Estrogen-replacement therapy in younger women with breast cancer

Approximately 25% of breast cancers occur in premenopausal women. In addition to local therapy, surgery or surgery plus irradiation, systemic chemotherapy administration has become the standard of care for all node-positive and many node-negative patients. Systemic adjuvant chemotherapy can result in ovarian dysfunction or failure. This renders many women prematurely estrogen deficient. The consequences of menopause, genitourinary atrophy, bone loss, and increased risk of cardiovascular disease, have not been routinely assessed in clinical trials. The risks of estrogen deficiency have not been assessed in comparison to improved disease-free and overall survival benefits of adjuvantly treated premenopausal breast cancer patients. Estrogen-replacement therapy in postmenopausal women has been shown to prevent osteoporosis and reduce fracture risk. The majority of studies also show a marked reduction in cardiovascular disease and mortality. Estrogen-replacement therapy has been considered a disease-prevention strategy rather than a therapeutic intervention. The risks and benefits of estrogen-replacement therapy in women with primary breast cancer are unknown. It is unknown how the well-known benefits accrued from reduction in skeletal and cardiovascular morbidity/mortality compare with the potential risks of increased breast cancer morbidity/mortality. Carefully designed prospective clinical trials with well-defined objectives and endpoints are required to learn if more harm than good is done by the withholding of estrogen therapy in breast cancer patients.     

The impact of hypothermia on dilutional coagulopathy

The control of hemorrhage in hypothermic patients with platelet and clotting factor depletion is often impossible. Determining the cause of coagulopathic bleeding (CB) will enable physicians to appropriately focus on rewarming, clotting factor repletion, or both. Objective: To determine the contribution of hypothermia in producing CB and ascertain if simultaneous hypothermia and dilutional coagulopathy (DC) interact synergistically. Method: Prothrombin time, partial thromboplastin time, and platelet function were determined at assay temperatures of 29 degrees to 37 degrees C on normal and critically ill, noncoagulopathic (NC) individuals. Dilutional coagulopathy was created using buffered saline and the assays repeated. Results: Hypothermic assay at < or = 35 degrees C significantly prolonged coagulation times. The effect of hypothermia on NC and DC samples was not different. Conclusion: Assays performed at 37 degrees C underestimate coagulopathy in hypothermic patients. The effect of hypothermia on NC and DC is not different, indicating the lack of a synergistic effect. Normalization of clotting requires both rewarming and clotting factor repletion.     

Laser additive processing of functionally-graded Fe–Si–B–Cu–Nb soft magnetic materials

Laser additive manufacturing is a novel tool for processing compositionally-graded alloys that are challenging to process via a conventional route. This article discusses a novel combinatorial approach for assessing composition–microstructure–magnetic property relationships, using laser deposited compositionally-graded Fe–Si–B–Nb–Cu alloys (by changing the silicon to boron ratios). The microstructure of Fe–Si–B–Nb–Cu alloys with a lower Si to B ratio consists of dendritic α-Fe₃Si grains, with B and Nb partitioning to the inter-dendritic regions, resulting in the formation of Fe₃B grains. As the Si/B ratio increases, the (Fe, Nb) enriched eutectic phase was observed along with α-Fe₃Si grains; and no Fe₃B was observed. These microstructural changes with varying Si/B ratios significantly affect the magnetic properties of these laser-deposited soft magnetic alloys.     

Etiology of bloody diarrhea in Bolivian children: implications for empiric therapy. Bolivian Dysentery Study Group

In Bolivia, few data are available to guide empiric therapy for bloody diarrhea. A study was conducted between December 1994 and April 1995 to identify organisms causing bloody diarrhea in Bolivian children. Rectal swabs from children <5 years old with bloody diarrhea were examined for Salmonella, Shigella, and Campylobacter organisms; fecal specimens were examined for Entamoeba histolytica. A bacterial pathogen was identified in specimens from 55 patients (41%). Shigella organisms were found in 39 specimens (29%); 37 isolates (95%) were resistant to ampicillin, 35 (90%) to trimethoprim-sulfamethoxazole, and 24 (62%) to chloramphenicol, but all were susceptible to nalidixic acid. Only 1 of 133 stool specimens contained E. histolytica trophozoites. Multidrug-resistant Shigella species are a frequent cause of bloody diarrhea in Bolivian children; E. histolytica is uncommon. Clinical predictors described in this study may help identify patients most likely to have Shigella infection. Laboratory surveillance is essential to monitor antimicrobial resistance and guide empiric treatment.     

Incisional hernia after laparoscopic nephrectomy with intact specimen removal: caveat emptor

The choline-containing phosphoglycolipid, MfGL-II, is the major polar lipid of Mycoplasma fermentans PG18. Anti-MfGL-II antisera raised in rabbits using the purified MfGL-II as an immunogen were employed in immunogold electron microscopic and immunofluorescence studies showing that MfGL-II is uniformly distributed and exposed on the cell surface of M. fermentans cells. The specificity of the antibodies was determined by immunostaining of lipid extracts separated by thin layer chromatography. The antibodies recognize lipids specific to M. fermentans but did not cross-react with lipid extracts of M. penetrans, M. capricolum, M. gallisepticum or Acholeplasma laidlawii. As phosphocholine almost completely abolished antibody interaction with MfGL-II in an ELISA assay it is suggested that the anti-MfGL-II repertoire is composed primarily of anti-phosphocholine antibodies. The anti-MfGL-II antisera inhibit the attachment of M. fermentans to Molt-3 lymphocytes suggesting that MfGL-II plays a major role in M. fermentans-host cell interaction.