Cargando…

The Non-Gastric H(+)/K(+) ATPase (ATP12A) Is Expressed in Mammalian Spermatozoa

H(+)/K(+) ATPase Type 2 is an heteromeric membrane protein involved in cation transmembrane transport and consists of two subunits: a specific α subunit (ATP12A) and a non-specific β subunit. The aim of this study was to demonstrate the presence and establish the localization of ATP12A in spermatozo...

Descripción completa

Detalles Bibliográficos
Autores principales: Favia, Maria, Gerbino, Andrea, Notario, Elisabetta, Tragni, Vincenzo, Sgobba, Maria Noemi, Dell’Aquila, Maria Elena, Pierri, Ciro Leonardo, Guerra, Lorenzo, Ciani, Elena
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8835340/
https://www.ncbi.nlm.nih.gov/pubmed/35162971
http://dx.doi.org/10.3390/ijms23031048
_version_ 1784649408816611328
author Favia, Maria
Gerbino, Andrea
Notario, Elisabetta
Tragni, Vincenzo
Sgobba, Maria Noemi
Dell’Aquila, Maria Elena
Pierri, Ciro Leonardo
Guerra, Lorenzo
Ciani, Elena
author_facet Favia, Maria
Gerbino, Andrea
Notario, Elisabetta
Tragni, Vincenzo
Sgobba, Maria Noemi
Dell’Aquila, Maria Elena
Pierri, Ciro Leonardo
Guerra, Lorenzo
Ciani, Elena
author_sort Favia, Maria
collection PubMed
description H(+)/K(+) ATPase Type 2 is an heteromeric membrane protein involved in cation transmembrane transport and consists of two subunits: a specific α subunit (ATP12A) and a non-specific β subunit. The aim of this study was to demonstrate the presence and establish the localization of ATP12A in spermatozoa from Bubalus bubalis, Bos taurus and Ovis aries. Immunoblotting revealed, in all three species, a major band (100 kDa) corresponding to the expected molecular mass. The ATP12A immunolocalization pattern showed, consistently in the three species, a strong signal at the acrosome. These results, described here for the first time in spermatozoa, are consistent with those observed for the β(1) subunit of Na(+)/K(+) ATPase, suggesting that the latter may assemble with the α subunit to produce a functional ATP12A dimer in sperm cells. The above scenario appeared to be nicely supported by 3D comparative modeling and interaction energy calculations. The expression of ATP12A during different stages of bovine sperm maturation progressively increased, moving from epididymis to deferent ducts. Based on overall results, we hypothesize that ATP12A may play a role in acrosome reactions. Further studies will be required in order to address the functional role of this target protein in sperm physiology.
format Online
Article
Text
id pubmed-8835340
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-88353402022-02-12 The Non-Gastric H(+)/K(+) ATPase (ATP12A) Is Expressed in Mammalian Spermatozoa Favia, Maria Gerbino, Andrea Notario, Elisabetta Tragni, Vincenzo Sgobba, Maria Noemi Dell’Aquila, Maria Elena Pierri, Ciro Leonardo Guerra, Lorenzo Ciani, Elena Int J Mol Sci Article H(+)/K(+) ATPase Type 2 is an heteromeric membrane protein involved in cation transmembrane transport and consists of two subunits: a specific α subunit (ATP12A) and a non-specific β subunit. The aim of this study was to demonstrate the presence and establish the localization of ATP12A in spermatozoa from Bubalus bubalis, Bos taurus and Ovis aries. Immunoblotting revealed, in all three species, a major band (100 kDa) corresponding to the expected molecular mass. The ATP12A immunolocalization pattern showed, consistently in the three species, a strong signal at the acrosome. These results, described here for the first time in spermatozoa, are consistent with those observed for the β(1) subunit of Na(+)/K(+) ATPase, suggesting that the latter may assemble with the α subunit to produce a functional ATP12A dimer in sperm cells. The above scenario appeared to be nicely supported by 3D comparative modeling and interaction energy calculations. The expression of ATP12A during different stages of bovine sperm maturation progressively increased, moving from epididymis to deferent ducts. Based on overall results, we hypothesize that ATP12A may play a role in acrosome reactions. Further studies will be required in order to address the functional role of this target protein in sperm physiology. MDPI 2022-01-19 /pmc/articles/PMC8835340/ /pubmed/35162971 http://dx.doi.org/10.3390/ijms23031048 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Favia, Maria
Gerbino, Andrea
Notario, Elisabetta
Tragni, Vincenzo
Sgobba, Maria Noemi
Dell’Aquila, Maria Elena
Pierri, Ciro Leonardo
Guerra, Lorenzo
Ciani, Elena
The Non-Gastric H(+)/K(+) ATPase (ATP12A) Is Expressed in Mammalian Spermatozoa
title The Non-Gastric H(+)/K(+) ATPase (ATP12A) Is Expressed in Mammalian Spermatozoa
title_full The Non-Gastric H(+)/K(+) ATPase (ATP12A) Is Expressed in Mammalian Spermatozoa
title_fullStr The Non-Gastric H(+)/K(+) ATPase (ATP12A) Is Expressed in Mammalian Spermatozoa
title_full_unstemmed The Non-Gastric H(+)/K(+) ATPase (ATP12A) Is Expressed in Mammalian Spermatozoa
title_short The Non-Gastric H(+)/K(+) ATPase (ATP12A) Is Expressed in Mammalian Spermatozoa
title_sort non-gastric h(+)/k(+) atpase (atp12a) is expressed in mammalian spermatozoa
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8835340/
https://www.ncbi.nlm.nih.gov/pubmed/35162971
http://dx.doi.org/10.3390/ijms23031048
work_keys_str_mv AT faviamaria thenongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT gerbinoandrea thenongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT notarioelisabetta thenongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT tragnivincenzo thenongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT sgobbamarianoemi thenongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT dellaquilamariaelena thenongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT pierriciroleonardo thenongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT guerralorenzo thenongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT cianielena thenongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT faviamaria nongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT gerbinoandrea nongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT notarioelisabetta nongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT tragnivincenzo nongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT sgobbamarianoemi nongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT dellaquilamariaelena nongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT pierriciroleonardo nongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT guerralorenzo nongastrichkatpaseatp12aisexpressedinmammalianspermatozoa
AT cianielena nongastrichkatpaseatp12aisexpressedinmammalianspermatozoa