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Tripeptidyl-peptidase II: Update on an oldie that still counts
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
2019 (English)In: Biochimie, ISSN 0300-9084, E-ISSN 1638-6183, Vol. 166, p. 27-37Article, review/survey (Refereed) Published
Abstract [en]

The huge exopeptidase, tripeptidyl-peptidase II (TPP II), appears to be involved in a large number of important biological processes. It is present in the cytosol of most eukaryotic cells, where it removes tripeptides from free amino termini of longer peptides through a 'molecular ruler mechanism'. Its main role appears to be general protein degradation, together with the proteasome. The activity is increased by stress, such as during starvation and muscle wasting, and in tumour cells. Overexpression of TPP II leads to accelerated cell growth, genetic instability and resistance to apoptosis, whereas inhibition or down-regulation of TPP II renders cells sensitive to apoptosis. Although it seems that humans can survive without TPP II, it is not without consequences. Recently, patients with loss-of-function mutations in the TPP2 gene have been identified. They suffer from autoimmunity leading to leukopenia and other consequences. Furthermore, a missense mutation in the TPP2 gene is associated with a sterile brain inflammation condition mimicking multiple sclerosis. This review will summarise what is known today regarding the activity and structure of this very large enzyme complex, and its potential function in various cellular processes. It is clear that more research is needed to identify natural substrates and/or interaction partners of TPP II, which can explain the observed effects in different cellular contexts.

Place, publisher, year, edition, pages
2019. Vol. 166, p. 27-37
Keywords [en]
TPP II, Proteasome, Proteolysis, Aminopeptidase, Evans disease, TRIANGLE disease
National Category
Biochemistry and Molecular Biology Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-397070DOI: 10.1016/j.biochi.2019.05.012ISI: 000492314700004PubMedID: 31108122OAI: oai:DiVA.org:uu-397070DiVA, id: diva2:1371865
Available from: 2019-11-21 Created: 2019-11-21 Last updated: 2019-11-21Bibliographically approved

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