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Related Concept Videos

Caspases01:24

Caspases

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Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside...
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Complement System01:27

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The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a...
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Complementation Tests00:49

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A complementation test is a simple cross to identify whether the two mutations are located on the same gene or different genes. It was first performed by Edward Lewis in the 1940s while working on fruit flies. He developed the test to identify the location and arrangement of different mutations on chromosomes.
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Most plants use the C3 pathway for carbon fixation. However, some plants, such as sugar cane, corn, and cacti that grow in hot conditions, use alternative pathways to fix carbon and conserve energy loss due to photorespiration. Photorespiration is the process that occurs when the oxygen concentration is high. Under such conditions, the rubisco enzyme in the Calvin cycle binds O2 instead of CO2, which halts photosynthesis and consumes energy.
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Light Acquisition02:16

Light Acquisition

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In order to produce glucose, plants need to capture sufficient light energy. Many modern plants have evolved leaves specialized for light acquisition. Leaves can be only millimeters in width or tens of meters wide, depending on the environment. Due to competition for sunlight, evolution has driven the evolution of increasingly larger leaves and taller plants, to avoid shading by their neighbors with contaminant elaboration of root architecture and mechanisms to transport water and nutrients.
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Light as Energy01:35

Light as Energy

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The energy required to carry out photosynthesis is light— typically electromagnetic radiation from the sun. The range of all possible wavelengths is known as the electromagnetic spectrum.
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Updated: Feb 13, 2026

Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation
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Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation

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Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation.

Chloé I Charendoff1, Lisa Bouchier-Hayes2

  • 1Department of Pediatrics, Division of Hematology-Oncology, Baylor College of Medicine.

Journal of Visualized Experiments : Jove
|March 20, 2018
PubMed
Summary
This summary is machine-generated.

Caspase Bimolecular Fluorescence Complementation (BiFC) visualizes initiator caspase activation. This imaging technique quantifies caspase recruitment to activation platforms, offering insights into apoptosis and innate immunity pathways.

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Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation
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Bimolecular Fluorescence Complementation
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Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP
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Area of Science:

  • Molecular biology
  • Cellular biology
  • Immunology

Background:

  • Initiator caspases are crucial proteases in apoptosis and innate immunity.
  • These caspases (e.g., caspase-1, -2, -8, -9) activate via dimerization on specific protein complexes.
  • Understanding early activation steps is key to studying these vital cellular processes.

Purpose of the Study:

  • To introduce and validate Caspase Bimolecular Fluorescence Complementation (BiFC) as a method.
  • To visualize and quantify the recruitment of initiator caspases to their activation platforms.
  • To provide a sensitive readout of early caspase activation events.

Main Methods:

  • Utilizing split fluorescent proteins fused to initiator caspases.
  • Employing microscopy-based approaches to detect fluorescence complementation.
  • Analyzing fluorescence to assess caspase recruitment and complex formation.

Main Results:

  • Caspase BiFC successfully visualizes initiator caspase recruitment and induced proximity.
  • The technique provides quantitative data on activation efficiency at the population level.
  • Microscopy allows for per-cell analysis of kinetics, complex size, and number.

Conclusions:

  • Caspase BiFC is a powerful imaging tool for studying initiator caspase activation.
  • This method offers detailed insights into the early molecular events of apoptosis and immunity.
  • BiFC enables quantitative analysis of caspase activation dynamics in living cells.