Evolutionary relationships of the prolyl oligopeptidase family enzymes

Venäläinen, Jarkko I.; Juvonen, Risto O.; Männistö, Pekka T.

doi:10.1111/j.1432-1033.2004.04199.x

Cited by 86 publications

(82 citation statements)

References 33 publications

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“…central glucose sensing | sympathetic nervous system | peripheral hormonal regulation P rolyl endopeptidase (PREP; EC 3.4.21.26) is a highly conserved enzyme (1). In humans and rodents it is highly expressed in the brain (2), including the cortex, striatum, hypothalamus, hippocampus, and amygdala (3)(4)(5)(6).…”

Section: Hypothalamic Prolyl Endopeptidase (Prep) Regulates Pancreatimentioning

confidence: 99%

Hypothalamic prolyl endopeptidase (PREP) regulates pancreatic insulin and glucagon secretion in mice

Kim¹,

Toda²,

D’Agostino³

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Fig. 1. Bone cells express Avprs. Immunofluorescence micrographs (A) and Western immunoblotting (B)show the expression of Avpr1α in osteoblasts and osteoclasts, and as a function of osteoblast (mineralization) and osteoclast (with Rankl) differentiation. The expression of Avp (ligand) and Avpr1α (receptor) in osteoblasts is regulated by 17β-estradiol, as determined by quantitative PCR (C) and Western immunoblotting (D). (Magnification: A, 63×.) Because Avp is a small peptide, its precursor neurophysin II is measured. Statistics: Student t test, P values shown compared with 0 h. Stimulation of Erk phosphorylation (p-Erk) as a function of total Erk (t-Erk) by Avp (10 −8 M) in osteoclast precursors (preosteoclasts), osteoclasts (OC), and osteoblasts establishes functionality of the Avpr1α in the presence or absence of the receptor inhibitor SR49059 (10 −8 M) (E). Western immunoblotting showing the expression of Avpr2 in preosteoclasts, OCs (F), and osteoblasts (G) isolated from Avpr1α −/− mice, as well as in MC3T3.E1 osteoblast precursors (G). Functionality of Avpr2 was confirmed by the demonstration that cells from Avpr1α −/− mice remained responsive to AVP in reducing the expression of osteoblast differentiation genes, namely Runx2, Osx, Bsp, Atf4, Opn, and Osteocalcin (quantitative PCR, P values shown) (H). Only relevant bands from Western blots are shown, with gaps introduced where empty lanes are excised to conserve space.

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Section: Hypothalamic Prolyl Endopeptidase (Prep) Regulates Pancreatimentioning

confidence: 99%

Hypothalamic prolyl endopeptidase (PREP) regulates pancreatic insulin and glucagon secretion in mice

Kim¹,

Toda²,

D’Agostino³

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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“…3.4.21.26; also called PO, POP, PE) is a serine protease (Venäläinen et al 2004). The primary function of PREP is thought to hydrolyze the Pro-Xaa bond of short peptides (Polgar 1994;Cunningham and O'Connor 1997).…”

Section: Introductionmentioning

confidence: 99%

Prolyl Endopeptidase-Deficient Mice Have Reduced Synaptic Spine Density in the CA1 Region of the Hippocampus, Impaired LTP, and Spatial Learning and Memory

D’Agostino

Kim²,

Liu³

et al. 2012

Cerebral Cortex

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Prolyl endopeptidase (PREP) is a phylogenetically conserved serine protease and, in humans and rodents, is highly expressed in the brain. Several neuropeptides associated with learning and memory and neurodegenerative disorders have been proposed to be the substrates for PREP, suggesting a possible role for PREP in these processes. However, its physiological function remains elusive. Combining genetic, anatomical, electrophysiological, and behavioral approaches, we show that PREP genetrap mice have decreased synaptic spine density in the CA1 region of the hippocampus, reduced hippocampal long-term potentiation, impaired hippocampalmediated learning and memory, and reduced growth-associated protein-43 levels when compared with wild-type controls. These observations reveal a role for PREP in mediating hippocampal plasticity and spatial memory formation, with implications for its pharmacological manipulation in diseases related to cognitive impairment.

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“…Prolyl oligopeptidase (POP, prolyl endopeptidase (PREP), EC 3.4.21.26) is a serine-type peptidase (family S9 of clan SC) [1,2] which hydrolyzes peptides shorter than 30 amino acids [3]. POP has been characterized from various mammalian and bacterial sources [2] and is widely distributed throughout different organisms [4].…”

Section: Introductionmentioning

confidence: 99%

Sequential Expression, Activity and Nuclear Localization of Prolyl Oligopeptidase Protein in the Developing Rat Brain

Hannula¹,

Männistö²,

Myöhänen³

2010

Dev Neurosci

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Prolyl oligopeptidase (POP) is a serine protease that hydrolyzes peptides shorter than 30-mer. Some evidence has recently been obtained that POP can generate protein-protein interactions and therefore participate in various physiological and pathological events. Several studies have reported that POP may be involved in neurogenesis since its activity increases during development and can be found in the nucleus of proliferating tissues. In cell cultures, POP has been shown to be localized in the nucleus, but only early in the development, since during maturation it is moved to the cytosol. We have now studied for the first time the expression of POP protein, its enzymatic activity and nuclear localization in vivo in the developing rat brain. We observed that enzymatic activity of POP is highest on embryonic day 18 while the protein amounts reach their peak at birth. Furthermore, POP is located in the nucleus only early in the development but is transferred to the cytosol already before parturition. Our in vivo results confirm the previous cell culture results supporting the role of POP in neurogenesis. A discordance of antenatal protein amounts and enzymatic activities is suggesting a tight regulation of POP activity and possibly even a nonhydrolytic role at that stage.

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Evolutionary relationships of the prolyl oligopeptidase family enzymes

Cited by 86 publications

References 33 publications

Hypothalamic prolyl endopeptidase (PREP) regulates pancreatic insulin and glucagon secretion in mice

Hypothalamic prolyl endopeptidase (PREP) regulates pancreatic insulin and glucagon secretion in mice

Prolyl Endopeptidase-Deficient Mice Have Reduced Synaptic Spine Density in the CA1 Region of the Hippocampus, Impaired LTP, and Spatial Learning and Memory

Sequential Expression, Activity and Nuclear Localization of Prolyl Oligopeptidase Protein in the Developing Rat Brain

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