Disease relevance of Tpp2

• Tripeptidyl-peptidase II expression and activity are increased in skeletal muscle during sepsis [1].

High impact information on Tpp2

• These indicated C-terminal carboxypeptidase, endopeptidase as well as N-terminal tripeptidyl-aminopeptidase activities in endosomes [2].
• Purification, substrate specificity, and classification of tripeptidyl peptidase II [3].
• The cholecystokinin-8 (CCK-8)-inactivating peptidase is a serine peptidase that has been shown to be a membrane-bound isoform of tripeptidyl peptidase II (EC 3.4.14.10) [4].
• Hence, whereas a fraction of tripeptidyl peptidase II-like immunoreactivity localization at the cellular level is consistent with its alleged function in cholecystokinin octapeptide inactivation, its association with the outside plasma membrane of neurons remains to be confirmed [5].
• Tripeptidyl peptidase II-like immunoreactivity was also detected at the ultrastructural level in the cerebral cortex and hypothalamus using either immunoperoxidase or silver-enhanced immunogold detection [5].

Chemical compound and disease context of Tpp2

• This result was blunted by the glucocorticoid receptor antagonist RU 38486, indicating that glucocorticoids participate in the upregulation of TPP II in skeletal muscle during sepsis [1].

Biological context of Tpp2

• Sepsis resulted in increased activity and protein and gene expression of TPP II in extensor digitorum longus muscles [1].

Anatomical context of Tpp2

• The second situation corresponds to cholecystokinin neuronal populations containing tripeptidyl peptidase II-like immunoreactivity, as in neurons of the supraoptic or paraventricular nuclei, axons in the median eminence or nigral neurons [5].
• Tripeptidyl peptidase II-like immunoreactivity was mostly detected in neurons, and also in ependymal cells and choroid plexuses, localizations consistent with a possible participation of the peptidase in the inactivation of cholecystokinin circulating in the cerebrospinal fluid [5].
• The third situation corresponds to areas with mismatches, such as the cerebellum, a region devoid of cholecystokinin, but in which Purkinje cells displayed high tripeptidyl peptidase II-like immunoreactivity, possibly related to a role in the inactivation of neuropeptides other than cholecystokinin [5].
• Distribution of tripeptidyl-peptidase II in the central nervous system of rat [6].

Associations of Tpp2 with chemical compounds

• Since it had previously been demonstrated that the enzyme can inactivate enkephalins and dynorphins in vitro by removing the N-terminal Tyr-Gly-Gly peptide, we wanted to see whether TPP II could be involved in this process also in vivo [6].

Analytical, diagnostic and therapeutic context of Tpp2

• TPP II protein and gene expression were determined by Western blot and real-time PCR, respectively [1].

References