Abstract
Although participation of matrix metalloproteinases (MMPs) in reproductive tract remodeling has been strongly suggested in mammalian species, the role of MMPs in the avian oviduct has received little attention. To gain a better understanding of the potential role of the MMP system in avian oviduct development, mRNA and protein expression, localization of selected MMPs and their tissue inhibitors (TIMPs), and gelatinolytic activity in the oviduct of growing chickens were examined. The oviducts were collected from Hy-Line Brown hens before (10, 12, 14 and 16 weeks of age) and after (week 17) the onset of egg laying. The MMP-2, -7, -9 and TIMP-2 and -3 genes were found to be differentially expressed in all examined oviductal sections: the infundibulum, magnum, isthmus and shell gland on both mRNA (by real time polymerase chain reaction) and protein (by western blotting and immunohistochemistry) levels. In the course of oviduct development, the relative expression of all genes decreased in most sections. Protein level of MMP-9 was diminished, while MMP-7 and TIMP-3 were elevated in the oviduct of growing birds. MMP-2 and TIMP-2 protein levels remained constant, with a slight increase in MMP-2 concentration just before reaching maturity. The relative activity of MMP-2 and -9 (assessed by gelatin zymography) was higher (P < 0.05, P < 0.01) in immature birds compared with adults. Immunohistochemistry demonstrated cell- and tissue-specific localization of MMPs and TIMPs in the wall of the chicken oviduct. We concluded that changes in the expression of examined MMPs and their inhibitors, as well as alterations in MMP activity occurring simultaneously with changes in the morphology of the chicken oviduct, suggest the involvement of the MMP system in the proper development and functioning of this organ. Mechanisms regulating the expression and activity of MMPs require further clarification.
Highlights
The extracellular matrix (ECM) is one of the most important regulators of cellular physiology, providing an environment for cell migration, proliferation, differentiation, and apoptosis (Smith et al 1999)
The present study demonstrates, for the first time, the expression of matrix metalloproteinases (MMPs)-2, -7 -9 and tissue inhibitors of metalloproteinases (TIMPs)-2 and -3 at mRNA and protein levels as well as activity of MMP-2 and -9 in particular segments of the chicken oviduct during maturation
Existing data related to MMPs were fragmentary and revealed only the presence of MMP-2, -9 and TIMP-2 and -3 transcripts in some parts of the chicken oviduct (Réhault-Godbert et al 2008; Dunn et al 2009; Song et al 2011; Hrabia et al 2013)
Summary
The extracellular matrix (ECM) is one of the most important regulators of cellular physiology, providing an environment for cell migration, proliferation, differentiation, and apoptosis (Smith et al 1999). Numerous studies have established that the key enzymes involved in the control of ECM turnover and homeostasis are matrix metalloproteinases (MMPs) (Page-McCaw et al 2007; Murphy and Nagase 2008; Kessenbrock et al 2010). Architectural features and substrate preference categorize the MMP family members into several classes, i.e. the collagenases (MMP-1, -8, -13), gelatinases (MMP-2, -9), stromelysins (MMP-3, -10, -11), matrilysins (MMP-7, -26), membrane type MMPs (MT-MMP-1, -2, -3, -4, -5, -6), and other less characterized members (Page-McCaw et al 2007). The gelatinases, stromelysins and matrilysins are capable of degrading major constituents of basement membranes, including type IV collagen, laminin and fibronectin (Senior et al 1991; Nagase et al 2006). In addition to the removal of unwanted ECM molecules, MMPs exhibit activity toward other MMPs, growth factors and cytokines. It has become clear that MMPs influence many cellular functions and so their activity
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