Table 2: Classification of the differentially expressed proteins revealed in the knee synovial tissues among the normal and vehicle-treated and QFGJS-treated CIA rats.

ClassificationSubclassificationName of proteinsFunctionsSpot no.

BindingAntigen bindingIgG-2a Ig gamma-2A chain C regionNucleotide sequence and antibody effector functions1
Cytoskeletal protein bindingAnxa2 isoform short of Annexin A2Calcium-regulated membrane-binding protein13
Protein bindingDes desminClass-III intermediate filaments10
Ogn osteoglycinInduces bone formation in conjunction with TGF-beta-1 or TGF-beta-221
Actb actin, cytoplasmic 1Involved in various types of cell motility23
Serum albuminRegulation of the colloidal osmotic pressure of blood24

Metabolic process Metabolic processGsto1 glutathione S-transferase omega-1Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities29
Gstp1 glutathione S-transferase PConjugation of reduced glutathione to hydrophobic electrophiles3
Pgam1 phosphoglycerate mutase 1Catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase)12
Tpi1 triosephosphate isomeraseBelongs to the triosephosphate isomerase family8
Lipid metabolic processApoe apolipoprotein EMediates the binding, internalization, and catabolism of lipoprotein particles30
Lipoprotein metabolic processApolipoprotein C-III, isoform CRA_bInhibits lipoprotein and hepatic lipase and decreases the uptake of lymph chylomicrons4
One-carbon metabolic processCa 3 carbonic anhydrase 3Involved in the metabolism of xenobiotics and of natural substrates6
Oxidation reductionAldh2 proteinAldehyde dehydrogenase (NAD) activity, identical protein binding 31
Aldh6a1 methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrialPlays a role in valine and pyrimidine metabolism5
Gpx1 glutathione peroxidase 1Protects the hemoglobin in erythrocytes14
Ivd isovaleryl-CoA dehydrogenase, mitochondrialIt is Oxidoreductase15
Idh3a isocitrate dehydrogenase [NAD] subunit alpha, mitochondrialIt is Oxidoreductase18
Ldhb L-lactate dehydrogenase B chainIdentical protein, NAD or NADH binding, and L-lactate dehydrogenase activity22
Mdh1 malate dehydrogenase, cytoplasmicOxidoreductase, NAD or NADH binding, and L-malate dehydrogenase activity28
RGD1565368 similar to glyceraldehyde-3-phosphate dehydrogenaseCatalytic activity19
Nucleobase, nucleoside, nucleotide, and nucleic acid metabolic processNp purine nucleoside phosphorylaseTransferase, glycosyltransferase, purine-nucleoside phosphorylase activity26
GlycolysisRGD1560402 similar to phosphoglycerate kinase 1 (Pgk1)Phosphoglycerate kinase activity11

Regulation of biological processActin filament cappingCapzb F-actin-capping protein subunit betaBlocking the exchange of subunits17
Capza2 F-actin-capping protein subunit alpha-2Blocking the exchange of subunits27
Signal transductionAnxa1 Annexin A1Promotes membrane fusion and is involved in exocytosis32

Cellular processProtein transportSelenbp1 Selenium-binding protein 1Involved in the sensing of reactive xenobiotics20
Intermediate filament-based processVim vimentinPlays a role in the stability of the cytoplasmic architecture2
Transmembrane transportVdac2 Voltage-dependent anion-selective channel protein 2Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules7

OtherCatalytic activityCes3 carboxylesterase 3Involved in the metabolism of xenobiotics and of natural substrates9
Acute inflammatory responseCrp C-reactive proteinDisplays several functions associated with host defense16
Cellular componentS100a4 protein S100-A4Interacts with PPFIBP1 in a calcium-dependent mode25

Spot no. denotes the number shown in the first column of Table 1.
The differentially expressed protein spots observed among the normal rats, CIA rats, and QFGJS-treated CIA rats are classified into five classes. 6 proteins are related to binding, 17 proteins are related to metabolic process, 3 proteins are related to biological process, and 3 proteins are related to cellular process and 3 proteins belongs to other class.