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Volume 3 Issue 6, June 2002

Paneth cells (stained reddish with phloxine-tartrazine) of the intestinal crypts discharge their antimicrobial-rich granules into the lumen of the small intestine. Bevins and colleagues (page 583) finally identified the human enzyme that cleaves and activates HD5, a major defensin released by Paneth cells, as trypsin. Magnification: ∼1000×.

Volume 3 Issue 6

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Commentary

  • In memoriam: César Milstein, who with the late Georges Köhler invented monoclonal antibodies, died on 24 March 2002. Their invention sprang from basic research on antibody diversity and specificity, and spawned revolutionary advances in biology, medicine and industry.

    • Timothy A. Springer
    Commentary
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News & Views

  • Some strains of mice fail to mount an efficient NK cell response to MCMV infection. With the use of deletion mutants, the in vivo basis for MCMV resistance to killing by NK cells is revealed.

    • Klas Kärre
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  • Although cytokines and STATs are accepted as being integral to TH1 differentiation, T-bet had emerged as a possible master control switch. Fresh data forces a reexamination of the factors that control TH cell development.

    • John J. O'Shea
    • William E. Paul
    News & Views

  • The α-defensins from Paneth cells in intestinal crypts need processing to be fully functional. Unlike for mice, the cleaving enzyme for human HD5 turns out to be trypsin.

    • Michael Zasloff
    News & Views

  • Classical opsonins are serum proteins that coat microorganisms and particles so as to enhance uptake by macrophages. A recent Nature paper has identified a macrophage-derived opsonin for apoptotic cells.

    • R Alan Ezekowitz
    News & Views
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