TY - JOUR
T1 - Specific integrin subunits in bovine oocytes, including novel sequences for alpha 6 and beta 3 subunits
AU - Pate, Barry J.
AU - White, Kenneth L.
AU - Winger, Quinton A.
AU - Rickords, Lee F.
AU - Aston, Kenneth I.
AU - Sessons, Benjamin R.
AU - Li, Guang Peng
AU - Campbell, Kenneth D.
AU - Weimer, Bart C
AU - Bunch, Thomas D.
PY - 2007/5
Y1 - 2007/5
N2 - Integrins facilitate attachment of cells to the extra-cellular matrix, often binding the arginine-glycine-aspartic acid tri-peptide motif, thus facilitating cell migration, mediating cell-cell adhesion, linking the extracellular matrix (ECM) with cytoskeletal elements, and acting as signaling molecules. Adhesion activates signaling mechanisms that regulate integrin function, cytoskeletal assembly, cell behavior, and protein synthesis. Immunofluorescence was used to determine the presence of integrin α and β subunits on the surface of bovine oocytes using a panel of monoclonal antibodies (mAbs) specific for αL, αM, αX, αV, α2, α4, α6, β1, β2, and β3 antigens, with multiple antibodies for each subunit. Confocal microscopy indicated the presence of αV, α6, α4, α2, β1, and β3 integrin subunits on the plasma membrane of bovine oocytes. The presence of these subunits was verified by RT-PCR analysis using primers designed based on known gene sequences of bovine integrin subunits, or by using sequence information using bovine expressed sequence tags (EST) compared with known human and murine integrin subunit gene sequence information. Previously unpublished sequence information for bovine α6 and β3 integrins was determined. The presence of these integrin subunits on the bovine oocyte vitelline membrane supports the hypothesis that sperm-oocyte interactions in the bovine are mediated by integrins.
AB - Integrins facilitate attachment of cells to the extra-cellular matrix, often binding the arginine-glycine-aspartic acid tri-peptide motif, thus facilitating cell migration, mediating cell-cell adhesion, linking the extracellular matrix (ECM) with cytoskeletal elements, and acting as signaling molecules. Adhesion activates signaling mechanisms that regulate integrin function, cytoskeletal assembly, cell behavior, and protein synthesis. Immunofluorescence was used to determine the presence of integrin α and β subunits on the surface of bovine oocytes using a panel of monoclonal antibodies (mAbs) specific for αL, αM, αX, αV, α2, α4, α6, β1, β2, and β3 antigens, with multiple antibodies for each subunit. Confocal microscopy indicated the presence of αV, α6, α4, α2, β1, and β3 integrin subunits on the plasma membrane of bovine oocytes. The presence of these subunits was verified by RT-PCR analysis using primers designed based on known gene sequences of bovine integrin subunits, or by using sequence information using bovine expressed sequence tags (EST) compared with known human and murine integrin subunit gene sequence information. Previously unpublished sequence information for bovine α6 and β3 integrins was determined. The presence of these integrin subunits on the bovine oocyte vitelline membrane supports the hypothesis that sperm-oocyte interactions in the bovine are mediated by integrins.
KW - Activation
KW - Bovine
KW - Integrin
KW - Oocyte
KW - Receptor
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U2 - 10.1002/mrd.20649
DO - 10.1002/mrd.20649
M3 - Article
C2 - 17039534
AN - SCOPUS:33947647863
VL - 74
SP - 600
EP - 607
JO - Molecular Reproduction and Development
JF - Molecular Reproduction and Development
SN - 1040-452X
IS - 5
ER -