Anti-Müllerian hormone stimulates expression of the collagen-specific chaperone 47-kDa heat shock protein in bovine uterine epithelial cells.

Abstract

Uterine collagen is the most abundant component of the uterine extracellular matrix and plays a critical role in pregnancy. The 47-kDa heat shock protein (HSP47) is the sole collagen-specific molecular chaperone. We investigated the mechanisms regulating the expression of HSP47 in the uterus by assessing the effect of anti-Müllerian hormone (AMH) stimulation on HSP47 expression in cultured bovine uterine epithelial cells. AMH receptor type 2 (AMHR2), AMH, and HSP47 expression was assessed by fluorescence immunocytochemistry in uterine epithelial layers of the uteri of Japanese Black cows. The effect of AMH on HSP47 expression was assessed in cultured epithelial cells. The effect of MEK/ERK inhibitor on AMH-induced HSP47 expression was also assessed. We confirmed the expression of AMHR2, AMH, and HSP47 in the uterine epithelial layers. We confirmed the expression of AMHR2, AMH, HSP47, and type IV collagen in cultured uterine epithelial cells. AMH treatment at 10 or 100 ng/ml promoted significant HSP47 expression (p < 0.05). MEK/ERK inhibitor U0126 pretreatment suppressed such AMH stimulation on HSP47. These findings indicate that AMH induced HSP47 protein expression through the ERK pathway in bovine uterine epithelial cells.