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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...
Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
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.
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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.
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Basal Lamina are the Specialized Form of ECM01:03

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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...
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Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.

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Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
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Published on: September 28, 2020

Laminin isoforms in development and disease.

Susanne Schéele1, Alexander Nyström, Madeleine Durbeej

  • 1Section for Cell and Matrix Biology, BMC B12, Department of Experimental Medical Science, Lund University, Sölvegatan 19, 22184, Lund, Sweden. susanne.scheele@med.lu.se

Journal of Molecular Medicine (Berlin, Germany)
|April 12, 2007
PubMed
Summary

Laminins are proteins found in basement membranes, which are thin layers of tissue in the body. These proteins help stabilize cells and influence their behavior through signaling. Different types of laminins are linked to specific diseases, like muscular disorders and skin blistering. Recent research has shown how mutations in these proteins can lead to various health problems. Scientists are now exploring new ways to treat these conditions, including stem-cell and gene therapy. This review summarizes the latest findings and suggests future directions for research.

Keywords:
laminin isoformsbasement membranecell signalinglamininopathies

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Area of Science:

  • Extracellular matrix biology
  • Developmental biology
  • Molecular pathology

Background:

Basement membranes are specialized extracellular structures found in nearly all organs. These membranes contain laminin heterotrimers, which are essential for connecting cells to their surrounding matrix. Prior research has shown that laminins stabilize tissues and influence cell signaling. However, the exact mechanisms by which laminins contribute to disease remain unclear. No prior work had fully resolved how specific laminin isoforms affect organ development. This gap motivated recent studies to explore laminin roles in health and disease. Understanding these roles could clarify how basement membranes contribute to pathogenesis. The need for precise knowledge of laminin functions has grown with the rise of targeted therapies. This paper addresses that need by reviewing recent findings on laminin isoforms.

Purpose Of The Study:

This review aims to synthesize recent findings on laminin isoforms and their roles in development and disease. Laminins are known to stabilize tissues and influence cell signaling, but their specific contributions to disease remain unclear. The authors focus on how different laminin isoforms affect organ development and pathology. They also examine how mutations in laminin chains lead to specific disorders. The study seeks to clarify the molecular mechanisms behind these effects. It builds on prior work that identified laminins as key basement membrane components. The goal is to inform future clinical approaches to laminin-related disorders. This work may guide the development of stem-cell and gene therapy strategies.

Main Methods:

The authors conducted a literature review to examine recent studies on laminin isoforms. They analyzed how different laminin chains interact with cell surface receptors. The review includes findings from both developmental and pathological contexts. They compared how specific laminin mutations lead to distinct diseases. The approach integrates data from multiple disciplines including cell biology and genetics. The authors synthesized evidence from animal models and human studies. They focused on molecular mechanisms rather than broad overviews. The review highlights gaps in current knowledge and suggests future research directions.

Main Results:

The strongest finding is that laminin isoforms govern cell fate through intracellular signaling. Different laminin chains are associated with distinct diseases, such as muscular disorders and kidney defects. The review shows that laminin mutations disrupt basement membrane stability. Laminins also serve as physical barriers, preventing tumor metastasis. The authors report that microbes and viruses exploit laminin interactions to enter cells. Specific isoforms, like laminin-α2, are linked to muscular dystrophy. Laminin-β3 mutations are tied to skin blistering. These findings suggest that isoform-specific therapies could be developed.

Conclusions:

The authors conclude that laminin isoforms play critical roles in both development and disease. Their findings suggest that isoform-specific mutations lead to distinct pathologies. The review proposes that understanding these mechanisms could lead to new treatments. They highlight the potential of stem-cell and gene therapy approaches. The authors emphasize the need for further research into laminin signaling pathways. They also suggest that targeting specific isoforms may improve clinical outcomes. The synthesis of current knowledge provides a foundation for future studies. These conclusions align with the evidence presented in the literature review.

Laminin isoforms stabilize cellular structures and govern cell fate through intracellular signaling.

Mutations in specific laminin chains cause muscular disorders, skin blistering, and kidney defects.

Different isoforms are linked to distinct diseases, suggesting isoform-specific therapies could be developed.

Laminins act as physical barriers, and tumors must pass through them to reach the vascular system.

Microbes and viruses enter cells by directly interacting with laminin isoforms on the cell surface.

The authors propose stem-cell and gene therapy as potential treatments for laminin-related disorders.