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Imaging Integrin Tension and Cellular Force at Submicron Resolution with an Integrative Tension Sensor
Published on: April 25, 2019
The beta integrins and cytoskeletal nanoimprinting
Mairead A Wood1, Pierre Bagnaninchi, Matthew J Dalby
1Center for Cell Engineering, Division of Infection and Immunity, Joseph Black Building, University of Glasgow, Glasgow, G12 8QQ, UK. m.wood@bio.gla.ac.uk
Experimental Cell Research
|November 21, 2007
Summary
Cellular nanoimprinting, where cells conform to nanotopography, is influenced by integrins. Blocking beta1 integrin enhanced nanoimprinting, while blocking beta3 reduced it, revealing inherent cytoskeletal nanopatterning.
Area of Science:
- Cell Biology
- Biophysics
- Materials Science
Background:
- Nanoimprinting describes topographical features imprinted on cells.
- Integrin-mediated cell-substrate adhesions are crucial for cell-environment signaling.
- Understanding nanoimprinting mechanisms is key to explaining cell behavior alterations.
Purpose of the Study:
- To investigate the role of beta1 and beta3 integrin subunits in cellular nanoimprinting.
- To determine how blocking these integrins affects cytoskeletal conformation to nanotopography.
Main Methods:
- Utilized scanning electron microscopy (SEM) and atomic force microscopy (AFM) to characterize nanofeatures.
- Quantified nanofeature circularity and cytoskeletal patterning on patterned and planar substrates.
- Employed cross-correlation analysis to compare topographical features with cytoskeletal patterns, with and without integrin antibodies.
Main Results:
- Inhibiting beta1 integrin subunits increased fibroblast nanoimprinting.
- Inhibiting beta3 integrin subunits decreased nanoimprinting of topography onto cells.
- Fibroblasts on planar surfaces exhibited inherent cytoskeletal nanopatterning.
Conclusions:
- Beta1 and beta3 integrins differentially regulate cellular response to nanotopography.
- Cellular nanoimprinting is modulated by specific integrin subunits.
- Cells possess intrinsic capabilities for high-resolution cytoskeletal nanopatterning.
Related Concept Videos
01:10Integrins
Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
01:15Activation of Integrins
Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
01:17Intracellular Signaling Affects Focal Adhesions
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Some...
01:03Anchoring Junctions
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:...
01:24Overview of Cell-Matrix Interactions
The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
01:25Fibronectins Connect Cells with ECM
Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...