Altered Expression of the Cell Cycle Regulatory Molecules pRb, p53 and MDM2 Exert a Synergetic Effect on Tumor Growth and Chromosomal Instability in Non-small Cell Lung Carcinomas (NSCLCs)

Gorgoulis, V. G.; Zacharatos, P.; Kotsinas, A.; Mariatos, G.; Liloglou, T.; Vogiatzi, T.; Foukas, P.; Rassidakis, G.; Garinis, G.; Ioannides, T.; Zoumpourlis, V.; Bramis, J.; Michail, P. O.; Asimacopoulos, P. J.; Field, J. K.; Kittas, Ch.

doi:10.1007/BF03402115

Molecular Medicine

Table 6 Correlations between p53 mutations and ploidy status of the carcinomas*

From: Altered Expression of the Cell Cycle Regulatory Molecules pRb, p53 and MDM2 Exert a Synergetic Effect on Tumor Growth and Chromosomal Instability in Non-small Cell Lung Carcinomas (NSCLCs)

Sample	Defective Exon	Gene Mutation	Amino Acid Substitution	Amino Acid Group¹ (99)		Position of the substituted amino acid located at: (98,99)		Class² (98)	Ploidy
				Normal Amino Acid	Substitute Amino Acid	Secondary Structure of the wt p53 Molecule	Favorable Secondary Structure
4	7	codon 249, AGG → AGT	R → S	IV	III	loop	loop	II	A
5	7	codon 244, GCC → TGC	G → C	III	III	loop	helix	II	A
6	5	codon 151, CCC → CAC	P → H	I	IV	loop	helix	II	A
7	8	codon 273, CGT → CTT	R → L	IV	I	sheet	helix	I	A
8	7	codon 248, CGG → TGG	R → W	IV	I	loop	sheet	I	D
9	7	codon 238, TGT → TIT	C → F	III	I	sheet	sheet	II	D
10	4	codon 93, CTG → ATG	L → M	I	I	helix	helix	II	A
11	8	codon 280, AGA → ATA	R → I	IV	I	helix	sheet	I	A
12	7	codon 234, TAC → TGC	Y → C	III	III	sheet	helix	II	A
13	7	codon 248, CGG → CTG	R → L	IV	I	loop	helix	I	D
14	7	codon 239, AAC → ACC	N → Τ	III	III	loop	sheet	II	A
15	5	codon 163, TAC → TGC	Y → c	III	III	sheet	helix	II	A
18	7	codon 230, ACC → AAC	T → Ν	III	III	sheet	loop	II	D
24	4	codon 74, GCC → ACC	A → Τ	I	III	helix	sheet	II	NI
26	6	codon 196, CGA → CCA	R → Ρ	IV	I	sheet	loop	II	A
27	8	codon 282, CGG → GG	FS	−	−	−	−	truncation	NI
28	5	codon 157, GTC → TTC	V → F	I	I	sheet	sheet	II	A
29	4	codon 69, GCT → GGT	A → G	I	III	helix	loop	II	A
32	5	codon 163, TAC → TGC	Y → C	III	III	sheet	helix	II	A
41	4	codon 110, CGT → C_T	FS	−	−	−	−	truncation	A
42	5	codon 157, GTC → TTC	V → F	I	I	sheet	sheet	II	A
43	4	codon 60, CCA → CCT	P → P	I	I	loop	loop	−	A
44	6	codon 213, CGA → _GA	FS	−	−	−	−	truncation	A
48	7	codon 237, ATG → ATA	M → I	I	I	sheet	sheet	II	D
52	8	codon 273, CGT → CAT	R → H	IV	IV	sheet	helix	I	A
53	9	codon 319, AAG → AAT	Κ → N	IV	III	helix	loop	II	A
55	8	codon 275, TGT → TTT	C → F	III	I	loop	sheet	II	A
57	5	codon 153, CCC → CAC	P → H	I	IV	loop	helix	II	A
59	5	codon 143, GTG − GCC	V → A	I	I	sheet	helix	II	A
62	8	codon 270, TTT → ATT	F → F	I	I	sheet	sheet	−	A
70	7	codon 233, CAC → TAC	H → Y	IV	III	sheet	sheet	II	D

¹I: non-polar, II: negatively charged, III: uncharged, IV: positively charged; ²I: site-specific DNA binding domain, II: conformational; IHC: Immunohistochemistry; SSCP: Single Strand Conformational Polymorphism analysis; wt: wild type: D, Diploid; A: Aneuploid; NI: Non informative.
*Gualberto et al. (32) demonstrated an association between class of p53 mutations and ploidy status. Our data indicate that, apart from the class of p53 mutations, other factors like amino acid family (98), secondary structure in which the substitute residue participates and interactions among the amino acids of the DNA binding domain with the residues of the p53 scaffold structure, may determine the overall structure and, thus, the function of the mutant p53 protein (97).

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ISSN: 1528-3658

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