aled that Hsp110 was a major protein component of the extract and addition of purified recombinant Hsp110 to colon-derived cells recapitulated the effects of the luminal contents by inducing increased CD1d expression. The authors also report that Hsp110 is abundantly expressed in IECs, suggesting that Hsp110 may undergo regulated release from epithelia, where it would provide a signal for CD1d regulation.

In an accompanying commentary, Christopher Nicchitta from Duke University, North Carolina, discusses some potential sites of gut Hsp110 and mechanisms of Hsp110 release.

TITLE: Intestinal heat shock protein 110 regulates expression of CD1d on intestinal epithelial cells

AUTHOR CONTACT:
Richard S. Blumberg
Brigham And Woman's Hospital, Boston, Massachusetts, USA
Phone: 617-732-6912
Fax: 617-264-5185
Email: rblumberg@partners.org
View the PDF of this article at: https://www.the-jci.org/press/17241.pdf

ACCOMPANYING COMMENTARY:
Come forth CD1d: Hsp110 in the regulation of intestinal epithelial CD1d expression

AUTHOR CONTACT:
Chris Nicchitta
Duke University Medical Center, Durham, North Carolina, USA
Phone: 919-684-8948
Fax: 919-684-5481
E-mail: c.nicchitta@cellbio.duke.edu
View the PDF of this commentary at: https://www.the-jci.org/press/19614.pdf

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Chronic workplace condition reveals independent T cell group

The differentiation of naive T cells into memory T cells is a crucial step in the evolution of an immune response. Optimal activation requires 2 steps: (i) T cell receptor binding to the foreign antigen; and (ii) engagement of the CD28 molecule on th
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Contact: Brooke Grindlinger
science_editor@the-jci.org
212-342-9006
Journal of Clinical Investigation
2-Sep-2003

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