scholarly journals High CD30 Ligand Expression by Epithelial Cells and Hassal's Corpuscles in the Medulla of Human Thymus

Blood ◽  
1998 ◽  
Vol 91 (9) ◽  
pp. 3323-3332 ◽  
Author(s):  
Paola Romagnani ◽  
Francesco Annunziato ◽  
Roberto Manetti ◽  
Carmelo Mavilia ◽  
Laura Lasagni ◽  
...  

Abstract CD30 is a member of tumor necrosis factor (TNF) receptor superfamily that is expressed by activated T cells in the presence of interleukin-4 (IL-4). Although CD30 can mediate a variety of signals, CD30-deficient mice have impaired negative selection of T cells, suggesting that at least in the context of murine thymus, CD30 is a cell death–mediating molecule. The ligand for CD30 (CD30L) is a membrane-associated glycoprotein related to TNF, which is known to be expressed mainly by activated T cells and other leukocytes. However, the nature of CD30L-expressing cells involved in the interaction with CD30+ thymocytes is unclear. We report here that in postnatal human thymus the great majority of CD30+ cells are double positive (CD4+CD8+), activated, IL-4 receptor–expressing T cells which selectively localize in the medullary areas. Moreover, many medullary epithelial cells and Hassal's corpuscles in the same thymus specimens showed unusually high expression of CD30L in comparison with other lymphoid or nonlymphoid tissues. These findings provide additional information on the nature and localization of CD30+ thymocytes and show that epithelial cells are the major holder of CD30L in the thymic medulla.

Blood ◽  
1998 ◽  
Vol 91 (9) ◽  
pp. 3323-3332 ◽  
Author(s):  
Paola Romagnani ◽  
Francesco Annunziato ◽  
Roberto Manetti ◽  
Carmelo Mavilia ◽  
Laura Lasagni ◽  
...  

CD30 is a member of tumor necrosis factor (TNF) receptor superfamily that is expressed by activated T cells in the presence of interleukin-4 (IL-4). Although CD30 can mediate a variety of signals, CD30-deficient mice have impaired negative selection of T cells, suggesting that at least in the context of murine thymus, CD30 is a cell death–mediating molecule. The ligand for CD30 (CD30L) is a membrane-associated glycoprotein related to TNF, which is known to be expressed mainly by activated T cells and other leukocytes. However, the nature of CD30L-expressing cells involved in the interaction with CD30+ thymocytes is unclear. We report here that in postnatal human thymus the great majority of CD30+ cells are double positive (CD4+CD8+), activated, IL-4 receptor–expressing T cells which selectively localize in the medullary areas. Moreover, many medullary epithelial cells and Hassal's corpuscles in the same thymus specimens showed unusually high expression of CD30L in comparison with other lymphoid or nonlymphoid tissues. These findings provide additional information on the nature and localization of CD30+ thymocytes and show that epithelial cells are the major holder of CD30L in the thymic medulla.


PLoS ONE ◽  
2018 ◽  
Vol 13 (10) ◽  
pp. e0205685 ◽  
Author(s):  
Douglas A. Carlow ◽  
Michelle C. Tra ◽  
Hermann J. Ziltener
Keyword(s):  
T Cells ◽  

2007 ◽  
Vol 56 (10) ◽  
pp. 3459-3467 ◽  
Author(s):  
Yann Parel ◽  
Michel Aurrand-Lions ◽  
Agneta Scheja ◽  
Jean-Michel Dayer ◽  
Eddy Roosnek ◽  
...  

Cytokine ◽  
1994 ◽  
Vol 6 (3) ◽  
pp. 279-284 ◽  
Author(s):  
Thomas Lehrnbecher ◽  
Martin Poot ◽  
Karin Orscheschek ◽  
Walter Sebald ◽  
Alfred C. Feller ◽  
...  

1993 ◽  
Vol 13 (8) ◽  
pp. 4793-4805 ◽  
Author(s):  
S J Szabo ◽  
J S Gold ◽  
T L Murphy ◽  
K M Murphy

Activity of the murine interleukin-4 (IL-4) promoter was localized to several cis-acting elements present within the first 300 bp from the transcriptional initiation site. Five repeated elements, P0 to P4, that share the common consensus ATTTTCCNNT were located between -40 and -250, and each was shown to interact with the T-cell-specific factor NF(P). These distinct P sites appear functionally interchangeable and cooperatively confer cyclosporin A-sensitive and ionomycin-inducible promoter activity. NF(P) may be closely related to the cytoplasmic component of NF-AT (nuclear factor of activated T cells), a T-cell-specific factor essential for IL-2 gene transcription, as judged from indistinguishable molecular weights and protease fragmentation patterns of UV-photolabeled factors. Also, we identified an element in the IL-4 promoter with homology to the Y box common to all major histocompatibility complex class II gene promoters. Our data show that the IL-4 promoter Y box -114CTGATTGG-107 significantly enhances overall promoter activity, since point mutations within this element diminish promoter activity by 85%. The factor binding this region is indistinguishable from the cloned nuclear factor NF-Y, as judged from interactions with specific anti-NF-Y monoclonal and polyclonal antibodies. Last, we point out the presence of two sites that share sequence identity to the OAP region of the ARRE-1 site within the IL-2 promoter (K. S. Ullman, W. M. Flanagan, C. A. Edwards, and G. R. Crabtree, Science 254:558-562, 1991). These regions, -85GTGTAATA-78 and -245GTGTAATT-238, reside adjacent to the NF(P) binding sites P1 and P4 and bind a distinct nuclear factor.


2006 ◽  
Vol 175 (1) ◽  
pp. 87-97 ◽  
Author(s):  
Mara Fornaro ◽  
Peter M. Burch ◽  
Wentian Yang ◽  
Lei Zhang ◽  
Claire E. Hamilton ◽  
...  

The formation of multinucleated myofibers is essential for the growth of skeletal muscle. The nuclear factor of activated T cells (NFAT) promotes skeletal muscle growth. How NFAT responds to changes in extracellular cues to regulate skeletal muscle growth remains to be fully defined. In this study, we demonstrate that mice containing a skeletal muscle–specific deletion of the tyrosine phosphatase SHP-2 (muscle creatine kinase [MCK]–SHP-2 null) exhibited a reduction in both myofiber size and type I slow myofiber number. We found that interleukin-4, an NFAT-regulated cytokine known to stimulate myofiber growth, was reduced in its expression in skeletal muscles of MCK–SHP-2–null mice. When SHP-2 was deleted during the differentiation of primary myoblasts, NFAT transcriptional activity and myotube multinucleation were impaired. Finally, SHP-2 coupled myotube multinucleation to an integrin-dependent pathway and activated NFAT by stimulating c-Src. Thus, SHP-2 transduces extracellular matrix stimuli to intracellular signaling pathways to promote skeletal muscle growth.


1993 ◽  
Vol 23 (12) ◽  
pp. 3120-3125 ◽  
Author(s):  
Mark de Boer ◽  
Ahmad Kasran ◽  
Jaap Kwekkeboom ◽  
Hugo Walter ◽  
Peter Vandenberghe ◽  
...  

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