Research Article

Molecular Insights into the Breast and Prostate Cancer Cells in Response to the Change of Extracellular Zinc

Table 1

Identified proteins in breast cancer cells (MCF-7) and normal breast epithelial cells (MCF10A) with or without exogenous zinc exposure.

Spot IDIdentified proteinsGene IDProtein accessionTheoretical MW (kDa)/pIObserved MW (KDa)/pIPLGS scoreMatched peptidesSequence coverage (%)(Fold change/ value)Molecular functions
MCF-7 T0/MCF10A T0MCF-7 T120/MCF10A T120MCF-7 T120/MCF-7 T0MCF10A T120/MFC10A T0

114-3-3 protein σSFNP3194727.8/4.527.9/4.525862444(0.5/0.02) ↓I
214-3-3 protein θYWHAQP2734827.8/4.529.0/4.7108061443(0.4/0.003) ↓(0.3/0.0001) ↓II
326S proteasome non-ATPase regulatory subunit 4PSMD4Q5VWC441.1/4.562.0/4.610852223(0.2/0.003) ↓III
439S ribosomal protein L12 mitochondrialMRPL12P5281521.3/9.217.7/5.34066830(0.7/0.03) ↓IV
560S acidic ribosomal protein P0RPLP0A0A024RBS234.3/5.642.0/5.6588616(0.3/0.002) ↓V
6α-Smooth muscle actin 2ACTA2D2JYH442.0/5.144.4/5.268312228(6.8/0.0003) ↑(0.3/0.003) ↓VI
7Actin cytoplasmic 1ACTBP6070941.7/5.159.6/5.3178352760(0.3/0.0004) ↓VII
8Actinin α1 isoform CRA aACTN1A0A024R694103.0/5.1156.6/5.5352576445(1.9/0.02) ↑VIII
9AdenosylhomocysteinaseAHCYA0A384MTQ347.7/5.950.1/6.09112419(0.5/0.04) ↓III
10AnnexinANXA8L1A0A075B75240.7/5.635.2/5.6623817(0.1/0.04) ↓VIII
11Annexin A1ANXA1P0408338.7/6.636.0/6.6215632762(0.2/0.03) ↓VIII
12Annexin A5ANXA5P0875835.9/4.729.0/5.03292820(0.5/0.03) ↓(4.4/0.02) ↑VIII
13Calmodulin-1CALM1P0DP2317.0/3.913.9/3.31613641(0.2/0.006) ↓VIII, III
14Cathepsin DCTSDA0A1B0GW4443.7/6.130.2/5.419081119(8.4/0.0001) ↑(3.3/0.007) ↑III
15Cytochrome b5 type BCYB5BO4316916.3/4.718.2/3.7867317(4.2/0.0003) ↑VIII
16D-3-Phosphoglycerate dehydrogenasePHGDHA0A286YF2255.9/6.369.2/6.74302816(2.0/0.02) ↑(0.8/0.04) ↓(1.4/0.02) ↑III
17Dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex) isoform CRA aDLSTA0A024R6C948.7/9.362.0/6.01601410(2.6/0.01) ↑III
18Dynactin 2 (P50) isoform CRA cDCTN2A0A384MDU944.2/4.959.2/5.263202152(0.4/0.03) ↓(0.7/0.04) ↓VII
19Elongation factor 1 δEEF1DA0A087X1X769.2/6.842.0/4.3525312125(0.7/0.001) ↓V
20Elongation factor TuTUFMA0A384ME1749.8/7.450.1/7.026444936(5.2/0.01) ↑(0.5/0.003) ↓(0.5/0.01) ↓(1.4/0.02) ↑V
21Exosome complex component MTR3EXOSC6Q5RKV628.2/6.032.4/5.9350417(0.5/0.04) ↓IV
22F-Actin-capping protein subunit βCAPZBA0A384MR5030.6/5.628.5/5.718121026(3.0/0.0003) ↑(2.4/0.03) ↑VI
23ATP-dependent RNA helicase DDX1DDX1A0A087X2G173.9/7.6136.2/8.12981912(1.4/0.04) ↑III
24Adenylosuccinate lyaseADSLA0A1B0GTJ754.4/6.767.2/7.658448(0.3/0.002) ↓(0.4/0.005) ↓III
25FUBP1FUBP1A0A1Z1G4M267.6/7.989.5/8.237259(2.1/0.02) ↑II
26Peptidyl-prolyl cis-trans isomerase FKBP4FKBP4Q0279051.8/5.262.0/5.6328274765(1.9/0.01) ↑(2.5/0.003) ↑IX
27Glutathione S-transferase Mu 3GSTM3P2126626.5/5.226.9/5.484362054(3.0/0.04) ↑(5.0/0.005) ↑III
28Glutathione S-transferase PGSTP1P0921123.3/5.324.6/5.6127693166(0.2/0.002) ↓III
29Glutathione synthetaseGSSP4863752.4/5.662.0/5.6112692657(1.5/0.04) ↑III
30Inorganic pyrophosphatasePPA1Q1518132.6/5.437.8/5.5957411(2.5/0.03) ↑III
31Heat shock protein 90 kDa alpha (cytosolic) class B member 1 isoform CRA aHSP90AB1A0A024RD8083.2/4.8143.0/5.458342833(0.5/0.0006) ↓IX
32Heat shock protein β 1HSPB1P0479222.8/6.026.0/5.9466792278(3.5/0.002) ↑(0.2/0.002) ↓IX
33Pyruvate dehydrogenase E1 component subunit αPDHA1A0A024RBX943.3/8.050.1/6.537336(1.7/0.04) ↑III
34Heterogeneous nuclear ribonucleoproteins C1/C2HNRNPCB2R5W231.9/4.940.8/5.072922443(8.0/0.0002) ↑(0.5/0.009) ↓X, IV
