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Study on PREP localization in mouse seminal vesicles and its possible involvement during regulated exocytosis

Published online by Cambridge University Press:  07 May 2019

Massimo Venditti ,
Francesco Aniello ,
Alessandra Santillo  and
Sergio Minucci Open the ORCID record for Sergio Minucci [Opens in a new window]
Massimo Venditti
Affiliation:
Dipartimento di Medicina Sperimentale, Sez. Fisiologia Umana e Funzioni Biologiche Integrate ‘F. Bottazzi’, Università degli Studi della Campania ‘Luigi Vanvitelli’, via Costantinopoli 16, 80138Napoli, Italy
Francesco Aniello
Affiliation:
Dipartimento di Biologia, Università degli Studi di Napoli ‘Federico II’, via Cinthia 26, 80126Napoli, Italy
Alessandra Santillo
Affiliation:
Dipartimento di Scienze e Tecnologie Ambientali, Biologiche e Farmaceutiche, Università degli Studi della Campania ‘Luigi Vanvitelli’, via Vivaldi 43, 81100Caserta, Italy
Sergio Minucci*
Affiliation:
Dipartimento di Medicina Sperimentale, Sez. Fisiologia Umana e Funzioni Biologiche Integrate ‘F. Bottazzi’, Università degli Studi della Campania ‘Luigi Vanvitelli’, via Costantinopoli 16, 80138Napoli, Italy
*
Address for correspondence: Sergio Minucci, Dipartimento di Medicina Sperimentale, Sez. Fisiologia Umana e Funzioni Biologiche Integrate ‘F. Bottazzi’, Università degli Studi della Campania ‘Luigi Vanvitelli’, via Costantinopoli 16, 80138 Napoli. Tel: +39 081 5665829. Fax: +39 081 5667500. E-mail: [email protected]
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Summary

Prolyl endopeptidase (PREP) is a post-proline cleaving enzyme. It is involved in the regulation of multiple inositol polyphosphate phosphatase activity implicated in the pathway of inositol 1,4,5-trisphosphate, resulting in the modulation of cytosolic Ca2+ levels. Besides its peptidase activity, PREP was identified as a binding partner of tubulin, suggesting that it may participate in microtubule-associate processes. In this paper, we evaluated the expression of PREP mRNA and protein by polymerase chain reaction and western blot analyses and its co-localization with tubulin by immunofluorescence in adult mouse seminal vesicles. We showed that both proteins are cytoplasmic: tubulin is localized at the apical half part of the cell, while PREP has a more diffuse localization, showing a prominent distribution at the apical cytoplasm. These findings support our hypothesis of a specific role for PREP in cytoskeletal rearrangement that occurs during the exocytosis of secretory vesicles, and in particular its association with tubulin filaments. Moreover, it may regulate Ca2+ levels, and promote the final step of vesicular exocytosis, namely the fusion of the vesicles with the plasma membrane. These results strongly suggest that there is a pivotal role for PREP in vesicle exocytosis, as well as in the physiology of mouse seminal vesicles.

Keywords

CytoskeletonExocrine glandProlyl endopeptidaseRegulated exocytosisSeminal vesiclesTubulin
Type
Research Article
Information
Zygote , Volume 27 , Issue 3 , June 2019 , pp. 160 - 165
Copyright
© Cambridge University Press 2019 

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