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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...
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.
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...
Basal Lamina are the Specialized Form of ECM01:03

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The Sarcomere01:08

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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

Laminin-211 in skeletal muscle function.

Johan Holmberg1, Madeleine Durbeej

  • 1Muscle Biology Unit, Department of Experimental Medical Science, Lund University, Lund, Sweden. johan_k.holmberg@med.lu.se

Cell Adhesion & Migration
|November 17, 2012
PubMed
Summary

This review explores how laminin-211 contributes to skeletal muscle function. Skeletal muscle relies on a network of proteins to transmit force and withstand stress. Laminin-211 is a key component of the extracellular matrix that supports muscle fiber stability. The review suggests that laminin-211 interacts with other proteins to maintain muscle structure and function. Deficiencies in laminin-211 are linked to muscular dystrophy. The authors propose that laminin-211 is particularly important for skeletal muscle compared to other laminin isoforms. This review synthesizes evidence on laminin-211's role in muscle physiology and disease.

Keywords:
laminin-211 rolemuscle extracellular matrixmuscular dystrophy causesskeletal muscle proteins

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Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
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Identification of Skeletal Muscle Satellite Cells by Immunofluorescence with Pax7 and Laminin Antibodies
07:18

Identification of Skeletal Muscle Satellite Cells by Immunofluorescence with Pax7 and Laminin Antibodies

Published on: April 19, 2018

Area of Science:

  • Muscle physiology
  • Extracellular matrix biology
  • Molecular pathology

Background:

Skeletal muscle function depends on structural integrity between muscle fibers and their surrounding matrix. Prior research has shown that disruptions in this connection lead to muscular dystrophies. It was already known that laminins, a family of extracellular matrix proteins, play roles in cell adhesion and survival. However, the specific role of laminin-211 in muscle remains unclear. This gap motivated a need to explore laminin-211's contribution to muscle health. No prior work had resolved how laminin-211 differs from other laminin isoforms in function. Understanding this could clarify mechanisms of muscle stability. This review addresses the current state of knowledge on laminin-211's role in muscle physiology.

Purpose Of The Study:

This review aims to evaluate the role of laminin-211 in skeletal muscle function. The specific problem is to determine how laminin-211 contributes to muscle fiber stability. The motivation stems from the high prevalence of muscular dystrophies linked to matrix disruptions. The authors propose to synthesize evidence on laminin-211's involvement in muscle. They suggest that laminin-211 may be particularly important for force transmission. The review also seeks to clarify how laminin-211 interacts with other matrix components. This could help distinguish laminin-211's role from other laminin isoforms. The study aims to inform future research on muscle disease mechanisms.

Main Methods:

The authors conducted a literature review focusing on laminin-211 and skeletal muscle. They analyzed studies on laminin isoforms and their roles in muscle. The review included data from animal models and human disease studies. They examined how laminin-211 interacts with muscle fiber cytoskeleton. The approach involved comparing laminin-211 to other laminin isoforms. The authors synthesized findings on laminin-211's structural and functional roles. They also considered how laminin-211 affects muscle fiber survival and adhesion. The review approach included evaluating clinical implications of laminin-211 deficiency.

Main Results:

Laminin-211 is a major component of the muscle basement membrane. It interacts with dystroglycan and integrins to stabilize muscle fibers. Studies suggest laminin-211 is necessary for proper force transmission. Deficiencies in laminin-211 are linked to muscular dystrophy in animal models. The protein supports adhesion between muscle fibers and surrounding matrix. It also contributes to muscle fiber survival during contraction. Laminin-211 appears to be more abundant in skeletal muscle than other isoforms. These findings suggest laminin-211 plays a unique role in muscle physiology.

Conclusions:

The authors propose that laminin-211 is essential for skeletal muscle function. They suggest that laminin-211 supports structural integrity of muscle fibers. The review highlights laminin-211's role in force transmission and adhesion. It may also contribute to muscle fiber survival during stress. The findings suggest laminin-211 is more specific to skeletal muscle than other isoforms. The authors propose that disruptions in laminin-211 may lead to muscular dystrophy. They suggest further study is needed to clarify these mechanisms. These conclusions are based on synthesized evidence from the literature.

Laminin-211 interacts with dystroglycan and integrins to stabilize muscle fibers and transmit force.

Laminin-211 is more abundant in skeletal muscle and supports adhesion and survival during contraction.

This interaction allows muscle fibers to transmit force and withstand contraction-induced stress.

The basement membrane, including laminin-211, provides structural support and signaling for muscle fibers.

Deficiencies in laminin-211 are linked to muscular dystrophy in animal models.

The authors propose that laminin-211 is essential for skeletal muscle function and stability.