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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...
Role of Matrix Metalloproteases in Degradation of ECM01:23

Role of Matrix Metalloproteases in Degradation of ECM

Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult body.
A...
Structural Protein Function01:56

Structural Protein Function

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.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Extracellular Matrix01:26

Extracellular Matrix

Unlike epithelial tissue, which is composed of cells closely packed with little or no extracellular space in between, connective tissue cells are dispersed in a matrix. This extracellular matrix (ECM) is composed of fibrous proteins like collagen, elastin, and fibronectin in a ground substance consisting of interstitial fluid, cell adhesion proteins, and proteoglycans. The proteoglycans form a gel-like material in the spaces between cells and provide hydration, buffering, binding, and force...
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...

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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

Lamins in development, tissue maintenance and stress.

Noam Zuela1, Daniel Z Bar, Yosef Gruenbaum

  • 1Department of Genetics, Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem 91904, Israel.

EMBO Reports
|November 14, 2012
PubMed
Summary

Lamins are nuclear proteins essential for cell structure and function. Recent research reveals their diverse roles in development, stress response, and disease, highlighting distinct A- and B-type lamin networks.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Lamins are nuclear intermediate filament proteins crucial for mechanical stability and chromatin organization.
  • They regulate key nuclear processes including transcription, replication, and nuclear positioning.
  • Lamins play vital roles in cellular development, differentiation, and response to various environmental stresses.

Purpose of the Study:

  • To provide new insights into the multifaceted roles of lamins.
  • To explore the functional implications of separate filament networks for A- and B-type lamins.
  • To elucidate the molecular basis of laminopathies and the involvement of lamin B1.

Main Methods:

  • Review of recent studies and experimental findings on lamin function.
  • Analysis of lamin composition changes across different cell types.
  • Investigation of mutations in lamin A and lamin C associated with human diseases.

Main Results:

  • Evidence suggests distinct filament networks for A- and B-type lamins with unique roles.
  • Changes in lamin composition are observed in various cell types.
  • New explanations are proposed for over 14 human diseases linked to lamin A/C mutations, with a potential role for lamin B1.

Conclusions:

  • Lamins are central to nuclear architecture, gene regulation, and cellular integrity.
  • Distinct lamin networks contribute to specialized cellular functions and stress responses.
  • Understanding lamin dynamics and mutations is critical for deciphering laminopathies.