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

Table 2

Identified proteins in prostate cancer cells (PC3) and normal prostate epithelial cells (RWPE-1) with or without exogenous zinc exposure.

Spot ID

Identified proteins

Gene ID

Protein accession

Theoretical MW (kDa)/pI

Observed MW (kDa)/pI

PLGS score

Matched peptides

Sequence coverage (%)

(Fold change/ value)

Molecular functions

PC3 T0/RWPE-1 T0

PC3 T120/RWPE-1 T120

PC3 T120/PC3 T0

RWPE-1 T120/RWPE-1 T0

75

14-3-3 protein σ

SFN

P31947

27.8/4.5

27.3/3.8

932

3

6

(0.4/0.001) ↓

I

76

14-3-3 protein θ

YWHAQ

P27348

27.8/4.5

27.3/4.7

15878

15

40

(0.4/0.003) ↓

(1.5/0.0009) ↑

II

77

40S ribosomal protein S18

RPS18

P62269

17.7/11.4

17.5/5.7

2004

6

38

(0.5/0.03) ↓

(0.3/0.02) ↓

III, IV

78

Transaldolase

TALDO1

A0A140VK56

37.5/6.4

39.1/5.6

423

11

18

(1.7/0.01) ↑

V

79

60S acidic ribosomal protein P0

RPLP1

A0A024RBS2

34.3/5.6

42.3/4.1

208

3

7

(1.4/0.01) ↑

(1.5/0.006) ↑

VI

80

Adenosylhomocysteinase

AHCY

A0A384MTQ3

47.7/5.9

50.9/5.9

657

20

22

(0.5/0.005) ↓

V

81

Aldehyde dehydrogenase 1 family member A3 isoform CRA a

ALDH1A3

A0A024RC95

56.1/7

74.4/7.7

3883

39

30

(1.5/0.02) ↑

V

82

Annexin A1

ANXA1

P04083

38.7/6.6

42.6/6.6

24829

27

55

(0.2/0.02) ↓

(0.3/0.04) ↓

VII

83

Annexin A5

ANXA5

P08758

35.9/4.7

33.4/5.1

12361

20

50

(0.2/0.0008) ↓

(0.3/0.004) ↓

VII

84

26S proteasome non-ATPase regulatory subunit 11

PSMD11

O00231

47.4/6.1

53.9/6.7

1037

18

34

(4.0/0.0009) ↑

(0.3/0.004) ↓

V

85

ATP synthase subunit α mitochondrial

ATP5F1A

P25705

59.7/9.4

56.3/7.8

26896

25

45

(0.4/0.008) ↓

(0.6/0.04) ↓

III, V

86

Calreticulin

CALR

P27797

48.1/4.1

81.3/4.4

9707

32

70

(1.7/0.007) ↑

VIII

87

Chaperonin containing TCP1 subunit 6A (ζ 1) isoform CRA a

CCT6A

A0A024RDL1

58/6.2

78.0/6.2

1700

21

33

(0.7/0.02) ↓

(0.6/0.003) ↓

VIII

88

Clathrin light chain A

CLTA

P09496

27/4.2

35.4/4.2

1196

8

14

(1.8/0.02) ↑

IV

89

Cytochrome c oxidase subunit 5A mitochondrial

COX5A

H3BRM5

7.8/5.7

14.2/5.0

1969

4

35

(0.6/0.01) ↓

(0.5/0.03) ↓

VII

90

ATP-dependent RNA helicase DDX39A

DDX39A

O00148

49.1/5.3

62.9/5.6

3285

8

14

(0.6/0.004) ↓

V

91

RNA helicase

DDX48

A0A024R8W0

46.8/6.3

58.3/6.2

4579

49

38

(0.5/0.02) ↓

(2.9/0.006) ↑

V

