Expression of the Human Immunoglobulin Heavy Chain VH6 Gene Element by Fetal B Lymphocytes

Fetal B lymphocytes in mice and humans use a limited number of the available V_H gene segments. Mouse fetal B cells primarily utilize 3' V_H elements, suggesting that the localization of these elements determines their rearrangement frequency. The previously reported non-random usage of human V_H genes has been more difficult to explain. In this study the authors analysed the expression of the most proximal 3' human V_H element (V_H6) using a monoclonal antibody (JE-6). V_H6 expression was assessed in various B cell differentiation stages from fetal liver, bone marrow and spleen at 12–20 weeks of gestation. The authors demonstrate that the level of V_H6 expression does not exceed a stochastic usage frequency. This suggests that the localization of V_H6 does not significantly promote its expression during human fetal life, and that other factors must affect the usage of V_H genes during human fetal development.     

Sustained eosinophil cationic protein release into tears after a single high-dose conjunctival allergen challenge

Background The appearance of eosinophils is a hallmark sign of the allergic late-phase response (LPR). Eosinophil cationic protein (ECP), a readily measurable product released from activated eosinophils, has so far not been evaluated in the ocular LPR. Objective Two sets of trials were performed in order to investigate changes of local and systemic eosinophil activity and their possible link with symptoms and hyper-reactivity in the allergic LPR in the eye. Methods In the first experiment, ECP was analysed in tears and serum and the clinical reaction was evaluated during a 72-h time–course after a single, high-dose allergen challenge out of season in one eye of 15 pollen-sensitized volunteers. In a second experiment, the hypothesis of an increased clinical response to an allergen challenge in an eye that had been provoked with allergen 48h previously was tested in nine sensitized individuals. Results In the first experiment, symptoms at 10 min and 2, 4, 6, 8 and 24 h significantly exceeded base line scores of the challenged eyes. Tear ECP was significantly elevated in challenged eyes compared to contralateral eyes at 6, 8 and 24 h. In addition, symptoms and ECP release correlated significantly at the 24-h evaluation. Serum ECP remained unchanged throughout the study period. In the second experiment, conjunctival hyperreactivity 48h after an allergen challenge was not confirmed. Conclusion ECP secretion occurs in the experimental ocular LPR and is in part associated with the magnitude of the clinical reaction, which suggests a truly pathogenic role of the activated eosinophil in pollen-induced allergic conjunctivitis.     

CHARACTERIZATION OF RAT TESTICULAR ALCOHOL DEHYDROGENASE

A protein from rat testes that catalyzes the oxidation of ethanolin the presence of NAD⁺, but not NADP⁺, has been characterizedenzymatically and compared to that of hepatic alcohol dehydrogenaseobtained from the same animals. The testicular enzyme, likethe hepatic enzyme, has a K_m value for ethanol in the 0.5–1.0-mMrange and can utilize other alcohols such as n-propanol, n-butanol,and isobutanol, although the K_m values for these other alcoholsare considerably lower (0.03–0.08 mM) that that for ethanol.The testicular enzyme is more heat-labile than is the hepaticenzyme. Finally, the testicular enzyme catalyzes the oxidationof retinol and its retinol dehydrogenase activity is inhibitedby ethanol.     

Histology of port wine stains after copper vapour laser treatment

We report histological changes in four patients with port wine stains treated with 578 nm yellow light from a high power copper vapour laser. Histology showed that selective damage occurred to the ectatic blood-vessels in the dermis, without haemorrhage and damage to non-vascular structures, and without scarring. The initial damage to the overlying epidermis was not permanent, and the damaged ectatic vessels returned to normal size or were completely necrosed and replaced by collagen.