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Related Concept Videos

Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
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Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
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Intralumenal Vesicles and Multivesicular Bodies01:38

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Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
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Post-translational Translocation of Proteins to the RER01:27

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
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Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
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Sequential Release of Proteins from Structured Multishell Microcapsules.

Ulyana Shimanovich1,2, Thomas C T Michaels1,3, Erwin De Genst1

  • 1Department of Chemistry, University of Cambridge , Lensfield Road, Cambridge CB2 1EW, United Kingdom.

Biomacromolecules
|August 10, 2017
PubMed
Summary
This summary is machine-generated.

Researchers created novel multiprotein microcapsules using self-assembly and microfluidics. These advanced biomaterials enable controlled, sequential release of functional proteins for diverse applications.

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Area of Science:

  • Biomaterials Science
  • Protein Engineering
  • Nanotechnology

Background:

  • Natural functional materials often utilize multicomponent proteins organized on the micrometer scale.
  • Current artificial protein biomaterials are typically single-component, limiting their complexity and applications.
  • Mimicking nature's multicomponent protein structures is a significant challenge in materials science.

Purpose of the Study:

  • To fabricate multicomponent protein microcapsules with controlled component positioning.
  • To develop a method for creating complex, multi-protein structures analogous to natural biomaterials.
  • To demonstrate tailored, sequential protein release from these engineered microcapsules.

Main Methods:

  • Utilized molecular self-assembly for nanoscale component organization.
  • Employed droplet microfluidics to assemble components on the micrometer scale.
  • Synthesized microcapsules using glucagon, insulin, and lysozyme, with fluorophore labeling for localization analysis via confocal microscopy.

Main Results:

  • Successfully fabricated multiprotein microcapsules with distinct protein components precisely localized.
  • Demonstrated controlled, sequential release of encapsulated proteins.
  • Identified protein release mechanisms governed by mass transport kinetics and shell dissolution.

Conclusions:

  • Developed a versatile method for creating complex, artificial multicomponent protein materials.
  • These protein microcapsules offer enhanced potential for applications in molecular medicine and materials science.
  • The findings pave the way for designing sophisticated, functional protein delivery systems.