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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.
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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
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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.
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Multiple non-catalytic ADAMs are novel integrin α4 ligands.

Lei Wang1, Jason A Hoggard1, Erica D Korleski1

  • 1Department of Biochemistry and Molecular Biology, The Brody School of Medicine, East Carolina University, Greenville, NC, 27834, USA.

Molecular and Cellular Biochemistry
|September 16, 2017
PubMed
Summary

Catalytically inactive ADAM proteins function as ligands, supporting cell adhesion through integrin interactions. This study reveals novel adhesive roles for non-catalytic ADAMs, expanding our understanding of ADAM-integrin signaling.

Keywords:
ADAMCell adhesionDisintegrinIntegrinLymphocyte

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • The ADAM (a disintegrin and metalloprotease) protein family possesses both catalytic and adhesive functions.
  • ADAMs are crucial for ectodomain shedding, regulating various biological processes, but their integrin ligand properties are less understood.
  • A subset of human ADAMs (8 of 21) are catalytically inactive, and their roles as integrin ligands are largely unexplored.

Purpose of the Study:

  • To investigate the integrin ligand properties of catalytically inactive ADAM proteins.
  • To determine if non-catalytic ADAMs can mediate cell adhesion via integrin interactions.

Main Methods:

  • Investigated the adhesive capabilities of specific catalytically inactive ADAM proteins.
  • Utilized cell adhesion assays to assess interactions with integrin receptors.

Main Results:

  • Human ADAM11, ADAM23, and ADAM29 were identified as selective ligands for integrin α4.
  • Demonstrated that the disintegrin-like domains of these inactive ADAMs support integrin-dependent cell adhesion.
  • This represents the first report of multiple catalytically inactive ADAMs acting as ligands for specific integrins.

Conclusions:

  • Catalytically inactive ADAMs possess functional integrin ligand properties.
  • These findings expand the known roles of ADAM proteins beyond ectodomain shedding.
  • The study highlights a novel mechanism of cell adhesion mediated by non-catalytic ADAM-integrin interactions.