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Related Concept Videos

Septins01:19

Septins

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Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
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Role of Septins01:02

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Septins are the recently discovered fourth major protein component of the cytoskeleton, along with microfilaments, microtubules, and intermediate filaments. These proteins can associate with other cytoskeletal filaments and carry out varied roles or can be free-floating in the cytoplasm.
Cellular Functions of Septins
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Structure and Function of Platelets01:18

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The cell fragments known as platelets are disc-shaped, with an average diameter of about 3 μm and a thickness of roughly 1 μm. They play a crucial role in the body's vascular clotting system, which also involves plasma proteins, blood cells, and blood vessel tissues.
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The platelet phase, the second stage of hemostasis, commences around 15-20 seconds after an injury. It follows and overlaps with the vascular phase, during which blood vessels constrict to minimize blood loss.
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Structural Protein Function01:56

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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Intracellular Signaling Affects Focal Adhesions01:17

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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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Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
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Contribution of septins to human platelet structure and function.

Oleg V Kim1, Rustem I Litvinov1, Elmira R Mordakhanova2

  • 1Department of Cell and Developmental Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.

Iscience
|July 14, 2022
PubMed
Summary

Septins play a crucial role in human platelet structure and function. This study reveals septin involvement in platelet shape, activation, and biomechanics, highlighting their importance in blood clotting.

Keywords:
Biological sciencesCell biologyFunctional aspects of cell biologyIntegrative aspects of cell biology

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Area of Science:

  • Cell Biology
  • Hematology
  • Biochemistry

Background:

  • Septins are a conserved family of GTPases essential for various cellular functions in nucleated cells.
  • The role of septins in anucleate blood platelets, critical for hemostasis, has remained largely unexplored.

Purpose of the Study:

  • To investigate the contribution of septins to the structural integrity and functional capabilities of human platelets.
  • To elucidate the localization and dynamics of septins within platelets and their interaction with the cytoskeleton.

Main Methods:

  • Immunofluorescence microscopy to visualize septin distribution and co-localization with microtubules.
  • Platelet activation assays using thrombin stimulation.
  • Pharmacological inhibition of septin dynamics using forchlorfenuron (FCF).
  • Assessment of platelet shape changes, integrin activation, phosphatidylserine exposure, and P-selectin expression.
  • Measurement of platelet contractility and spreading on fibrinogen-coated surfaces.

Main Results:

  • Septin-2 and Septin-9 are localized at the platelet periphery, co-localizing with microtubules in resting platelets.
  • Platelet activation leads to septin clustering and reduced association with microtubules.
  • Inhibition of septin dynamics with FCF alters platelet shape, suggesting a role in cytoskeletal stabilization.
  • FCF treatment suppresses integrin αIIbβ3 activation, promotes phosphatidylserine exposure, and induces P-selectin expression.
  • Septin inhibition significantly reduces platelet contractility and abrogates spreading on fibrinogen.

Conclusions:

  • Septins are integral components of the human platelet cytoskeleton, influencing structural stability.
  • Septin dynamics are critical for proper platelet activation, shape change, and adhesive functions.
  • Targeting septin dynamics represents a potential strategy for modulating platelet activity in thrombosis and hemostasis.