The matrix metalloproteases and endothelin-1 in infection-associated preterm birth

Nicole S Olgun1, Sandra E Reznik

  • 1Department of Pharmaceutical Sciences, College of Pharmacy and Allied Health Professions, St. John's University, St. Albert Hall G018-B, 8000 Utopia Parkway, Jamaica, NY 11439, USA.

Insights

Preterm birth, a leading cause of infant mortality, is often linked to intrauterine infection. This study explores how matrix metalloproteinases (MMPs) and endothelin-1 (ET-1) may contribute to infection-associated preterm labor.

Area of Science:

  • Obstetrics and Gynecology
  • Molecular Biology
  • Reproductive Science

Background:

  • Preterm birth (PTB) is a major obstetric challenge, accounting for 12-13% of US births and being the primary cause of perinatal mortality.
  • Intrauterine infection is the most common cause of PTB, yet no FDA-approved therapies exist.
  • Matrix metalloproteinases (MMPs) and endothelin-1 (ET-1) are implicated in parturition and infection-associated PTB.

Purpose of the Study:

  • To investigate the role of MMPs and ET-1 in the molecular pathway of infection-associated preterm birth.
  • To understand the pathogenesis of preterm labor (PTL) to identify potential therapeutic targets.

Main Methods:

  • Review of existing evidence linking MMPs and ET-1 to preterm birth.
  • Focus on the molecular pathway shared by MMPs and ET-1 in infection-associated PTL.

Main Results:

  • Evidence suggests MMPs are involved in normal and infection-triggered parturition.
  • Evidence indicates a role for ET-1 in infection-associated preterm delivery.
  • This paper consolidates evidence that MMPs and ET-1 function within the same molecular pathway leading to PTB.

Conclusions:

  • MMPs and ET-1 are key molecular players in infection-associated preterm birth.
  • Understanding this shared pathway is crucial for developing new therapies for PTB.
  • Further research into this pathway could lead to interventions for preventing preterm labor.

Related Concept Videos

Role of Matrix Metalloproteases in Degradation of ECM01:23

Role of Matrix Metalloproteases in Degradation of ECM

Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult body.
A...
Regulation of Angiogenesis and Blood Supply01:24

Regulation of Angiogenesis and Blood Supply

Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits.  Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl hydroxylase and factor...
Overview of Cell-Matrix Interactions01:24

Overview of Cell-Matrix Interactions

The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...