Related Experiment Video
Updated: Jun 21, 2025
08:45
Quantitating Iron Transport Across the Mouse Placenta In Vivo Using Nonradioactive Iron Isotopes
Published on: May 10, 2022
2.0K
Meconium Proteins Involved in Iron Metabolism
Ewa Skarżyńska1, Artur Jakimiuk2,3, Tadeusz Issat4
1Department of Laboratory Medicine, Medical University of Warsaw, 02-097 Warsaw, Poland.
International Journal of Molecular Sciences
|July 13, 2024
Summary
Investigating fetal iron regulation, this study analyzed proteins in meconium. High ferritin levels suggest fetal iron demand, while protein correlations hint at intrauterine iron transport and immune roles.
Area of Science:
- Perinatal Medicine
- Biochemistry
- Neonatology
Background:
- Understanding intrauterine iron supply regulation is limited by a lack of specific biomarkers.
- Meconium, a neonatal waste product, offers a unique window into fetal development and physiological processes.
Purpose of the Study:
- To investigate the roles of key iron-related and inflammatory proteins in fetal development by quantifying their concentrations in meconium.
- To explore potential biomarkers for intrauterine iron regulation and fetal iron status.
Main Methods:
- Enzyme-linked immunosorbent assay (ELISA) was used to measure concentrations of ferritin, transferrin, haptoglobin, ceruloplasmin, lactoferrin, myeloperoxidase (MPO), neutrophil gelatinase-associated lipocalin (NGAL), and calprotectin.
- Meconium samples were collected from 122 neonates.
Main Results:
- Strong correlations were observed between meconium concentrations of haptoglobin, transferrin, and NGAL (p < 0.05).
- Meconium ferritin concentrations were significantly higher than other measured proteins, with calprotectin also found in high concentrations.
- Ceruloplasmin concentrations correlated with MPO, NGAL, lactoferrin, and calprotectin, suggesting potential roles in regulating neutrophil activity.
Conclusions:
- Correlations among haptoglobin, transferrin, and NGAL in meconium suggest their collaborative role in intrauterine iron storage and transport.
- Elevated meconium ferritin may indicate fetal iron demand and utilization.
- Associations between ceruloplasmin and neutrophil proteins point to ceruloplasmin's involvement in intrauterine immune regulation.
Related Concept Videos
01:28The Early Endosome: Endocytosis of Transferrin
3.3K
Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
3.3K
01:22Lifecycle of Erythrocytes
1.9K
Erythrocytes, also known as red blood cells, constantly move through blood capillaries. As a result, they damage their plasma membrane due to the continuous friction. Typically, after 100 to 120 days, erythrocytes become rigid and fragile as they wear out. As they pass through small vessels in the spleen and liver, they can get trapped and break apart into fragments.
The resident phagocytic macrophages deal with these damaged cells by engulfing them and separating their globin and heme groups....
The resident phagocytic macrophages deal with these damaged cells by engulfing them and separating their globin and heme groups....
1.9K
01:15Transcytosis of IgG
2.7K
Transcytosis is the process in which molecules are internalized by endocytosis, transported across the cell, and released through exocytosis from the opposite end of the cell. Molecules such as insulin, immunoglobulins, and certain nutrients are transferred through the recycling endosomes by recycling and transcytosis.
IgG molecules from a mother undergo transcytosis starting around 13 weeks of gestation. The amount of IgG transferred and entering the fetal blood circulation increases with...
IgG molecules from a mother undergo transcytosis starting around 13 weeks of gestation. The amount of IgG transferred and entering the fetal blood circulation increases with...
2.7K
01:21Structure of Porins
2.9K
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
2.9K
01:19Translocation of Proteins into the Mitochondria
3.1K
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,...
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,...
3.1K
01:39Mitochondrial Protein Sorting
4.3K
Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death. Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
4.3K