Related Experiment Video

Updated: Jan 5, 2026

Real-Time Measurement of the Mitochondrial Bioenergetic Profile of Neutrophils
09:39

Real-Time Measurement of the Mitochondrial Bioenergetic Profile of Neutrophils

Published on: June 2, 2023

2.4K

Microbes mediate mitochondrial misinformation to misguide neutrophils

Mausita Karmakar1, George R Dubyak1

  • 1Department of Physiology & Biophysics, Case Western Reserve University, School of Medicine, Cleveland, Ohio, USA.

Journal of Leukocyte Biology
|October 22, 2019
PubMed

Insights

Lipopolysaccharide (LPS) disrupts neutrophil mitochondrial localization and purinergic signaling, impairing E. coli infection control. This affects immune cell function and bacterial clearance mechanisms.

Area of Science:

  • Immunology
  • Cell Biology
  • Microbiology

Background:

  • Neutrophils are crucial immune cells for combating bacterial infections like E. coli.
  • Chemotaxis, the directed movement of neutrophils, is essential for effective infection control.
  • Mitochondrial localization and purinergic signaling play roles in neutrophil function.

Discussion:

  • Lipopolysaccharide (LPS) from Gram-negative bacteria disrupts normal neutrophil mitochondrial localization.
  • This disruption interferes with autocrine purinergic signaling pathways.
  • Impaired signaling affects neutrophil chemotaxis and their ability to clear E. coli infections.

Key Insights:

  • LPS directly impacts neutrophil organelle positioning critical for function.
  • Autocrine purinergic signaling is a key mediator affected by LPS.
  • Neutrophil dysfunction under LPS influence compromises host defense against E. coli.

Outlook:

  • Understanding LPS-induced neutrophil defects can inform therapeutic strategies.
  • Targeting mitochondrial localization or purinergic signaling may enhance anti-bacterial immunity.
  • Further research into neutrophil-host-pathogen interactions is warranted.

More Related Videos

Author Spotlight: Two-Step Tag-Free Isolation of Mitochondria for Improved Protein Discovery and Quantification09:04

Author Spotlight: Two-Step Tag-Free Isolation of Mitochondria for Improved Protein Discovery and Quantification

Published on: June 2, 2023

7.6K
Morphological and Compositional Analysis of Neutrophil Extracellular Traps Induced by Microbial and Chemical Stimuli14:05

Morphological and Compositional Analysis of Neutrophil Extracellular Traps Induced by Microbial and Chemical Stimuli

Published on: November 4, 2022

3.0K

Related Concept Videos

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,...
11.8K
The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
4.4K
Mitochondrial Membranes01:45

Mitochondrial Membranes

A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
16.5K
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

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...
5.5K
Animal Mitochondrial Genetics02:59

Animal Mitochondrial Genetics

Among all the organelles in an animal cell, only mitochondria have their own independent genomes. Animal mitochondrial DNA is a double-stranded, closed-circular molecule with around 20,000 base pairs. Mitochondrial DNA is unique in that one of its two strands, the heavy, or H, -strand is guanine rich, whereas the complementary strand is cytosine rich and called the light, or L, -strand. Compared to nuclear DNA, mitochondrial DNA has a very low percentage of non-coding regions and is marked by...
8.9K
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
4.4K