PubMed · 7360821
A method of correction of inverted nipples is presented, which appears to be simple, safe, and effective, leaving little scarring.
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J M Hamilton. 1980. Inverted nipples.. https://doi.org/10.1097/00006534-198004000-00021
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Review of research protocols involving positron emission tomography studies on healthy volunteers focused attention on the radiation exposure disclosure statements contained in the informed consent form. Of particular concern was the observation that breast doses from positron emission tomography studies are greater than breast doses from other research uses of radioisotopes, as well as routine nuclear medicine and radiographic procedures. Disclosure of individual organ doses is not normally provided on informed consent forms. A worksheet was developed to aid research investigators in the determination of effective dose equivalents and organ dose equivalents from all sources of radiation to which a volunteer is exposed. Three standardized risk statements are discussed. The final selection and use of these statements are determined by worksheet calculations of effective dose equivalents and organ dose equivalents.
P68 is a potent inhibitor of protein synthesis in virally infected cells and has been suggested to function in noninfected cells as a tumor suppressor gene. We have previously demonstrated that p68 expression correlates directly with cellular differentiation and inversely with proliferative activity in normal epithelium and in several human tumor systems. In order to determine the role of p68 in human breast cancer, we utilized immunohistochemistry and mapped the expression of p68 in tissue from 200 breast biopsy specimens. A total of 434 foci, ranging from normal breast tissue to infiltrating carcinoma were examined. We found that p68 was present at basal levels in normal lobular and luminal ductal epithelial cells, with higher levels present in myoepithelial cells. Nonproliferative fibrocystic lesions showed variable expression of p68, with high levels seen within foci of apocrine metaplasia and low levels in cystically dilated terminal duct units. Low levels of p68 were seen in typical ductal proliferations, lobular neoplasia (atypical lobular hyperplasia and lobular carcinoma in situ), and in fibroadenomas. Foci of atypical ductal hyperplasia in situ and invasive ductal carcinoma generally showed higher levels of p68 expression. Among the infiltrating carcinomas, p68 expression correlated with nuclear grade. This suggests that the ability of p68 to inhibit cellular proliferation may be impaired in breast cancer and that its expression, although modestly paralleling cellular differentiation, is not a predictive indicator of improved survival.
In this study we examine the relationship between p21CIP1/Waf1 (CIP1), a 21 kDa protein that binds to and modulates the activity of several cyclin dependent kinases and expression of wild-type (WT) p53 in human breast epithelial cells. Basal CIP1 protein, but not CIP1 mRNA levels correlated well with expression of WT p53 in human breast epithelial cells. To obtain more direct evidence that WT p53 regulated the level of CIP1 protein, the Human Papilloma Virus (HPV) E6 protein was introduced into immortalized 184B5 breast cells. Residual WT p53 levels correlated well with CIP1 protein but not CIP1 mRNA levels in isolated clones of transfected cells. CIP1 protein was increased at early times after growth factor arrested cells were stimulated to proliferate. The rise in CIP1 protein was due to a concomitant increase in CIP1 mRNA levels in MCF10, but not in normal mammary epithelial cells. DNA damage induced by ionizing radiation resulted in a transient increase in WT p53 levels but a prolonged induction of CIP1 protein. The sustained increase in CIP1 protein 24 h after radiation could not be attributed to a concomitant increase in CIP1 mRNA levels. Although the half-life of the CIP1 protein was not altered following irradiation, a fourfold increase in the amount of radioactivity incorporated into CIP1 protein was detected. When considered together these data suggest that wild-type p53 affects CIP1 protein accumulation at a posttranscriptional level in human breast epithelial cells under different physiologic and stress conditions.