92

Dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex) isoform CRA a

DLST

A0A024R6C9

48.7/9.3

62.9/5.8

2675

12

18

(0.2/0.0003) ↓

(0.6/0.03) ↓

V

93

Dihydropyrimidinase-related protein 2

DPYSL2

A0A1C7CYX9

73.5/5.9

81.9/6.0

3385

19

29

(0.3/0.001) ↓

V

94

Dopamine receptor interacting protein 4

DRIP4

Q4W4Y1

96.0/6.1

158.9/6.1

5782

44

38

(0.3/0.004) ↓

II

95

S-Adenosylmethionine synthase

MAT2A

B4DEX8

39.7/5.6

52.2/6.1

1183

16

27

(1.3/0.03) ↑

V

96

Elongation factor 1 δ

EEF1D

A0A087X1X7

69.2/6.8

40.1/5.0

26412

18

23

(1.6/0.03) ↑

(1.4/0.04) ↑

(1.2/0.03) ↑

VI

97

Elongation factor 1 γ

EEF1G

P26641

50.1/6.2

54.3/6.0

2159

10

18

(0.4/0.004) ↓

VI

98

Elongation factor Tu

TUFM

A0A384ME17

49.8/7.4

50.5/6.7

2726

51

33

(5.1/0.0004) ↑

VI

99

Ethanolamine-phosphate cytidylyltransferase

PCYT2

I3L1R7

41.4/7.0

54.3/7.2

803

9

23

(0.1/0.008) ↓

IX

100

Eukaryotic translation initiation factor 3 subunit E

EIF3E

B2R806

52.2/5.6

57.9/5.7

1850

11

21

(2.0/0.002) ↑

VI

101

Eukaryotic translation initiation factor 3 subunit I

EIF3I

Q13347

36.5/5.3

40.1/5.6

1091

6

17

(3.4/0.0003) ↑

VI

102

Exosome complex component MTR3

EXOSC6

Q5RKV6

28.2/6.0

29.5/5.9

795

13

19

(0.3/0.001) ↓

(0.6/0.01) ↓

III

103

F-Actin-capping protein subunit β

CAPZB

A0A384MR50

30.6/5.6

30.1/5.7

3939

12

27

(0.6/0.006) ↓

X

104

Glucose-6-phosphate 1-dehydrogenase

G6PD

A0A384NL00

59.2/6.4

71.2/7.1

8928

24

38

(5.5/0.01) ↑

IX

105

Glutamate dehydrogenase

GLUD1

B4DMF5

56.6/6.8

65.4/7.5

4823

19

37

(0.6/0.009) ↓

IX

106

Glutathione S-transferase P

GSTP1

P09211

23.3/5.3

24.6/5.6

21246

47

67

(0.3/0.006) ↓

(0.4/0.0002) ↓

V

107

Histone H4

HIST1H4J

B2R4R0

11.4/11.8

34.9/9.2

3206

8

62

(0.3/0.02) ↓

(1.5/0.03) ↑

IV

108

Glycine tRNA ligase

GARS1

A0A090N8G0

77.5/5.8

116.0/5.9

5889

112

41

(0.3/0.00001) ↓

V

109

60 kDa heat shock protein, mitochondrial

HSPD1

A0A024R3W0

61.0/5.6

70.7/5.6

16269

32

48

(1.5/0.02) ↑

(1.9/0.0005) ↑

(2.9/0.01) ↑

VIII

110

Heat shock 70 kDa protein 1B

HSPA1B

A0A0G2JIW1

70.1/5.3

90.2/5.6

10234

35

40

(1.5/0.02) ↑

(0.5/0.004) ↓

VIII

111

Heat shock protein 90 kDa alpha (cytosolic) class B member 1 isoform CRA a

HSP90AB1

A0A024RD80

83.2/4.8

123.6/5.3

10935

37

41

(1.8/0.002) ↑

