Membrane adhesion and domain formation

نویسندگان

  • Thomas R. Weikl
  • Reinhard Lipowsky
چکیده

2 Modelling of membranes 7 2.1 Homogeneous or uniform membranes . . . . . . . . . . . . . . . . 8 2.1.1 Membrane configurations and effective Hamiltonian . . . 8 2.1.2 Classification of effective membrane potentials . . . . . . 9 2.2 Discretized models for uniform membranes . . . . . . . . . . . . . 10 2.3 Lattice gas models: General form . . . . . . . . . . . . . . . . . . 11 2.4 Membranes with sticker molecules . . . . . . . . . . . . . . . . . 12 2.5 Two types of membrane-anchored molecules . . . . . . . . . . . . 14

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

O 7: KCNK2 Regulates the Nanoscale Formation of Immune Docking Structures on Brain Endothelial Cells Under Autoinflammatory Conditions

KCNK2 was previously shown to regulate immune-cell trafficking into the central nervous system (CNS). Kcnk2-/- mice demonstrated a more severe disease course in experimental autoimmune encephalomyelitis, an animal model of multiple sclerosis, due to an increased immune-cell migration into the CNS. An upregulation of the cellular adhesion molecules ICAM1 and VCAM1 on brain endothelial cells in K...

متن کامل

Line Tension and Stability of Domains in Cell-Adhesion Zones Mediated by Long and Short Receptor-Ligand Complexes

Submicron scale domains of membrane-anchored receptors play an important role in cell signaling. Central questions concern the stability of these microdomains, and the mechanisms leading to the domain formation. In immune-cell adhesion zones, microdomains of short receptor-ligand complexes form next to domains of significantly longer receptor-ligand complexes. The length mismatch between the re...

متن کامل

Segregation of receptor-ligand complexes in cell adhesion zones: Phase diagrams and role of thermal membrane roughness

The adhesion zone of immune cells, the ‘immunological synapse’, exhibits characteristic domains of receptor-ligand complexes. The domain formation is likely caused by a length difference of the receptor-ligand complexes, and has been investigated in experiments in which T cells adhere to supported membranes with anchored ligands. For supported membranes with two types of anchored ligands, MHCp ...

متن کامل

Pathogenic interactions between Helicobacter pylori adhesion protein HopQ and human cell surface adhesion molecules CEACAMs in gastric epithelial cells

Objective(s): The present paper aims to review the studies describing the interactions between HopQ and CEACAMs along with possible mechanisms responsible for pathogenicity of Helicobacter pylori.Materials and Methods: The literature was searched on “PubMed” using different key words including Helicobacter pylori, CEACAM and gastric.<br ...

متن کامل

Repulsion by Slit and Roundabout prevents Shotgun/E-cadherin–mediated cell adhesion during Drosophila heart tube lumen formation

During Drosophila melanogaster heart development, a lumen forms between apical surfaces of contralateral cardioblasts (CBs). We show that Slit and its receptor Roundabout (Robo) are required at CB apical domains for lumen formation. Mislocalization of Slit outside the apical domain causes ectopic lumen formation and the mislocalization of cell junction proteins, E-cadherin (E-Cad) and Enabled, ...

متن کامل

Mesangial cells organize the glomerular capillaries by adhering to the G domain of laminin alpha5 in the glomerular basement membrane

Mesangial cells organize the glomerular capillaries by adhering to the G domain of laminin alpha5 in the glomerular basement membrane. n developing glomeruli, laminin ␣ 5 replaces laminin ␣ 1 in the glomerular basement membrane (GBM) at the capillary loop stage, a transition required for glomerulogenesis. To investigate domain-specific functions of laminin ␣ 5 during glomerulogenesis, we produc...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2007