Abnormal Proteins in Primary Breast Cancer Tissues from 25 Sudanese Patients

This study was designed to compare antigen content of normal with cancerous breast tissues from Sudanese patients. Fifty tissue samples (normal and cancerous) from 25 Sudanese patients with primary breast cancer were analyzed for their protein content using 2D PAGE, and for protein identification using LC/MS and nr.fasta data base search. Four proteins were found in the cancerous tissues which were absent from the normal tissues of the same patients: thioredoxin mutant D60n, Chain A, X-ray crystal structure of human galectin −1, rcTPM3 and a truncated isoform-2 of beta tropomyosin spots. The thioredoxin mutant is a protein with 105 amino acids and is characterized by the fact that Asp 60 is replaced by Asn. The Chain A, X-ray crystal structure of human galectin-1 is a synthetic mutated protein with 134 amino acids, cysteine 16 is replaced by unknown amino acid (X). The rcTPM3 is a fragment of tropomyosin-3 with 247 amino acids. The truncated beta tropomyosin is isoform 2 with 257 amino acids. Primary breast cancer tissues from Sudanese patients are characterized by abnormal proteins which are undetectable in the normal tissues. These proteins can be used, as a target for drug therapy, for diagnosis and in vaccination trials