Fetal or gestational membranes extend from the placenta to enclose the fetus and amniotic fluid. While the membranes spontaneously rupture at term in normal pregnancies, they can rupture prematurely before the onset of labor, termed preterm prelabor rupture of membranes (PPROM). PPROM can be triggered by bacterial infection or sterile inflammation in the membranes, known as chorioamnionitis (CAM). The membranes derive their tensile strength from a collagen-rich extracellular matrix (ECM); as such, understanding the enzymes and processes that can degrade the membrane ECM are of paramount importance. Matrix metalloproteinases (MMPs) are a class of enzymes capable of degrading collagen and other components of the ECM, and can be induced by inflammation. We used a scoping review to address the question of how MMP activity is associated with PPROM, particularly their induction due to sterile or nonsterile CAM. We have found that the most studied MMPs in PPROM were MMPs 2, 8, and 9. Additionally, some MMPs are constitutively active, while others are induced by inflammation. Mechanistic studies of the pathways that induce MMP activation are sparse, and this area is ripe for future studies. Targeting MMP activation could be a future strategy to delay or prevent PPROM.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11729612 | PMC |
http://dx.doi.org/10.1111/aji.13642 | DOI Listing |
Invest Ophthalmol Vis Sci
January 2025
University Eye Clinic Maastricht, Maastricht University Medical Center, Maastricht, the Netherlands.
Cell Death Dis
January 2025
Department of Pathology, Qilu Hospital and School of Basic Medical Sciences Shandong University, Jinan, Shandong, PR China.
Long noncoding RNAs (lncRNAs) are key regulators during gastric cancer (GC) development and may be viable treatment targets. In the present study, we showed that the expression of the long intergenic noncoding RNA 01016 (LINC01016) is significantly higher in GC tissues with lymph node metastasis (LNM) than those without LNM. LINC01016 overexpression predicts a poorer relapse-free survival (RFS) and overall survival (OS).
View Article and Find Full Text PDFBiochem Genet
January 2025
Department of Physiology, University of Louisville School of Medicine, Louisville, KY, 40202, USA.
Although DNA methyltransferase 1 (DNMT1) and RNA editor ADAR triplications exist in Down syndrome (DS), their specific roles remain unclear. DNMT methylates DNA, yielding S-adenosine homocysteine (SAH), subsequently converted to homocysteine (Hcy) and adenosine by S-adenosine homocysteine (Hcy) hydrolase (SAHH). ADAR converts adenosine to inosine and uric acid.
View Article and Find Full Text PDFBiochem Biophys Res Commun
January 2025
Department of Biochemistry and Molecular Cell Biology, Shanghai Jiao Tong University School of Medicine, Shanghai, China. Electronic address:
The glomerular filtration barrier (GFB) has a unique spatial structure, including porous capillary endothelial cells, glomerular basal membrane (GBM) and highly specialized podocytes. This special structure is essential for the hemofiltration process of nephrons. GBM is the central meshwork structure of GFB formed by the assembly and fusion of various extracellular matrix (ECM) macromolecules, such as laminins and collagens, which undergo isoform transformation and maturation that may require precise regulation by metalloproteinases.
View Article and Find Full Text PDFAn Acad Bras Cienc
January 2025
Universidade Federal de Pernambuco, Departamento de Histologia e Embriologia, Av. Prof. Moraes Rego, 1235, Cidade Universitária, 50760-420 Recife, PE, Brazil.
Matrix metalloproteinases (MMP) have been identified as biomarkers for several diseases, including cancer. The increase in the expression of these enzymes has been related to greater tumor aggressiveness. MMP-26 is expressed constitutively in the endometrium and some cancer cells of epithelial origin.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!