Abundance of ADAM-8, -9, -10, -12, -15 and -17 and ADAMTS-1 in mouse uterus during the oestrous cycle
Citations Over TimeTop 25% of 2005 papers
Abstract
The aim of the present study was to determine whether a disintegrin and metalloproteinase (ADAM)-8, -9, -10, -12, -15 and -17 and a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS)-1 are involved in the remodelling process of the mouse uterus during the oestrous cycle. The mRNA expression of ADAM was observed in all uterine tissues throughout the entire cycle. The levels of ADAM-8 mRNA were maximal at pro-oestrus, whereas the expression of ADAM-9 and ADAMTS-1 mRNA was maximal at oestrus. The minimum mRNA level of all ADAM genes always occurred at dioestrus. The mRNA levels of ADAM-10, -12, -15 and -17 did not vary significantly, regardless of the stage of the oestrous cycle. Immunoblot analyses demonstrated the presence of all ADAM proteins throughout the cycle. In terms of protein intensities, ADAM-8, -12 and -17 were maximal at pro-oestrus, whereas ADAM-10 and ADAMTS-1 were maximal at metoestrus and ADAM-9 was maximal at oestrus. Regardless of the ADAM species, minimal protein expression always occurred at dioestrus. Immunohistochemical studies showed ADAM protein expression in luminal and glandular epithelial layers, but not in the stromal layer. Moreover, ADAM proteins were found to be heterogeneously localised and their individual localisations depended on the stage of the oestrous cycle. From these observations, we suggest that the ADAM genes play an important role in mouse uterine tissue remodelling during the oestrous cycle.
Related Papers
- → Structural Characterization of the Ectodomain of a Disintegrin and Metalloproteinase-22 (ADAM22), a Neural Adhesion Receptor Instead of Metalloproteinase(2009)65 cited
- → A Disintegrin and Metalloprotease 17 in the Cardiovascular and Central Nervous Systems(2016)63 cited
- → Molecular cloning and functional characterization of a snake venom metalloprotease(1999)47 cited
- → Functional roles of the two distinct domains of halysase, a snake venom metalloprotease, to inhibit human platelet aggregation(2005)23 cited
- The Role of CD9 in Regulating TNF-α-Induced Expression of A Disintegrin and Metalloprotease 17 (ADAM17) in Aortic Endothelial Cells(2019)