Ontogeny of Soluble and Particulate Prolyl Endopeptidase Activity in Several Areas of the Rat Brain and in the Pituitary Gland

Agirregoitia, Naiara; Irazusta, Amaia; Ruíz, Francisco López; Irazusta, Jon; Gil, Javier

doi:10.1159/000073508

Cited by 16 publications

(20 citation statements)

References 43 publications

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“…Alternatively, the mouse placental POP may not even be involved in cell proliferation and have other roles. It is interesting that the cytoplasmic POP had a higher enzymatic activity than the membrane-associated form, which is consistent with previous reports (Agirregoitia et al, 2003;Irazusta et al, 2002;Tenorio-Laranga et al, 2008). The cytoplasmic POP was found in every placental cell by immunohistochemistry, suggesting that it has a common function to many cells.…”

Section: Molecular Mass Of Popsupporting

confidence: 91%

“…The POP enzymatic activity or its mRNA expression have been reported to be high at early developmental stages of the rat brain (Kato et al, 1980;Fuse et al, 1990;Yamanaka et al, 1999;Agirregoitia et al, 2003Agirregoitia et al, , 2010, pituitary (Agirregoitia et al, 2003), and liver (Matsubara et al, 1998) as well as of the mouse testis (Kimura et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

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Localization and subcellular distribution of prolyl oligopeptidase in the mouse placenta

2011

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Prolyl oligopeptidase (POP) is a serine endopeptidase which selectively digests a -Pro-X-peptide bond.Our previous study showed that POP mRNA was strongly expressed in the spongiotrophoblast of the mouse placenta at E17.5, suggesting its importance in development. To gain more insight into POP's role during gestation, we investigated its expression using different developmental stages of placenta. As a result of in situ hybridization, we found that localization of POP mRNA changed at E12.5. POP mRNA was strongly expressed in the spongiotrophoblast and labyrinth at E10.5 and E11.5 but thereafter only in the spongiotrophoblast. Immunohistochemistry revealed that POP was present in the parietal trophoblast giant cell, the spongiotrophoblast cell, and the labyrinth at E11.5 but the strong expression in the labyrinth was maintained only in the canal-associated and sinusoidal trophoblast giant cells at E16.5 and E18.5. To determine subcellular distribution of the POP protein, we fractionated the placental extract into cytoplasmic, membrane, and nuclear subfractions. By Western blot analysis, POP was detected in the cytoplasmic and membrane fractions but not in the nuclear fraction at E11.5 and E16.5. Interestingly, the cytoplasmic POP exhibited higher enzymatic activity than the membrane-associated type. These data suggest that the cytoplasmic and membrane-associated POP have distinct roles in different types of placental cells.

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Section: Molecular Mass Of Popsupporting

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Localization and subcellular distribution of prolyl oligopeptidase in the mouse placenta

2011

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“…The developmental decrease in the degradation process was consistent with previous reports in males [41, 42], whereas the increase observed in females was not previously described. To our knowledge, developing PEP activity has not been studied so far in females.…”

Section: Discussionsupporting

confidence: 92%

Molecular Polymorphism of Native Gonadotropin-Releasing Hormone (GnRH) Is Restricted to Mammalian GnRH and [Hydroxyproline<sup>9</sup>] GnRH in the Developing Rat Brain

Gautron

Gras²,

Enjalbert³

2005

Neuroendocrinology

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Although chicken gonadotropin-releasing hormone (GnRH)-II is thought to occur in most animal species, its presence and that of two other variants (lamprey GnRH-III, salmon GnRH) is questionable in rodents. Here we report on the GnRH peptides present in the hypothalamus and the remaining brain of rat of both sexes during development. No immunoreactivity was detected in the elution zone of either native or hydroxylated forms of the above three variants in any of brain extracts chromatographed. The main peptides detected were mammalian GnRH (mGnRH) and m[hydroxyproline⁹]GnRH (mHypGnRH). In the hypothalamus, these peptides were associated with their free acid and precursor forms. N-terminal fragments from both native decapeptides ([1–5]GnRH) and mGnRH ([1–9]GnRH) were observed only in the hypothalamus. C-terminal fragments were detected in both tissues. The relative proportions of mGnRH and mHypGnRH showed no developmental changes in the remaining brain. The hypothalamic proportions of mHypGnRH were high on day 5, and decreased from day 15 onwards. The [Gly¹¹]-precursor to mHypGnRH molar ratio was twofold lower than with the non-hydroxylated peptides. The mGnRH to [1–9]GnRH molar ratio increased in males but decreased in females during development. No sex-related differences were observed in the native decapeptide to [1–5]GnRH molar ratio. It was concluded that (1) chicken GnRH-II is not present in all mammals, (2) mGnRH and mHypGnRH are the main GnRH isoforms present in the rat brain, (3) the processing of [Gly¹¹]-precursor into mHypGnRH occurs at a higher rate than that of mGnRH, and (4) the catabolism does not interfere with the developmental changes undergone by the mGnRH and mHypGnRH brain contents.

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“…In humans and rodents it is highly expressed in the brain (2), including the cortex, striatum, hypothalamus, hippocampus, and amygdala (3)(4)(5)(6). The physiological role of PREP remains elusive (7).…”

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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Ontogeny of Soluble and Particulate Prolyl Endopeptidase Activity in Several Areas of the Rat Brain and in the Pituitary Gland

Cited by 16 publications

References 43 publications

Localization and subcellular distribution of prolyl oligopeptidase in the mouse placenta

Localization and subcellular distribution of prolyl oligopeptidase in the mouse placenta

Molecular Polymorphism of Native Gonadotropin-Releasing Hormone (GnRH) Is Restricted to Mammalian GnRH and [Hydroxyproline<sup>9</sup>] GnRH in the Developing Rat Brain

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

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