Senescence-Associated Changes in Proteome and O-GlcNAcylation Pattern in Human Peritoneal Mesothelial Cells

Table 1

Identified proteins showing significant differential abundance between young and senescent HPMC cells () with references of their predicted or reported O-GlcNAcylated sites.

Protein name	Gene name	SwissProt; entry name	MW; (kD)	pI	Length	Spot	Potential O-GlcNAc sites	S	T	Predicted O-GlcNAc sites	S	T	References
Actin, cytoplasmic 2	ACTG1	ACTG_HUMAN	41.8	5.31	375	294	51	25	26	9	8	1	[43]
Actin, cytoplasmic 1	ACTB	ACTB_HUMAN	41.7	5.29	375	294	51	25	26	9	8	1	[38, 40, 44]
Keratin, type II cytoskeletal 7	KRT7	K2C7_HUMAN	51.4	5.39	469	52	63	46	17	4	4	0	— [36–38, 44]
Cofilin-2	CFL2	COF2_HUMAN	18.7	7.88	166	198	20	12	8	4	4	0	[24]
Transgelin-2	TAGLN2	TAGL2_HUMAN	22.4	8.45	199	173	17	7	10	2	2	0	[41, 43]
60 kDa heat shock protein, mitochondrial	HSPD1	CH60_HUMAN	61.0	5.24	573	19	14	6	8	6	4	2	[37, 39, 41, 42, 44]
Heat shock cognate 71 kDa protein	HSPA8	HSP7C_HUMAN	70.9	5.37	646	16	82	35	47	4	2	2	[36–38, 41, 43–45]
Proteasome subunit beta type-2	PSMB2	PSB2_HUMAN	22.8	6.52	201	180	18	10	8	9	5	4	[41, 43]
Proteasome subunit beta type-3	PSMB3	PSB3_HUMAN	22.9	6.12	205	150	20	7	13	2	0	2	— [41, 43]
Nucleoside diphosphate kinase A	NME1	NDKA_HUMAN	17.1	5.82	152	198	11	6	5	3	2	1	[41]
5′(3′)-deoxyribonucleotidase, cytosolic type	NT5C	NT5C_HUMAN	23.4	6.18	201	150	14	6	8	1	0	1	—

Relative molecular mass of the protein as calculated from the amino acid sequence of the polypeptide without any co- or posttranslational modifications; calculated pI of the protein as obtained from SwissProt database; number of amino acids in the protein sequence; spots numbered according to Figure 2; potential O-GlcNAcylation sites expressed as the total number of serine (S) and threonine (T) residues in the protein sequence; predicted O-GlcNAcylation sites expressed as the number of predicted serine (S) and threonine (T) residues in the protein, obtained from dbOGAP database using default settings in OGlcNAcScan tool; references within protein candidates that have been reported to be O-GlcNAcylated. proteins from the same protein family of the candidate have been reported to be O-GlcNAcylated. [dbOGAP: http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html].