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Related Concept Videos

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Tension Response at Adherens Junctions

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The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
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Elastic fiber contains the protein elastin along with lesser amounts of other proteins and glycoproteins. The main property of elastin is that it will return to its original shape after being stretched or compressed. Elastic fibers are prominent in elastic tissues found in skin and the elastic ligaments of the vertebral column.
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Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
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In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue. 
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Adherens Junctions

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Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
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Catenins01:23

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Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
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Production of Elastin-like Protein Hydrogels for Encapsulation and Immunostaining of Cells in 3D
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Catechol-Functionalized Elastin-like Polypeptides as Tissue Adhesives.

Malav S Desai1,2,3, Min Chen4, Farn Hing Julio Hong1

  • 1Department of Bioengineering, University of California, Berkeley, Berkeley, California 94720, United States.

Biomacromolecules
|June 2, 2020
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel hydrogel adhesive using engineered proteins (Cat-ELPs) for effective wound closure. This bioadhesive demonstrates strong bonding on wet surfaces and excellent biocompatibility, offering a promising solution for medical applications.

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Area of Science:

  • Biomaterials Science
  • Polymer Chemistry
  • Tissue Engineering

Background:

  • Current wound closure adhesives face challenges with wet surface adhesion, swelling, and biocompatibility.
  • Recombinant elastin-like polypeptides (ELPs) offer customizable protein platforms for biomedical applications.

Purpose of the Study:

  • To design and characterize a novel hydrogel bioadhesive with enhanced properties for wound closure.
  • To evaluate the bonding strength, biocompatibility, and biodegradation of the developed hydrogel adhesive.

Main Methods:

  • Chemically modifying ELPs with dopamine to create catechol-functionalized ELPs (Cat-ELPs).
  • Characterizing hydrogel properties (flexibility, viscoelasticity, swelling) using rheology.
  • Assessing fibroblast binding, in vivo biocompatibility, and biodegradation in mice.
  • Evaluating adhesive bonding strength on porcine skin using tensile pull-off and lap-shear tests.

Main Results:

  • Cat-ELP hydrogels exhibited stable swelling at 37 °C and demonstrated flexibility and viscoelasticity.
  • Incorporation of RGD peptides into Cat-ELPs improved fibroblast binding, enhancing biological properties.
  • In vivo studies confirmed the biocompatibility and biodegradation of Cat-ELP hydrogels over 10 weeks.
  • Adhesives achieved significant bonding strengths of 37 kPa (tensile) and 39 kPa (lap-shear) on porcine skin.

Conclusions:

  • The developed Cat-ELP hydrogel adhesive shows promise for fast and efficient wound closure due to its strong bonding and biocompatibility.
  • The strategy of combining recombinant protein engineering with chemical modification provides a pathway for creating advanced bioadhesives.