analysis; D051997:ADP-ribosyl Cyclase 1; D015703:Antigens, CD / Q000032:analysis; D001360:Avidin / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D019921:Biotinylation; D018821:CD18 Antigens / Q000032:analysis; D002352:Carrier Proteins / Q000032:analysis; D002374:Catalase / Q000032:analysis; D045744:Cell Line, Tumor; D002846:Chromatography, Affinity; D015180:Electrophoresis, Gel, Two-Dimensional; D000091342:Endoplasmic Reticulum Chaperone BiP; D018922:HL-60 Cells; D015235:HLA-B Antigens / Q000032:analysis; D018840:HSP70 Heat-Shock Proteins / Q000032:analysis; D006360:Heat-Shock Proteins / Q000032:analysis; D006735:Horseradish Peroxidase / Q000737:chemistry; D006801:Humans; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000032:analysis* / Q000302:isolation & purification; D018832:Molecular Chaperones / Q000032:analysis; D011145:Polyvinyls / Q000737:chemistry; D011485:Protein Binding; D019704:Protein Disulfide-Isomerases / Q000032:analysis; D020543:Proteome / Q000032:analysis*; D040901:Proteomics / Q000379:methods*; D011990:Receptors, Transferrin / Q000032:analysis; D016622:Silver Staining; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D020298:U937 Cells; D005465:Fluorocarbon Polymers
D036541:ADP-ribosyl Cyclase; D051997:ADP-ribosyl Cyclase 1; D015703:Antigens, CD; D001360:Avidin; D001426:Bacterial Proteins; D018821:CD18 Antigens; D002352:Carrier Proteins; D002374:Catalase; D000091342:Endoplasmic Reticulum Chaperone BiP; D015235:HLA-B Antigens; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D006735:Horseradish Peroxidase; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D018832:Molecular Chaperones; D011145:Polyvinyls; D019704:Protein Disulfide-Isomerases; D020543:Proteome; D011990:Receptors, Transferrin; C041533:HLA-B58 antigen; C058865:Strep-avidin conjugated horseradish peroxidase; C018551:glucose-regulated proteins; C024865:polyvinylidene fluoride; D005465:Fluorocarbon Polymers; C498154:CD38 protein, human