Next Article in Journal
Hepatitis C Virus-Infected Apoptotic Hepatocytes Program Macrophages and Hepatic Stellate Cells for Liver Inflammation and Fibrosis Development: Role of Ethanol as a Second Hit
Next Article in Special Issue
A Functional Analysis of the Cyclophilin Repertoire in the Protozoan Parasite Trypanosoma Cruzi
Previous Article in Journal
Ceramide Synthase 6: Comparative Analysis, Phylogeny and Evolution
Article Menu
Issue 4 (December) cover image

Export Article

Open AccessReview
Biomolecules 2018, 8(4), 112; https://doi.org/10.3390/biom8040112

The Multiple Roles of Peptidyl Prolyl Isomerases in Brain Cancer

Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC H3A2B4, Canada
Received: 21 September 2018 / Accepted: 9 October 2018 / Published: 11 October 2018
Full-Text   |   PDF [240 KB, uploaded 11 October 2018]

Abstract

Peptidyl prolyl isomerases (PPIases) are broadly expressed enzymes that accelerate the cis-trans isomerization of proline peptide bonds. The most extensively studied PPIase family member is protein interacting with never in mitosis A1 (PIN1), which isomerizes phosphorylated serine/threonine–proline bonds. By catalyzing this specific cis-trans isomerization, PIN1 can alter the structure of its target proteins and modulate their activities in a number of different ways. Many proteins are targets of proline-directed phosphorylation and thus PIN1-mediated isomerization of proline bonds represents an important step in the regulation of a variety of cellular mechanisms. Numerous other proteins in addition to PIN1 are endowed with PPIase activity. These include other members of the parvulin family to which PIN1 belongs, such as PIN4, as well as several cyclophilins and FK506-binding proteins. Unlike PIN1, however, these other PPIases do not isomerize phosphorylated serine/threonine–proline bonds and have different substrate specificities. PIN1 and other PPIases are overexpressed in many types of cancer and have been implicated in various oncogenic processes. This review will discuss studies providing evidence for multiple roles of PIN1 and other PPIases in glioblastoma and medulloblastoma, the most frequent adult and pediatric primary brain tumors. View Full-Text
Keywords: brain cancer; cancer stem-like cells; glioblastoma; medulloblastoma; nuclear factor-kappa B; PIN1; peptidyl prolyl isomerase brain cancer; cancer stem-like cells; glioblastoma; medulloblastoma; nuclear factor-kappa B; PIN1; peptidyl prolyl isomerase
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Stifani, S. The Multiple Roles of Peptidyl Prolyl Isomerases in Brain Cancer. Biomolecules 2018, 8, 112.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Biomolecules EISSN 2218-273X Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top