35High mobility group protein B1HMGB1A0A024RDR024.9/5.523.5/6.33179826(1.9/0.03) ↑X
36Histidine-tRNA ligase cytoplasmicHARS1P1208157.4/5.662.0/5.832241525(1.5/0.04) ↑III
37Histone H4HIST1H4JB2R4R011.4/11.818.2/5.7897436(2.5/0.007) ↑(1.9/0.001) ↑VII, X
38Heat shock 70 kDa protein 1AHSPA1AA0A1U9X7W470.0/5.389.5/5.5295653849(1.7/0.02) ↑IX
39Inosine-5′-monophosphate dehydrogenaseIMPDHA0A384N6C255.8/6.569.2/7.03921814(0.6/0.04) ↓(1.5/0.005) ↑III
40L-Lactate dehydrogenase B chainLDHBP0719536.6/5.638.9/5.762821128(0.6/0.004) ↓III
41C-1-Tetrahydrofolate synthase, cytoplasmicMTHFD1A0A024R652101.5/6.8156.6/7.83421818(0.5/0.04) ↓XI, V
42Myosin regulatory light chain 12AMYL12AJ3QRS320.4/4.417.3/4.81142529(0.4/0.0003) ↓VIII
43NADH dehydrogenase (ubiquinone) iron-sulfur protein 3 mitochondrialNDUFS3O7548930.2/7.429.0/5.71561520(2.5/0.0004) ↑III
44Nucleoside diphosphate kinaseNMEA0A384MTW717.1/5.819.1/5.83957630(2.8/0.01) ↑(1.7/0.03) ↑III
45PerilipinPLINA0A140VJN846.9/5.155.1/5.137601132(0.1/0.005) ↓XII
46Plastin 3PLS3P1379770.8/5.392.2/5.644292031(1.8/0.04) ↑VIII
47Actin γACTG2P6326741.9/5.247.1/5.1111631130(5.2/0.001) ↑VII
48Proliferating cell nuclear antigenPCNAP1200428.8/4.436.0/4.734121344(1.5/0.004) ↑(0.6/0.02) ↓X
49Peroxiredoxin 6PRDX6A0A024R93825.0/6.026.0/6.325212634(1.9/0.04) ↑III
50Proteasome subunit β type 6PSMB6P2807225.3/4.621.4/4.91361521(1.4/0.04) ↑(0.3/0.03) ↓III
51Protein S100A2S100A2P2903411.0/4.512.0/4.52026318(0.04/0.004) ↓(0.08/0.01) ↓(0.4/0.02) ↓VIII
52Cytochrome c oxidase subunit 6B1COX6B1P1485410.2/6.912.4/5.9833828(1.9/0.02) ↑(0.7/0.04) ↓XII
53Protein S100A13S100A13Q9958411.5/5.813.1/5.790881760(4.1/0.001) ↑(4.0/0.0002) ↑VIII
54Protein SETSETQ0110533.5/4.050.1/4.488111634(0.2/0.0009) ↓(0.2/0.0001) ↓IX, X
55RadixinRDXB0YJ8868.5/6.0110.1/6.358282836(1.3/0.02) ↑(0.3/0.0004) ↓(1.6/0.004) ↑VI
56Rho GDP-dissociation inhibitor 1ARHGDIAP5256523.2/4.826.8/5.11996828(0.6/0.04) ↓III
5740S ribosomal protein SARPSAA0A024R2L632.8/4.647.1/5.12510816(4.4/0.0005) ↑VII
5860S acidic ribosomal protein P2RPLP2A0A024RCA711.7/4.215.9/4.384971177(0.7/0.004) ↓V
59Serine/threonine-protein kinase PAK 2PAK2Q1317758.0/5.673.4/5.822391728(0.5/0.03) ↓III
60Serpin B5SERPINB5A0A024R2B642.1/5.645.7/5.824661538(0.2/0.0007) ↓III
61START domain-containing 10 isoform CRA aSTARD10A0A024R5L833.0/6.739.8/6.01134520(3.1/0.002) ↑XIII
62StathminSTMN1P1694917.3/5.716.5/5.785241253(0.4/0.002) ↓VII
63SUMO-1 activating enzyme subunit 1 isoform CRA bSAE1A0A024R0R438.4/5.042.0/5.439301128(0.1/0.03) ↓III
64T-Complex protein 1 subunit αTCP1P1798760.3/5.775.5/5.845081730(0.4/0.008) ↓IX
65T-Complex protein 1 subunit γCCT3B3KX1157.9/6.589.5/6.110501723(0.8/0.02) ↓IX
66T-Complex protein 1 subunit θCCT8P5099059.6/5.373.4/5.612891528(0.2/0.03) ↓IX
67ThioredoxinTXNH9ZYJ211.7/4.614.5/5.113891534(1.4/0.0004) ↑III
68Torsin-1A-interacting protein 1TOR1AIP1A0A0A0MSK552.4/6.675.5/6.11086921(0.2/0.001) ↓(2.3/0.0005) ↑III
69Transitional endoplasmic reticulum ATPaseVCPP5507289.3/5.0132.3/5.425522728(0.6/0.01) ↓V, III
70Triosephosphate isomeraseTPI1P6017430.8/5.625.5/7.74224832(3.0/0.002) ↑(3.8/0.03) ↑III
71Tubulin alpha-1C chainTUBA1CQ9BQE350.1/4.814.8/5.31665412(0.2/0.0001) ↓(0.2/00) ↓(3.1/0.03) ↑VII
72Tumour protein D53TPD52L1E9PNK618.7/5.519.1/5.6160139(4.8/0.0005) ↑(13.6/0.001) ↑II
73Tumour protein D54TPD52L2A0A087WYR323.8/6.127.9/5.230421138(2.5/0.04) ↑II
74Vesicle amine transport protein 1VAT1A0A024R1Z641.9/5.957.5/6.054851221(0.7/0.04) ↓III

