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Physiological and Pathogenic Roles of Prolyl Isomerase Pin1 in Metabolic Regulations via Multiple Signal Transduction Pathway Modulations
- Source :
- International Journal of Molecular Sciences, Vol 17, Iss 9, p 1495 (2016), International Journal of Molecular Sciences
- Publication Year :
- 2016
- Publisher :
- MDPI AG, 2016.
-
Abstract
- Prolyl isomerases are divided into three groups, the FKBP family, Cyclophilin and the Parvulin family (Pin1 and Par14). Among these isomerases, Pin1 is a unique prolyl isomerase binding to the motif including pSer/pThr-Pro that is phosphorylated by kinases. Once bound, Pin1 modulates the enzymatic activity, protein stability or subcellular localization of target proteins by changing the cis- and trans-formations of proline. Several studies have examined the roles of Pin1 in the pathogenesis of cancers and Alzheimer's disease. On the other hand, recent studies have newly demonstrated Pin1 to be involved in regulating glucose and lipid metabolism. Interestingly, while Pin1 expression is markedly increased by high-fat diet feeding, Pin1 KO mice are resistant to diet-induced obesity, non-alcoholic steatohepatitis and diabetic vascular dysfunction. These phenomena result from the binding of Pin1 to several key factors regulating metabolic functions, which include insulin receptor substrate-1, AMPK, Crtc2 and NF-κB p65. In this review, we focus on recent advances in elucidating the physiological roles of Pin1 as well as the pathogenesis of disorders involving this isomerase, from the viewpoint of the relationships between signal transductions and metabolic functions.
- Subjects :
- 0301 basic medicine
glucose metabolism
Parvulin
Review
Isomerase
Biology
Models, Biological
Catalysis
lcsh:Chemistry
Inorganic Chemistry
Mice
03 medical and health sciences
Pin1
Metabolic Diseases
lipid metabolism
Prolyl isomerase
Animals
Humans
vascular inflammation
Physical and Theoretical Chemistry
NIMA-Interacting Peptidylprolyl Isomerase
lcsh:QH301-705.5
Molecular Biology
Spectroscopy
Cyclophilin
bone formation
Organic Chemistry
General Medicine
Computer Science Applications
Glucose
030104 developmental biology
FKBP
lcsh:Biology (General)
lcsh:QD1-999
Biochemistry
Cardiovascular Diseases
PIN1
Signal transduction
Signal Transduction
Subjects
Details
- ISSN :
- 14220067
- Volume :
- 17
- Database :
- OpenAIRE
- Journal :
- International Journal of Molecular Sciences
- Accession number :
- edsair.doi.dedup.....876489db5805793e35ec281f7ad76385