IBR   13079
INSTITUTO DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
ANNEXINA2 AND S100A10 IN THE MAMMALIAN OVIDUCT EPITHELIUM
Autor/es:
TEIJEIRO JUAN MANUEL Y MARINI PATRICIA
Lugar:
Smolenice, República de Eslovaquia
Reunión:
Workshop; Workshop European Calcium Society Smolenice 2009; 2009
Resumen:
<!--
/* Font Definitions */
@font-face
{font-family:Times-Roman;
panose-1:0 0 0 0 0 0 0 0 0 0;
mso-font-charset:0;
mso-generic-font-family:roman;
mso-font-format:other;
mso-font-pitch:auto;
mso-font-signature:3 0 0 0 1 0;}
/* Style Definitions */
p.MsoNormal, li.MsoNormal, div.MsoNormal
{mso-style-parent:"";
margin:0cm;
margin-bottom:.0001pt;
mso-pagination:widow-orphan;
font-size:12.0pt;
mso-bidi-font-size:10.0pt;
font-family:"Times New Roman";
mso-fareast-font-family:"Times New Roman";
mso-ansi-language:CS;
mso-fareast-language:SK;}
@page Section1
{size:595.3pt 841.9pt;
margin:70.9pt 70.9pt 70.9pt 70.9pt;
mso-header-margin:35.45pt;
mso-footer-margin:35.45pt;
mso-paper-source:0;}
div.Section1
{page:Section1;}
-->
In eutherian mammals, sperm-oviduct
interaction provides the formation of a sperm storage and allows the selection
of sperm with certain qualities. In sows, we proposed
that the oviductal Sperm Binding Glycoprotein SBG is involved in sperm selection. As to reservoir formation, in bovine, essential proteins involved have been characterized as sperm
adsorbed PDC109 and oviductal cells Annexin (ANXA) 1, 2, 4 and 5. In porcine, AQN1 is the
sperm component and ANXA2 the oviductal component most likely to be clue
proteins responsible for sperm reservoir formation. We have previously proposed
that ANXA2 may be part of a ubiquous mechanism of sperm-oviduct interaction. As
S100A10 is usually associated to ANXA2, in this work we search for the presence
of ANXA2 and S100A10 in the oviducts of several mammals by western blot. We
find that ANXA2 and S100A10 co-exist in the oviductal cell extracts from pig,
human, cow, cat, dog, mouse and rabbit. Immunohistochemistry of porcine isthmus
and ampulla shows that ANXA2 and S100A10 localize to the same type of cells, cilliary
isthmic cells surrounding the lumen. Different extraction procedures were
performed on porcine oviductal cell membranes, showing ANXA2 liberation in
every case, and S100A10 release increasing from Triton X100 to ionic strength
to EGTA containing buffer, suggesting Ca++ may be involved in its
attachment. Immunoprecipitation of epithelial cell extracts with anti-ANXA2
antibodies shows S100A10 co-precipitation.
We conclude that ANXA2-S100A10 complex is
present in the mammalian oviduct and that its interaction with sperm proteins may
be a part of the sperm-oviductal cell relation in several mammals.