Abstract
Extracellular matrix (ECM) turnover is characterized by a unique balance between matrix metalloproteinases’ degradation activity and their natural inhibition by collagen specific tissue inhibitors. Human uterine ECM is a complex structure, majorly consisting of proteins as fibrillar collagen types I and III, fibronectin, and laminin. Collagenases are enzymes from the matrix metalloproteinases’ family, which are predominantly involved in fibrillar collagen types I and III degradation. They are mainly represented by matrix metalloproteinase-1, -13 (MMP-1, -13), naturally inhibited by tissue inhibitors (TIMP-1, -2). The collagen structure of the uterus has been shown to be impaired in women with preeclampsia. This is a result of MMPs/TIMPs dysregulation interplay. This review article summarizes the actual available research data in the literature about the role of MMP-1, MMP-13 and TIMP-1, and TIMP-2 in collagen types I and III turnover in healthy and complicated pregnancy. Their potential use as circulating markers for diagnosis, prognosis, and monitoring of the development of preeclampsia is discussed as well.
Highlights
Extracellular matrix (ECM) turnover is characterized by a unique balance between matrix metalloproteinases’ degradation activity and their natural inhibition by collagen specific tissue inhibitors
While TIMP-1 potently inhibits the activity of most Matrix Metalloproteinases (MMPs), with the exception of MMP-2 and MT1-MMP, TIMP-2 is a potent inhibitor of most MMPs, except MMP-9 [22]
They have concluded that failure of regulation of the MMP/TIMP system in controlling the extracellular matrix remodeling may lead to diverse pathology, such as gestational hypertension and preeclampsia
Summary
Collagen type I is a major connective tissue protein. It increases the strength and stability of the cytoskeleton. Type I collagen is fibrillar collagen and a major part of the interstitial membrane’s structure It is the most prevalent type of collagen and a key structural composition of many tissues. Type I collagen is the main structural protein of bone, skin, tendon, ligaments, sclera, cornea, and blood vessels, as well as an important component of other tissues. It is gathered in fibers forming a structural-mechanical scaffold (matrix) of bones, skin, tendons, cornea, blood vessel walls, and other connective tissues [1]. (I) chain and with a pro-alpha (I) chain (produced by the COL1A2 gene) to make a molecule of type I procollagen These triple-stranded, rope-like procollagen molecules must be processed by enzymes outside the cell. Type I collagen provides tensile stiffness in tendons and fascia, while in bone, it defines considerable biomechanical properties concerning load bearing and tensile [4]
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