VIII

112

Heat shock protein β 1

HSPB1

P04792

22.8/6.0

27.1/5.4

5134

9

42

(2.1/0.02) ↑

(2.2/0.02) ↑

VIII

113

Aspartate aminotransferase

GOT1

A0A140VK69

46.2/6.6

46.4/7.5

682

20

24

(0.40/0.004) ↓

V

114

Histidine tRNA ligase, cytoplasmic

HARS1

B4DDD8

48.5/5.0

58.3/5.6

548

5

11

(0.6/0.03) ↓

V

115

Copine 1

CPNE1

B0QZ18

59.7/5.6

90.2/5.6

11670

27

26

(1.8/0.004) ↑

V

116

Latexin

LXN

Q9BS40

25.7/5.4

29.8/5.6

1946

19

23

(0.8/0.02) ↓

II

117

Leukotriene A (4) hydrolase

LTA4H

A0A140VK27

69.2/5.7

90.9/5.8

2315

27

24

(0.2/0.01) ↓

VII

118

L-Lactate dehydrogenase B chain

LDHB

A0A5F9ZHM4

37.4/5.8

34.6/5.6

2746

8

23

(2.0/0.01) ↑

(2.2/0.0003) ↑

(0.7/0.03) ↓

V

119

L-Lactate dehydrogenase

LDHA

A0A3B3IS95

30.7/6.1

45.0/5.7

3821

14

25

(1.9/0.02) ↑

V

120

MAD1 mitotic arrest deficient-like 1

MAD1L1

A4D218

91.7/8.1

134.2/4.8

738

23

26

(0.5/0.04) ↓

II

121

Moesin

MSN

P26038

67.8/6.0

102.0/6.1

3846

26

32

(0.7/0.004) ↓

(1.6/0.002) ↑

VIII

122

Myosin light polypeptide 6

MYL6

B7Z6Z4

26.7/4.8

14.1/4.7

5045

6

24

(0.3/0.006) ↓

VII

123

Protein NDRG1

NDRG1

A0A024R9I3

39.5/6.1

53.9/5.6

8387

11

27

(1.8/0.03) ↑

II

124

NSFL1 cofactor p47

NSFL1C

Q9UNZ2

40.6/4.8

47.4/5.2

11230

29

65

(5.0/0.0003) ↑

(2.4/0.004) ↑

VIII

125

Peroxiredoxin 6

PRDX6

A0A024R938

25.0/6.0

25.3/6.2

4671

45

52

(8.4/0.0007) ↑

(2.8/0.02) ↑

(0.2/0.03) ↓

V

126

Peroxiredoxin 2

PRDX2

P32119

21.9/5.6

20.9/5.6

4964

13

40

(2.4/0.0003) ↑

V

127

Plastin 3

PLS3

P13797

69.3/5.5

86.1/5.6

1149

12

17

(0.6/0.01) ↓

VII

128

Prohibitin

PHB

A8K401

29.8/5.4

26.6/5.6

3671

17

55

(2.5/0.0001) ↑

XI

129

Prostaglandin E synthase 3

PTGES3

A0A087WYT3

19.1/4.2

19.8/4.1

339

11

14

(2.1/0.03) ↑

VIII

130

Proteasome (prosome macropain) activator subunit 3 (PA28 γ ki) isoform CRA a

PSME3

A0A024R203

30.9/6.3

31.7/5.7

3923

12

36

(1.7/0.04) ↑

I

131

Proteasome subunit α type 1

PSMA1

P25786

29.5/6.2

29.8/6.8

3657

10

35

(9.5/0.0005) ↑

III

132

Protein DDI1 homolog 2

DDI2

Q5TDH0

44.5/4.8

56.3/5.1

320

4

12

(0.2/0.007) ↓

V

133

Protein disulfide-isomerase

P4HB

A0A024R8S5

57.1/4.6

67.7/4.9

21868

53

66

(1.4/0.03) ↑

V

134

Protein kinase C substrate 80K-H isoform CRA a (glucosidase 2 subunit beta)

