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Related Concept Videos

Laminins are the Adhesive Proteins of Basal Lamina00:55

Laminins are the Adhesive Proteins of Basal Lamina

Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
Basal Lamina are the Specialized Form of ECM01:03

Basal Lamina are the Specialized Form of ECM

The basal lamina is a thin extracellular layer that lies underneath the cells and separates them from other tissues. The three layers of the basal lamina are lamina lucida, lamina densa and lamina reticularis. The basal lamina, a mixture of glycoproteins and collagen, provides an attachment site for the epithelium, separating it from underlying connective tissue. The framework of basal lamina has other essential proteins such as laminins mesh, perlecan, entactin, and type IV collagen.
Proteins...
Anchoring Junctions01:03

Anchoring Junctions

Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can exist in...
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
Integrins01:10

Integrins

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.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...

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Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
06:56

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells

Published on: September 28, 2020

Laminins in basement membrane assembly.

Erhard Hohenester1, Peter D Yurchenco

  • 1Imperial College London, London, UK. e.hohenester@imperial.ac.uk

Cell Adhesion & Migration
|October 19, 2012
PubMed
Summary
This summary is machine-generated.

Basement membranes form crucial networks essential for embryonic development. Laminins and type IV collagen self-assemble into interconnected structures, anchoring cells and ensuring tissue integrity.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Developmental Biology

Background:

  • Basement membranes are essential extracellular matrix structures.
  • Heterotrimeric laminins are key components, self-assembling into a cell-associated network.
  • This network requires specific laminin chain combinations (α, β, γ) for node formation.

Purpose of the Study:

  • To describe the self-assembly and structural organization of basement membranes.
  • To elucidate the interactions between laminins, proteoglycans, and type IV collagen.
  • To highlight the importance of basement membrane maturation in embryonic development.

Main Methods:

  • Molecular self-assembly principles.
  • Analysis of protein-protein interactions.
  • Structural biology of extracellular matrix components.

Main Results:

  • Laminin molecules form a network via their short arms, with globular domains binding cellular receptors.
  • Proteoglycans (perlecan, agrin) provide collateral anchorage to the laminin network.
  • Type IV collagen forms a second network, interacting with the laminin network via perlecan and agrin heparan sulfate chains and nidogen linkage.

Conclusions:

  • Basement membrane assembly involves intricate self-assembly of laminins and type IV collagen.
  • Proteoglycans and nidogen play critical roles in stabilizing and interconnecting these networks.
  • The mature basement membrane structure is vital for later stages of embryonic development.