Protein signatures of molecular pathways in non-small cell lung carcinoma (NSCLC): comparison of glycoproteomics and global proteomics

Table 2 Experimental design of tissues from human lung

List	ID	Age	Sex	Pathology	iTRAQ	iTRAQ group	Set	Position	Type	Dimension (mm)	Size of tumor
1	HC	68	M	HC		115	1
2	SqCC.N1	80	M	N	114	116	1	LUL	SqCC	6.5	pT2b
3	SqCC.C1			C		117	1
4	SqCC.N2	82	M	N	114	115	2	UL	SqCC	3	pT1b
5	SqCC.C2			C		116	2
6	SqCC.N2	74	M	N	114	117	2	RUL	SqCC	4.7	pT2a
7	SqCC.C3			C		115	3
8	ADC.N1	79	F	N		116	3	RUL	ADC	1.6	pT1
9	ADC.C1			C		117	3
10	ADC.N2	74	F	N	114	115	4	RUL	ADC	3	pT1b
11	ADC.C2			C		116	4
12	ADC.N3	65	M	N		117	4	RLL	ADC	3.3	pT2a
13	ADC.C3			C		115	5
14	ADC.N4	71	M	N	114	116	5	RLL	ADC	5.2	pT2b
15	ADC.C4			C		117	5
16	ADC.C5			C		116	6
17	ADC.N5	61	F	N	114	115	6	RLL	ADC	4.5	pT3
18	ADC.C6			C		117	6

Proteins from six benign tissue sections (N = normal) were pooled and labeled by iTRAQ channel 114. Proteins from 18 specimens including benign, health control and tumor tissues were labeled by 4-plex iTRAQ reagents (115, 116, and 117). The labeled proteins were pooled to six sets of iTRAQ groups. Proteins or glycoproteins were quantified by the relative intensity of 115, 116, 117 versus that of 114 in each group. Change of protein expression was estimated by iTRAQ quantitation. RUL right upper lung, RLL right left lung, HC health control, N normal (or benign), C cancer, SqCC squamous cell carcinoma, ADC adenocarcinoma. The HC was used as one of the controls for the determination of fold-change of proteins in cancer tissues

ISSN: 1559-0275