Suppression of membrane vesiculation as anticoagulant and anti-metastatic mechanism. Role of stability of narrow necks

Gen Physiol Biophys. 2013 Mar;32(1):33-45. doi: 10.4149/gpb_2013007.


Nanovesicles that are pinched off from biological membranes in the final stage of budding constitute a cell-cell communication system. Recent studies indicate that in vivo they are involved in blood clot formation and in cancer progression. The bud is connected to the mother membrane by a thin neck so it dwells close to the mother membrane. Using the electron microscopy we have observed in blood cells that adhesion between the membrane of the bud and of the mother cell in the vicinity of the neck took place and prevented the bud to pinch off from the mother vesicle. The same effect was observed in giant phospholipid vesicles (GPVs) due to attractive interaction between the bud and the mother vesicle mediated by the plasma protein beta-2-glycoprotein I. The stability of the neck is important for this process. By using Fourier method we analyzed thermal fluctuations of a GPV while a protrusion composed of beads connected by thin necks was spontaneously integrated into the mother GPV. Stepwise change of Fourier coefficients indicates an increased stability of necks which contributes to the retention of buds by the mother membrane and promotes anticoagulant and anti-metastatic mechanism by suppression of nanovesiculation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anticoagulants / pharmacology*
  • Antineoplastic Agents / pharmacology*
  • Cell Communication
  • Disease Progression
  • Fourier Analysis
  • Humans
  • Image Processing, Computer-Assisted
  • Ionophores / pharmacology
  • Microscopy, Electron, Scanning
  • Microscopy, Electron, Transmission
  • Models, Statistical
  • Neoplasms / drug therapy*
  • Neoplasms / pathology
  • Phospholipids / chemistry
  • Thrombosis / drug therapy
  • Time Factors
  • Vacuoles
  • beta 2-Glycoprotein I / metabolism


  • Anticoagulants
  • Antineoplastic Agents
  • Ionophores
  • Phospholipids
  • beta 2-Glycoprotein I