PRKCSH

A0A024R7F1

59.3/4.1

133.2/4.5

2052

10

18

(2.1/0.01) ↑

V, VII

135

Protein S100A6

S100A6

P06703

10.2/5.2

12.1/5.3

3080

6

33

(1.6/0.039) ↑

VII

136

Protein SET

SET

Q01105

33.5/4.0

50.9/4.4

4249

14

33

(0.2/0.0002) ↓

(0.4/0.0001) ↓

(1.7/0.02) ↑

(0.7/0.004) ↑

VIII, XII

137

Rho GDP-dissociation inhibitor 1

ARHGDIA

P52565

23.2/4.8

25.5/5.1

4058

13

43

(0.6/0.006) ↓

V

138

40S ribosomal protein SA

RPSA

A0A024R2L6

32.8/4.6

52.2/5.0

8860

69

27

(0.5/0.0003) ↓

(1.5/0.006) ↑

IV

139

Serpin B5

SERPINB5

A0A024R2B6

42.1/4.9

42.6/5.7

14963

33

63

(0.3/0.002) ↓

(0.4/0.006) ↓

V

140

Staphylococcal nuclease domain-containing protein

SND1

A0A140VK49

101.9/6.8

158.9/7.6

4962

70

48

(0.3/0.00009) ↓

V

141

Stathmin

STMN1

P16949

17.3/5.7

18.0/5.4

2472

9

45

(5.1/0.03) ↑

IV

142

Succinate dehydrogenase (ubiquinone) flavoprotein subunit mitochondrial

SDHA

A0A024QZ30

72.7/7.0

90.9/6.2

2908

15

20

(0.6/0.03) ↓

V

143

Superoxide dismutase (Cu-Zn)

SOD1

P00441

15.9/6.7

17.4/5.7

6360

3

18

(2.3/0.004) ↑

VIII

144

T-Complex protein 1 subunit α

TCP1

P17987

60.3/5.7

74.4/5.8

4205

14

22

(0.6/0.025) ↓

(0.4/0.05) ↓

(4.6/0.02) ↑

VIII

145

Eukaryotic translation initiation factor 3 subunit F

EIF3F

B3KSH1

39.1/5.1

54.3/5.1

10070

7

25

(1.4/0.005) ↑

II

146

Torsin-1A-interacting protein 1

TOR1AIP1

A0A0A0MSK5

52.4/6.6

71.2/6.1

1483

14

33

(0.2/0.003) ↓

V

147

Tropomyosin 3 isoform 2

TPM3

A0A0S2Z4G8

28.7/4.5

32.4/4.9

12626

25

63

(1.5/0.002) ↑

X

148

Tubulin α 1A chain

TUBA1A

Q71U36

50.1/4.8

68.2/5.1

74078

20

49

(0.5/0.002) ↓

(0.6/0.007) ↓

(1.3/0.02) ↑

IV

149

Ubiquitin carboxyl-terminal hydrolase

USP14

A6NJA2

51.1/5.6

78.0/5.6

2543

4

8

(0.5/0.03) ↓

(0.5/0.003) ↓

(3.0/0.004) ↑

V

150

Zyxin

ZYX

Q15942

61.2/6.2

116.0/6.2

768

7

16

(0.6/0.02) ↓

VII

151

Acetyltransferase component of pyruvate dehydrogenase complex

DLAT

B4DJX1

62.7/5.4

101.2/5.6

1844

24

17

(1.6/0.01) ↑

V

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, PC3 for prostate cancer cells, and RWPE-1 for prostate 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). PC3 T₀/RWPE-1 T₀ is the expression fold change of the proteins in PC3 cells compared to RWPE-1 cells without zinc exposure (T₀), PC3 T₁₂₀/RWPE-1 T₁₂₀ is the expression fold change of the proteins in PC3 cells compared to RWPE-1 cells following the zinc exposure for 120 min (T₁₂₀), PC3 T₁₂₀/PC3 T₀ is the expression fold change of the proteins in PC3 cells following zinc exposure for T₁₂₀ compared to T₀, and RWPE-1 T₁₂₀/RWPE-1 T₀ is the expression fold change of the proteins in RWPE-1 cells following zinc exposure for T₁₂₀ compared to T₀. Molecular functions: I, apoptosis; II, signalling; III, RNA binding; IV, structural; V, catalytic activity; VI, protein synthesis; VII, metal ion binding; VIII, molecular chaperone; IX, metabolism; X, protein binding; XI, transcription; XII, DNA binding.