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Matrix Metallopeptidase 9 Promotes Contraction in Human Uterine Myometrium.
Reprod Sci
January 2025
Department of Pharmacology, University of Nevada, Reno School of Medicine, 1664 North Virginia St., Reno, NV, 89557, USA.
Matrix metallopeptidase 9 (MMP9) is a secreted zinc-dependent peptidase known for extracellular remodeling. MMP9 is elevated in tissues from women experiencing preterm labor, and previous research has shown that the addition of combined matrix metallopeptidases 2 and 9 (MMP2/9) enhances uterine contractions. We hypothesized that adding MMP9 alone would enhance myometrial contractions and that specific MMP9 inhibition would suppress uterine contractions.
View Article and Find Full Text PDFStructural characterization of pyruvic oxime dioxygenase, a key enzyme in heterotrophic nitrification.
J Bacteriol
January 2025
Department of Environment and Energy Systems, Graduate School of Science and Technology, Shizuoka University, Shizuoka, Japan.
Nitrification by heterotrophic microorganisms is an important part of the nitrogen cycle in the environment. The enzyme responsible for the core function of heterotrophic nitrification is pyruvic oxime dioxygenase (POD). POD is a non-heme, Fe(II)-dependent enzyme that catalyzes the dioxygenation of pyruvic oxime to produce pyruvate and nitrite.
View Article and Find Full Text PDFEffects of Zinc-Biofortified Wheat Intake on Plasma Markers of Fatty Acid Metabolism and Oxidative Stress Among Adolescents.
Nutrients
December 2024
Department of Nutrition, University of California, Davis, CA 95616, USA.
Background/objective: Zinc deficiency is common worldwide and has been linked to reduced growth and immune function, increased risk of and slower recovery from infections, and increased risk of non-communicable diseases. To address the issue, zinc biofortification of wheat has been proposed as a sustainable approach to increase dietary zinc intake in countries like Pakistan, where zinc deficiency rates are high and wheat is the primary staple crop. Since plasma zinc concentration (PZC) does not reliably respond to small changes in zinc intake, biomarkers sensitive to small changes in zinc intake achievable though biofortification are needed.
View Article and Find Full Text PDFThe Complex Role of Matrix Metalloproteinase-2 (MMP-2) in Health and Disease.
Int J Mol Sci
December 2024
Pittsburgh Heart, Lung and Blood Vascular Medicine Institute (VMI), University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.
Matrix metalloproteinase-2 (MMP-2), a zinc-dependent enzyme, plays a critical role in the degradation and remodeling of the extracellular matrix (ECM). As a member of the gelatinase subgroup of matrix metalloproteinases, MMP-2 is involved in a variety of physiological processes, including tissue repair, wound healing, angiogenesis, and embryogenesis. It is primarily responsible for the degradation of type IV and V collagen, fibronectin, laminin, and elastin, which are essential components of the ECM.
View Article and Find Full Text PDFAlzheimer's Disease: In Vitro and In Vivo Evidence of Activation of the Plasma Bradykinin-Forming Cascade and Implications for Therapy.
Cells
December 2024
Astria Pharmaceuticals, Boston, MA 02210, USA.
The plaques associated with Alzheimer's disease are formed as a result of the aggregation of Aβ peptides, which vary in length from 38 to 43 amino acids. The 1-40 peptide is the most abundant, while the 1-42 peptide appears to be the most destructive to neurons and/or glial cells in a variety of assays. We have demonstrated that aggregated Aβ, a state prior to plaque formation, will activate the plasma bradykinin-forming pathway when tested in vitro.
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