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Integrins01:10

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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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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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Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
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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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The alpha4beta1 integrin in sickle cell disease.

J E Brittain1, L V Parise

  • 1Department of Biochemistry and Biophysics, School of Medicine, University of North Carolina at Chapel Hill, CB 7260, Chapel Hill, NC 27599, USA.

Transfusion Clinique Et Biologique : Journal De La Societe Francaise De Transfusion Sanguine
|May 27, 2008
PubMed
Summary
This summary is machine-generated.

Alpha4beta1 integrin on sickle reticulocytes drives cell adhesion in sickle cell disease (SCD). Targeting this integrin offers new therapeutic strategies to prevent vaso-occlusion.

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Area of Science:

  • Hematology
  • Cell Biology
  • Immunology

Background:

  • Alpha4beta1 integrin is an adhesion receptor found on reticulocytes.
  • In sickle cell disease (SCD), this integrin mediates reticulocyte adhesion to the endothelium and matrix proteins.
  • This adhesion contributes to vaso-occlusion, a hallmark of SCD.

Purpose of the Study:

  • To review the activation mechanisms of alpha4beta1 integrin on sickle reticulocytes.
  • To discuss the novel roles of activated alpha4beta1 integrin in SCD pathogenesis.
  • To highlight potential therapeutic strategies targeting alpha4beta1 integrin for SCD.

Main Methods:

  • Literature review of studies on alpha4beta1 integrin in SCD.
  • Analysis of mechanisms underlying integrin activation on sickle reticulocytes.
  • Evaluation of existing and emerging therapies targeting alpha4beta1 integrin.

Main Results:

  • Alpha4beta1 integrin activation on sickle reticulocytes is a key event in SCD.
  • Activated alpha4beta1 integrin plays multifaceted roles in SCD pathophysiology beyond simple adhesion.
  • Targeting alpha4beta1 integrin presents a promising avenue for novel SCD treatments.

Conclusions:

  • Understanding alpha4beta1 integrin activation is crucial for comprehending SCD.
  • Novel therapies targeting alpha4beta1 integrin hold potential to alleviate vaso-occlusive crises in SCD.
  • Further research into alpha4beta1 integrin modulation could lead to improved SCD management.