Fine needle aspiration cytology in lupus lymphadenopathy. A case report.

This case report describes the aspiration cytologic characteristics of histologically proven acute lupus lymphadenitis. The aspirate contained numerous lymphoid cells and many amorphous, basophilic, hematoxylin-stained bodies dispersed in a granular, necrotic background that lacked polymorphonuclear leukocytes. The lymphadenopathy was diagnosed cytologically as necrotizing lymphadenitis and histologically as acute lupus lymphadenitis.     

Expression and characterization of recombinant human ciliary neurotrophic factor from Escherichia coli

The gene for ciliary neurotrophic factor (CNTF) was cloned from a human genomic DNA library by screening with a DNA fragment amplified from human genomic DNA using the polymerase chain reaction. A DNA sequence coding for human CNTF was placed under control of an regulatable promoter in the expression vector pJU1003 and transformed into Escherichia coli strain BL21(DE3). Induction of expression in cultures of this transformant led to the accumulation of approx. 25 mg/l per A600 unit of human CNTF. CNTF was purified to homogeneity from cell lysates via anion-exchange, cation-exchange and Zn(2+)-affinity chromatography. Purified CNTF contained less than 0.1% contaminating E. coli proteins, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), Western blot analysis and reversed-phase high-pressure liquid chromatography (HPLC). The protein exhibited an ultraviolet absorption maximum at 279 nm with a calculated extinction coefficient of A1%(279) = 9.0. Peptide map and amino acid sequence analyses confirmed that the expressed protein has the amino acid sequence expected for human CNTF, except for the absence of the amino-terminal methionine. High-purified recombinant human CNTF supported the survival of chick embryo parasympathetic, sympathetic and sensory neurons in culture at low picomolar concentrations. These results indicate that the biological activities previously ascribed to impure CNTF preparations indeed reside in one molecule.     

Obituary for Roland Schauer

Glycoconjugate Journal -     

Binding of antigen in the absence of histocompatibility proteins by arsonate-reactive T-cell clones

Inducer T-cell clones reactive to the p-azobenzenearsonate (arsonate) hapten possess binding sites for radioactive arsanylated proteins, which are not present on clones with other antigen specificities. Binding occurred in the absence of histocompatibility proteins. Binding was specific for the p-azobenzenearsonate hapten, since unconjugated proteins and proteins conjugated to the nonactivating o-azobenzenearsonate hapten neither bound to the clones nor competed binding of radioactive antigen. One of the clones was studied in more detail, using a panel of structural analogs of arsonate conjugated to the carrier protein ovalbumin. All conjugates that activated the clone in the presence of antigen-presenting cells also competed binding of radioactive antigen in the absence of antigen-presenting cells. Nonactivating conjugates did not compete binding. Based on evidence in this and the succeeding paper (Rao et al., accompanying paper), we suggest that these arsonate-binding sites may include the physiological antigen receptors of arsonate-reactive T-cell clones.     

Primary tuberculosis of the parotid gland

A very unusual presentation of Mycobacterium tuberculosis in the parotid gland substance is described to suggest reexamination of the place of tuberculosis in the differential diagnosis of a parotid mass. In this patient, diagnosis was made postoperatively only by histologic examination of the excised specimen. When M. tuberculosis etiology is suspected, either clinically or at operation, culture confirmation should be tried, and a Mantoux test should be performed to complete the investigation.