Lc3-ii Cleavage
Lc3-ii Cleavage - Related Videos
01:33
Cleavage and Blastulation
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2019
After a large-single-celled zygote is produced via fertilization, the process of cleavage occurs while zygotes travel through the uterine tube. Cleavage is a mitotic cell division that does not result in growth. With each round of successive cell division, daughter cells get increasingly smaller. Zygotic Genome Activation At the beginning of embryogenesis, maternal mRNAs control development. However, by the eight-cell stage of cleavage, embryonic genes become activated in a process called...
11:39
Assessing Autophagic Flux by Measuring LC3, p62, and LAMP1 Co-localization Using Multispectral Imaging Flow Cytometry
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Cited by 94 •
2017
Here, multispectral imaging flow cytometry with an analytical feature that compares bright detail images of 3 autophagy markers and quantifies their co-localization, along with LC3 spot counting, was used to measure autophagy in an objective, quantitative, and statistically robust manner.
07:33
Physical Properties Of Minerals I: Crystals and Cleavage
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2023
Source: Laboratory of Alan Lester - University of Colorado Boulder The physical properties of minerals comprise various measurable and discernible attributes, including color, streak, magnetic properties, hardness, crystal growth form, and crystal cleavage. Each of these properties are mineral-specific, and they are fundamentally related to a particular mineral’s chemical make-up and atomic structure. This experiment examines two properties that stem primarily from symmetric repetition of...
06:58
Evaluation of LC3-II Release via Extracellular Vesicles in Relation to the Accumulation of Intracellular LC3-positive Vesicles
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Cited by 7 •
2024
Here, we present the methodology for concisely assessing autophagosome marker LC3-II levels in extracellular vesicles (EVs) by immunoblotting. Analysis for LC3-II levels in EVs, autolysosome formation, and omegasome formation suggests the new role of STX6 in the release of LC3-II-positive EVs when autophagosome-lysosome fusion is inhibited.
02:42
A Fluorogenic Peptide Cleavage Assay to Screen the Proteolytic Activity of Proteases
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2025
This video demonstrates an assay to screen for the proteolytic activity of proteases using fluorogenic peptides. The protease recognizes its cleavage site on the peptide, cleaving it and separating the quencher from the fluorophore, enabling its fluorescence emission. The fluorescence signal is detected and analyzed to check for the cleavage efficiency of different peptide variants.
FAQs
These processes act in opposite directions within LC3 processing. Lipidation converts LC3-I into membrane-associated LC3-II, whereas ATG4-mediated cleavage removes LC3-II from phosphatidylethanolamine and releases LC3-I. Keeping the reactions distinct is essential when interpreting whether an observed change reflects LC3 attachment to autophagosomes or removal and recycling from their membranes.
ATG4 cleaves the amide bond that anchors LC3-II to phosphatidylethanolamine, converting the membrane-associated form into soluble LC3-I. This recycling step regulates the available LC3 pool for continued autophagy-related processing. Consequently, altered cleavage can affect how LC3 abundance is interpreted during studies of autophagosome formation and turnover.
LC3-II represents the lipid-conjugated, membrane-associated form, while LC3-I is soluble after release by cleavage. Comparing these forms provides mechanistic context for LC3 processing rather than treating total LC3 abundance as a single readout. This distinction helps connect molecular measurements with membrane remodeling during autophagy.
LC3-II cleavage should be examined together with LC3 abundance, autophagosome formation, and lysosomal inhibition. This combined approach helps distinguish changes in processing from changes in autophagosome production or lysosomal handling. Measuring cleavage alone therefore provides a narrower view, while the broader set of observations supports a more informative assessment of autophagic flux.
In immunology and infection studies, the analysis can clarify how immune cells regulate intracellular pathogens through autophagy-related pathways. Examining LC3 processing alongside autophagosome formation and lysosomal inhibition helps relate molecular changes to host-cell responses. This makes the approach relevant to investigations of intracellular pathogen control and host defense.
The measurement can help researchers examine whether microbes alter autophagy-related pathways in infected cells. Interpreted with LC3 abundance, autophagosome formation, and lysosomal inhibition, cleavage data can contribute to studies of pathogen-associated changes in host processing. These findings may also inform research on inflammation and therapeutic strategies targeting autophagy-related responses.