Abstract
We investigated whether chronic ethanol intake is capable of altering the MMP-2 and MMP-9 activities and TIMP-2 and TIMP-1 expression in the dorsal and lateral prostatic lobes of low (UChA) and high (UChB) ethanol-preferring rats. MMP-2 and MMP-9 activities and TIMP-1 and TIMP-2 expression were significantly reduced in the lateral prostatic lobe of the ethanol drinking animals. Dorsal prostatic lobe was less affected showing no significant alterations in these proteins, except for a reduction in the TIMP-1 expression in UChA rats. These important findings demonstrate that chronic ethanol intake impairs the physiological balance of the prostate extracellular matrix turnover, through downregulation of MMPs, which may contribute to the development of prostatic diseases. Furthermore, since these proteins are also components of prostate secretion, the negative impact of chronic ethanol intake on fertility may also involve reduction of MMPs and TIMPs in the seminal fluid.
Highlights
The ethanol alters the epithelial cells [1], the normal stromalepithelial homeostasis [2], the inflammation [3], and the concentration of retinoic acid [4] in the prostate
matrix metalloproteinase (MMP)-2 activity was significantly decreased in UChA rats (Figure 1(b)) and slightly reduced in the UChB rats (Figure 1(d))
The amount of ethanol consumed by the UChA and UChB rats allowed us to evaluate their effects upon MMP-2 and MMP-9 activities as well as TIMP-1 and TIMP-2 expression in the dorsal and lateral prostatic lobes
Summary
The ethanol alters the epithelial cells [1], the normal stromalepithelial homeostasis [2], the inflammation [3], and the concentration of retinoic acid [4] in the prostate. This gland produces and secretes collagenase-like peptidase and gelatinolytic proteinases, such as matrix metalloproteinase (MMP), that are important for reproduction [5,6,7] and for turnover of the extracellular matrix components (ECM) as collagens, elastins, gelatin, matrix glycoproteins, and proteoglycan [8,9,10]. Ethanol has been demonstrated to alter MMP-2 and MMP-9 activities in isolated vascular cells and breast cancer cells [15, 16]
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