TY - JOUR
T1 - Short-chain fatty acid signaling pathways in bovine mammary epithelial cells
AU - Yonezawa, Tomo
AU - Haga, Satoshi
AU - Kobayashi, Yosuke
AU - Katoh, Kazuo
AU - Obara, Yoshiaki
N1 - Funding Information:
The authors sincerely thank Dr. Komatsu T. (National Agricultural Research Organization, National Agricultural Center for Tohoku region, Iwate-ken, Japan) for the gift of bovine mammary gland samples. This work was supported by a grant from Japan Society for Promotion of Science.
PY - 2009/2/25
Y1 - 2009/2/25
N2 - GPR41 and 43 have recently been identified as G-protein-coupled cell-surface receptors for short-chain fatty acids (SCFAs). Bovine orthologs of GPR41 and 43 (bGPR41 and 43) mRNA were detected by RT-PCR in cloned bovine mammary epithelial cells (bMEC) and various lactation stages of bovine mammary gland. Acetate and propionate caused an increase in intracellular Ca2+ concentrations in these cells that was blocked by the treatment with pertussis toxin (PTX). SCFAs significantly reduced forskolin-induced cAMP concentrations in these cells. The phosphorylation of mitogen-activated protein kinase (MAPK) p38 was selectively increased by SCFAs. The downstream substrate heat shock protein 27 (HSP27) was also phosphorylated by SCFAs at Ser-78 and -82, but not -15. These results suggest that bGPR41 mainly, but not bGPR43, mediate SCFA signaling in mammary epithelial cells and thereby plays some important role in mammary gland.
AB - GPR41 and 43 have recently been identified as G-protein-coupled cell-surface receptors for short-chain fatty acids (SCFAs). Bovine orthologs of GPR41 and 43 (bGPR41 and 43) mRNA were detected by RT-PCR in cloned bovine mammary epithelial cells (bMEC) and various lactation stages of bovine mammary gland. Acetate and propionate caused an increase in intracellular Ca2+ concentrations in these cells that was blocked by the treatment with pertussis toxin (PTX). SCFAs significantly reduced forskolin-induced cAMP concentrations in these cells. The phosphorylation of mitogen-activated protein kinase (MAPK) p38 was selectively increased by SCFAs. The downstream substrate heat shock protein 27 (HSP27) was also phosphorylated by SCFAs at Ser-78 and -82, but not -15. These results suggest that bGPR41 mainly, but not bGPR43, mediate SCFA signaling in mammary epithelial cells and thereby plays some important role in mammary gland.
KW - Mammary epithelial cell
KW - Receptors for short-chain fatty acids
KW - Short-chain fatty acids
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U2 - 10.1016/j.regpep.2008.11.012
DO - 10.1016/j.regpep.2008.11.012
M3 - Article
C2 - 19101595
AN - SCOPUS:59849087617
VL - 153
SP - 30
EP - 36
JO - Regulatory Peptides
JF - Regulatory Peptides
SN - 0167-0115
IS - 1-3
ER -