Clinico-pathologic manifestations of Iranian patients with breast cancer

Breast cancer is the most common malignancy in women and is the second cause of cancer death in female population. The objective was to find out different clinical manifestations and epidemiology of breast cancer among various ethnics groups to help improve health system in the country. In this retrospective cross sectional study, we evaluated clinical and pathologic features of one thousand Iranian women with breast cancer. The data including age, type of surgery, pathology report, tumor size, lymph node involvement, tumor stage and receptor status were extracted from medical records and were analyzed. The highest prevalence of breast cancer was in patients in 40-49 years age group [37.4%]. The most common performed surgery was modified radical mastectomy and the most common pathology report was intra-ductal carcinoma. Tumor size was 2-5 cm in most of patients. Sixty percent of patients had lymph node involvement. Finally, 49.1% of patients were diagnosed when they were in stage II and 36.7% were in stage III. In 72.9% of patients, estrogen receptor, progesterone receptor or both receptors were positive and of 116 patients who were checked for Her-2, 27 patients [23.2%] were 3+ positive. Our findings suggest that Iranian breast cancer patients are relatively younger than patients in western countries and mostly present at higher pathologic stages. We highly recommend screening test to be performed at lower ages [at least 40 years old]

Stereochemical aspects of interaction of DNA binding domain of human progesterone receptor with d(AGGTCATGCT)2.

Structures of (i) 66 amino-acid fragment (residues 567-633) from DNA binding domain of human progesterone receptor (hPR), (ii) a ten base pair DNA sequence d(AGGTCATGCT)2 from hormone responsive element (HRE) and (iii) a complex of these two are optimised by computer modelling and molecular mechanics technique using extensive steric constraints from secondary structure predictions, comparison with the structures of known metalloproteins, geometric constraints imposed by tetrahedral coordination with the zinc ion and comparison with structures of DNA binding domains of human glucocorticoid and estrogen receptors (hGR and hER). Structure of the complex was obtained using genetic modification data on steroid receptors and general consensus about protein-DNA interaction. DNA is in distorted B conformation. Sequence dependent as well as protein-induced conformation changes are noticed. There is change in propeller twist, buckle and angle between glycosyl bonds. However, H-bonding network is preserved. The complex is stabilized with eighteen hydrogen-bonds, mainly between peptide side-chains and backbone phosphate. There are five specific H-bonds between basic amino acid side chains, Lys 22, Lys 26 and Arg 27, and DNA bases, A1, G3, G16 and A17. Gly 19, Ser 20 and Val 23 are in close proximity of DNA.