Affinity purification of a high molecular weight human breast cancer-associated antigen identified by the BCD-B4 monoclonal antibody

This study reports the purification and characterization of a high molecular weight human breast cancer-associated antigen identified by a previously described (1,2) murine monoclonal antibody, BCD-B4. Immunohistochemical analysis indicated that BCD-B4 recognizes an antigen expressed in an altered form on the human breast carcinoma cell line, BT-20, compared to the non-malignant human mammary epithelial cell line, HBL-100. Chemical treatments and enzymatic digestions suggested that the recognized moiety was a protein. The antigenic determinant was resistant to neuraminidase and periodate treatments but was sensitive to trypsin and proteinase K. The antigen was purified by affinity chromatography and its molecular weight, determined by SDS-PAGE analysis under non-reducing conditions, was proven to be 250 Kd. Under reducing conditions, the molecule dissociated into two polypeptides of 125 and 45 Kd, respectively. Both subunits could be isolated from normal HBL-100 and neoplastic BT-20 cellular protein extracts by affinity chromatography. The higher molecular weight subunit showed; however, qualitative and quantitative differences between the two cell lines: it was expressed in greater quantity on BT-20 cells and its molecular weight was 15 Kd higher. Both subunits could also be identified by immunoblots of BT-20 cells.     

Curriculum for musculoskeletal radiology.

Although general suggestions have been made regarding a radiology residency curriculum, no specific list of entities has been offered. Over the past ten years, we have developed a resident-run morning conference in musculoskeletal radiology that is supervised by faculty and covers a specific curriculum. We offer our curriculum as an example that may assist other departments in developing their own curricula.     

In situ hybridization analysis for herpes simplex virus nucleic acids in Alzheimer disease

Histological sections of brain from patients showing evidence of advanced pathology of Alzheimer disease (AD) were examined for the presence of herpes simplex type-1 (HSV-1) nucleic acids by a sensitive in-situ hybridization technique. Samples from neurologically normal patients were examined in parallel. Sensitivity of the assay was verified by the detection of HSV-1 nucleic acids in neurons of trigeminal ganglia taken from cases of AD and normal controls. This indicated that the hybridization reaction was sufficiently sensitive to detect latent HSV-1 infections. Positive hybridization in the brain was only detected in a confirmed case of herpes simplex virus encephalitis. These results appear to confirm previous reports that HSV-1 infection is not directly involved in the pathology associated with AD.