ISSN:
1573-675X
Schlagwort(e):
aminodipeptidase
;
caspase
;
quiescence
;
quiescent cell proline dipeptidase
;
proteasome
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
,
Medizin
Notizen:
Abstract We recently isolated and cloned an intracellular post-proline cleaving aminodipeptidase, quiescent cell proline dipeptidase (QPP), which has a substrate specificity very similar to that of dipeptidyl peptidase IV (CD26/DPPIV). Highly specific inhibitors of proline aminodipeptidases activate a novel apoptotic pathway in quiescent lymphocytes. The target of these inhibitors is not CD26/DPPIV, but appears to be QPP. The apoptosis pathway induced by the aminodipeptidase inhibitors is unusual in that it is restricted to quiescent lymphocytes, but not activated or transformed lymphocytes. The caspases activated in this apoptotic pathway are different from those activated in Fas or gamma-irradiation mediated cell death pathways, and furthermore, the proteasome appears to play a role in this death pathway. A large number of signal molecules including chemokines and cytokines have a highly conserved X-Pro motif on the N-terminus, rendering them potential substrates of QPP and players in the survival of resting lymphocytes.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1023/A:1009675223443
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