Role of CD26/dipeptidyl peptidase IV in human T cell activation and function

10.2741/2844 ◽  
2008 ◽  
Vol 13 (13) ◽  
pp. 2299 ◽  
Author(s):  
Kei Ohnuma
2002 ◽  
Vol 383 (7-8) ◽  
Author(s):  
D. Reinhold ◽  
T. Kähne ◽  
A. Steinbrecher ◽  
S. Wrenger ◽  
K. Neubert ◽  
...  

2005 ◽  
Vol 5 (5) ◽  
pp. 258-265 ◽  
Author(s):  
Dirk Reinhold ◽  
Thilo Kähne ◽  
Andreas Steinbrecher ◽  
Annegret Gerber ◽  
Vera Preller ◽  
...  

2020 ◽  
Vol 21 (17) ◽  
pp. 6118 ◽  
Author(s):  
Marianna Szczypka

Phosphodiesterase 7 (PDE7), a cAMP-specific PDE family, insensitive to rolipram, is present in many immune cells, including T lymphocytes. Two genes of PDE7 have been identified: PDE7A and PDE7B with three or four splice variants, respectively. Both PDE7A and PDE7B are expressed in T cells, and the predominant splice variant in these cells is PDE7A1. PDE7 is one of several PDE families that terminates biological functions of cAMP—a major regulating intracellular factor. However, the precise role of PDE7 in T cell activation and function is still ambiguous. Some authors reported its crucial role in T cell activation, while according to other studies PDE7 activity was not pivotal to T cells. Several studies showed that inhibition of PDE7 by its selective or dual PDE4/7 inhibitors suppresses T cell activity, and consequently T-mediated immune response. Taken together, it seems quite likely that simultaneous inhibition of PDE4 and PDE7 by dual PDE4/7 inhibitors or a combination of selective PDE4 and PDE7 remains the most interesting therapeutic target for the treatment of some immune-related disorders, such as autoimmune diseases, or selected respiratory diseases. An interesting direction of future studies could also be using a combination of selective PDE7 and PDE3 inhibitors.


Immunobiology ◽  
1995 ◽  
Vol 194 (4-5) ◽  
pp. 429-442 ◽  
Author(s):  
Sachiko Iwaki-Egawa ◽  
Yasuhiro Watanabe ◽  
Yukio Fujimoto

1998 ◽  
Vol 41 (12) ◽  
pp. 2100-2110 ◽  
Author(s):  
Coralie Nguyen ◽  
Julià Blanco ◽  
Jean-Paul Mazaleyrat ◽  
Bernard Krust ◽  
Christian Callebaut ◽  
...  

1997 ◽  
Vol 186 (11) ◽  
pp. 1865-1872 ◽  
Author(s):  
Tamas Oravecz ◽  
Marina Pall ◽  
Gregory Roderiquez ◽  
Mark D. Gorrell ◽  
Mary Ditto ◽  
...  

CD26 is a leukocyte activation marker that possesses dipeptidyl peptidase IV activity but whose natural substrates and immunological functions have not been clearly defined. Several chemo-kines, including RANTES (regulated on activation, normal T cell expressed and secreted), have now been shown to be substrates for recombinant soluble human CD26. The truncated RANTES(3–68) lacked the ability of native RANTES(1–68) to increase the cytosolic calcium concentration in human monocytes, but still induced this response in macrophages activated with macrophage colony-stimulating factor. Analysis of chemokine receptor messenger RNAs and patterns of desensitization of chemokine responses showed that the differential activity of the truncated molecule results from an altered receptor specificity. RANTES(3–68) showed a reduced activity, relative to that of RANTES(1–68), with cells expressing the recombinant CCR1 chemokine receptor, but retained the ability to stimulate CCR5 receptors and to inhibit the cytopathic effects of HIV-1. Our results indicate that CD26-mediated processing together with cell activation–induced changes in receptor expression provides an integrated mechanism for differential cell recruitment and for the regulation of target cell specificity of RANTES, and possibly other chemokines.


Author(s):  
Julia E. Rey Nores ◽  
Armand Bensussan ◽  
Natalio Vita ◽  
Felix Stelter ◽  
Mauricio A. Arias ◽  
...  

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