Note. MW stands for molecular weight, kDa for kilo Dalton, pI for isoelectric point, PLGS for ProteinLynx Global Server, T0 for 0 min or without zinc exposure (control), T120 for 120 min, ↑ for upregulation, ↓ for downregulation, MCF-7 for breast cancer cells, and MCF10A for breast normal epithelial cells. The PLGS score, protein accession, theoretical MW/pI, matched peptides, and sequence coverage (%) were obtained using ProteinLynx Global Server (PLGS) software (version 3.0, Waters Corporation, USA) and the UniProt (Homo sapiens, human) database. Gene ID was derived from UniProt database. The observed MW and pI were calculated according to the protein standards. The fold changes and values were acquired from the quantitative analysis of the gel images (each group n = 3) by Delta2D software (version 4.0.8, DECODON Gmbh, Germany). MCF-7 T0/MCF10A T0 is the expression fold change of the proteins in MCF-7 cells compared to MCF10A cells without zinc exposure (T0), MCF-7 T120/MCF10A T120 is the expression fold change of the proteins in MCF-7 cells compared to MCF10A cells following the zinc exposure for 120 min (T120), MCF-7 T120/MCF-7 T0 is the expression fold change of the proteins in MCF-7 cells following zinc exposure for T120 compared to T0, and MCF10A T120/MFC10A T0 is the fold change of the proteins in MCF10A cells following zinc exposure for T120 compared to T0. Molecular functions: I, apoptosis; II, signalling; III, catalytic activity; IV, RNA binding; V, protein synthesis; VI, protein binding; VII, structural; VIII, metal ion binding; IX, molecular chaperone; X, DNA binding; XI, DNA synthesis; XII, metabolism; XIII, lipid binding.