Disruption of cell junctions induces apoptosis and reduces synthetic activity in lactating goat mammary gland

Journal of Dairy Science
H Ben ChedlyP Lacasse

Abstract

Although it is known that disruption of the cell junctions in the mammary gland induces a decrease in milk yield, the cellular mechanisms involved in milk secretion reduction during mammary cell junction disruption are not well understood. The aim of this study was to investigate the cellular regulations taking place after cell junction disruption in the mammary gland of goats. We performed intramammary infusions of Ca chelators to induce cell junction disruption. In a first group of 5 goats, intramammary infusions of ethylene glycol-bis(2-aminoethylether)-N,N,N',N'-tetraacetic acid (EGTA) in the right gland halves and saline as a control in the left gland halves were performed after 4 consecutive milkings. A second group of 4 goats received 4 intramammary infusions of citrate solution in the right gland halves and lactose solution as a control in the left halves. Intramammary infusion of EGTA and lactose induced a disruption of cell junctions, whereas citrate infusions failed to modify mammary epithelium integrity. The effect of the infused solutions was also tested in vitro via the measurement of transepithelial resistance, confirming mammary epithelium disruption by the EGTA, lactose, and citrate solutions at high concentrat...Continue Reading

References

Jun 1, 1974·The Journal of Cell Biology·D A Goodenough, N B Gilula
Mar 1, 1967·Journal of Dairy Science·G K Murthy, U Rhea
Jan 1, 1981·The Journal of Physiology·M C Neville, M Peaker
Dec 15, 1981·Biochemical and Biophysical Research Communications·C J WildeR J Mayer
Oct 1, 1995·The American Journal of Physiology·K StelwagenC G Prosser
Oct 23, 1997·Experimental Physiology·C J WildeD G Fernig
Jan 12, 2000·Journal of Dairy Science·L BouchardP Lacasse
Mar 11, 2000·Reviews of Reproduction·T M RowlandsO W Blaschuk
Apr 27, 2001·Small Ruminant Research : the Journal of the International Goat Association·P WareskiT Ploszaj
Jun 7, 2002·Mechanisms of Development·Oréda BoussadiaRolf Kemler
Aug 13, 2002·The Journal of Membrane Biology·B Rothen-RutishauserH Wunderli-Allenspach
Sep 30, 2004·Journal of Dairy Science·G LeitnerN Silanikove
Aug 16, 2005·Current Opinion in Cell Biology·Karl MatterMaria S Balda
Nov 1, 2006·Veterinary Immunology and Immunopathology·T L RobinsonJ Sutherland
Oct 16, 2007·The Journal of Investigative Dermatology·Carien M Niessen
Feb 23, 2008·Journal of Dairy Science·M BoutinaudJ Guinard-Flament
Jan 6, 2009·Biochimica Et Biophysica Acta·Maria S Balda, Karl Matter

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Citations

Sep 18, 2010·American Journal of Physiology. Gastrointestinal and Liver Physiology·Chang XiaoYana Zavros
Nov 19, 2015·Frontiers in Genetics·Marion BoutinaudVanessa Lollivier
Jul 2, 2021·Journal of Animal Science·Antoine LeducMarion Boutinaud

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