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  • 1
    Online Resource
    Online Resource
    Cellular and subcellular distribution of rat brain prolyl oligopeptidase and its association with specific neuronal neurotransmitters
    Wiley ; 2008
    In:  Journal of Comparative Neurology Vol. 507, No. 5 ( 2008-04-10), p. 1694-1708
    Details
    In: Journal of Comparative Neurology, Wiley, Vol. 507, No. 5 ( 2008-04-10), p. 1694-1708
    Abstract: Prolyl oligopeptidase (POP) is a serine endopeptidase that hydrolyzes proline‐containing peptides shorter than 30‐mer. It has been suggested that POP is associated with cognitive functions and inositol 1,4,5‐triphosphate (IP 3 ) signaling. However, little is known about the distribution and physiological role of POP in the brain. We used immunohistochemistry to determine the cellular and subcellular distribution of POP in the rat brain. POP was specifically expressed in the glutamatergic pyramidal neurons of the cerebral cortex, particularly in the primary motor and somatosensory cortices, and also in the CA1 field of hippocampus. Purkinje cells of the cerebellum were also intensively immunostained for POP. Double immunofluorescence indicated that POP was present in the γ‐aminobutyric acid (GABA)ergic and cholinergic interneurons of the thalamus and cortex but not in the nigrostriatal dopaminergic neurons. POP did not colocalize with astrocytic markers in any part of the rat brain. We used postembedding immunoelectron microscopy to determine the distribution of POP at the subcellular level. POP was mainly present in neuronal cytosol and membranes, hardly at all in neuronal plasma membrane, but more extensively in intracellular membranes such as the rough endoplasmic reticulum and Golgi apparatus. Our findings point to a role for POP—evidently modifying neuropeptide levels—in excitatory and inhibitory neurotransmission in the central nervous system via glutamatergic, GABAergic, and cholinergic neurotransmission systems. Furthermore, according to our results, POP may be involved in thalamocortical neurotransmission, memory and learning functions of the hippocampal formation, and GABAergic regulation of voluntary movements. Subcellular distribution of POP points to a role in protein processing and secretion. J. Comp. Neurol. 507:1694–1708, 2008. © 2008 Wiley‐Liss, Inc.
    Type of Medium: Online Resource
    ISSN: 0021-9967 , 1096-9861
    URL: Issue
    URL: Article
    DOI: 10.1002/cne.v507:5
    DOI: 10.1002/cne.21642
    Language: English
    Publisher: Wiley
    Publication Date: 2008
    detail.hit.zdb_id: 1474879-4
    SSG: 12
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  • 2
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    Distribution of prolyl oligopeptidase in the mouse whole-body sections and peripheral tissues
    Springer Science and Business Media LLC ; 2008
    In:  Histochemistry and Cell Biology Vol. 130, No. 5 ( 2008-11), p. 993-1003
    Details
    In: Histochemistry and Cell Biology, Springer Science and Business Media LLC, Vol. 130, No. 5 ( 2008-11), p. 993-1003
    Type of Medium: Online Resource
    ISSN: 0948-6143 , 1432-119X
    URL: Article
    DOI: 10.1007/s00418-008-0468-x
    RVK:
    WA 15000
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2008
    detail.hit.zdb_id: 1398345-3
    SSG: 12
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  • 3
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    Slow-binding inhibitors of prolyl oligopeptidase with different functional groups at the P1 site
    Portland Press Ltd. ; 2004
    In:  Biochemical Journal Vol. 382, No. 3 ( 2004-09-15), p. 1003-1008
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 382, No. 3 ( 2004-09-15), p. 1003-1008
    Abstract: POP (prolyl oligopeptidase) specifically hydrolyses a number of small proline-containing peptides at the carboxy end of the proline residue and POP inhibitors have been shown to have cognition-enhancing properties. It has been noted that certain functional groups at the P1 site of the inhibitor, which correspond to the substrate residue on the N-terminal side of the bond to be cleaved, increase the inhibitory potency. However, detailed mechanistic and kinetic analysis of the inhibition has not been studied. In the present study, we examined the effect of different functional groups at the P1 site of the parent inhibitor isophthalic acid bis-(L-prolylpyrrolidine) amide on the binding kinetics to POP. Addition of CHO, CN or COCH2OH groups to the P1 site increased the inhibitory potency by two orders of magnitude (Ki=11.8–0.1 nM) and caused a clear slow-binding inhibition. The inhibitor containing a CHO group had the lowest association rate constant, kon=(2.43±0.12)×105 M−1·s−1, whereas the inhibitor with a CN group exhibited the fastest binding, kon=(12.0±0.08)×105 M−1·s−1. In addition, the dissociation rate was found to be crucially dependent on the type of the functional group. Compounds with COCH2OH and CHO groups had much longer half-lives of dissociation (over 5 h) compared with the compound with the CN group (25 min), although the Ki values of the compounds were relatively similar. A possibility to optimize the duration of inhibition by changing the functional group at the P1 site is important when planning therapeutically useful POP inhibitors.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/BJ20040992
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 2004
    detail.hit.zdb_id: 1473095-9
    SSG: 12
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