Laminin: Difference between revisions

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'''Laminin''' is an important protein found in the [[extracellular matrix]], the sheets of protein that form the substrate of all internal organs also called the [[basement membrane]]. It has four arms that can bind to four other molecules. The three shorter arms are particularly good at binding to other laminin molecules, which allows them to form a flexible woven sheet. The long arm is capable of binding to cells, which helps anchor the actual organs to the membrane.
{{DISPLAYTITLE:Laminin}}


The laminin protein is made up of three separate parts, called the A, B1, and B2 chains. This gives the large protein molecule a total of six "ends", which each can bind to a specific type of molecule. The three shorter arms each form a coil with another laminin molecule, forming a network of protein that can stretch and bend. The long arm can bind to a cell, linking the cell to the extracellular matrix, and thus to other cells.
== Overview ==
[[File:Laminin111.png|thumb|right|Diagram of Laminin structure]]
'''Laminin''' is a crucial protein in the [[extracellular matrix]] (ECM) and plays a significant role in the structural scaffolding of tissues. It is a high-molecular-weight protein of the [[glycoprotein]] family and is an integral part of the [[basement membrane]] in almost every animal tissue.


Laminin and other ECM proteins are secreted and incorporated into cell-associated extracellular matrices. Laminin is vital for the maintenance and survival of tissues. Defective laminins can cause muscles to form improperly, leading to a form of muscular dystrophy, lethal skin blistering disease ([[Junctional epidermolysis bullosa]]) and defects of the kidney filter ([[Nephrotic syndrome]]).
== Structure ==
Laminin is a heterotrimeric protein composed of three different polypeptide chains: _ (alpha), _ (beta), and _ (gamma). These chains are linked together to form a cross-like structure, which is essential for its function in the ECM. The specific combination of these chains determines the type of laminin, such as laminin-111, laminin-211, etc.


==Structure==
== Function ==
Laminins are high-molecular weight (~400 to ~900 kDa) proteins of the extracellular matrix. They are a major component of the basal lamina (one of the layers of the basement membrane), a protein network foundation for most cells and organs. The laminins are an important and biologically active part of the basal lamina, influencing cell differentiation, migration, and adhesion.
Laminin plays a vital role in cell adhesion, differentiation, migration, and phenotype stability. It interacts with other ECM components like [[collagen]], [[nidogen]], and [[perlecan]], as well as with cell surface receptors such as [[integrins]] and [[dystroglycan]]. These interactions are crucial for maintaining the structural integrity of tissues and for signaling pathways that regulate cell behavior.


==Function==
== Role in Development ==
Laminins are cell-adhesive glycoproteins that can create a scaffold for cells, allowing them to move and grow. They also play a crucial role in cell survival, proliferation and differentiation. Laminins are vital for the formation and function of the basement membrane and function in the [[cell adhesion]], growth, migration, and differentiation of cells.
During [[embryogenesis]], laminin is essential for the formation of the [[basement membrane]], which provides a substrate for cell attachment and migration. It is involved in the development of various tissues, including the [[nervous system]], [[muscle]], and [[epithelial]] tissues.


==Clinical significance==
== Clinical Significance ==
Mutations in laminin genes are associated with congenital muscular dystrophy, junctional epidermolysis bullosa, laryngoonychocutaneous syndrome, and Pierson syndrome. Laminins are being researched for their use in regenerative medicine, especially in relation with diseases affecting muscle tissue.
Mutations in laminin genes can lead to a variety of diseases, such as [[muscular dystrophy]], [[epidermolysis bullosa]], and [[Pierson syndrome]]. These conditions often result from the disruption of the basement membrane, leading to compromised tissue integrity and function.


==See also==
== Related Pages ==
* [[Extracellular matrix]]
* [[Extracellular matrix]]
* [[Basement membrane]]
* [[Basement membrane]]
* [[Cell adhesion]]
* [[Integrin]]
* [[Collagen]]
* [[Muscular dystrophy]]
* [[Muscular dystrophy]]
* [[Junctional epidermolysis bullosa]]
* [[Nephrotic syndrome]]


[[Category:Glycoproteins]]
[[Category:Proteins]]
[[Category:Extracellular matrix]]
[[Category:Extracellular matrix]]
[[Category:Cell adhesion molecules]]
{{stub}}

Latest revision as of 03:52, 13 February 2025


Overview[edit]

Diagram of Laminin structure

Laminin is a crucial protein in the extracellular matrix (ECM) and plays a significant role in the structural scaffolding of tissues. It is a high-molecular-weight protein of the glycoprotein family and is an integral part of the basement membrane in almost every animal tissue.

Structure[edit]

Laminin is a heterotrimeric protein composed of three different polypeptide chains: _ (alpha), _ (beta), and _ (gamma). These chains are linked together to form a cross-like structure, which is essential for its function in the ECM. The specific combination of these chains determines the type of laminin, such as laminin-111, laminin-211, etc.

Function[edit]

Laminin plays a vital role in cell adhesion, differentiation, migration, and phenotype stability. It interacts with other ECM components like collagen, nidogen, and perlecan, as well as with cell surface receptors such as integrins and dystroglycan. These interactions are crucial for maintaining the structural integrity of tissues and for signaling pathways that regulate cell behavior.

Role in Development[edit]

During embryogenesis, laminin is essential for the formation of the basement membrane, which provides a substrate for cell attachment and migration. It is involved in the development of various tissues, including the nervous system, muscle, and epithelial tissues.

Clinical Significance[edit]

Mutations in laminin genes can lead to a variety of diseases, such as muscular dystrophy, epidermolysis bullosa, and Pierson syndrome. These conditions often result from the disruption of the basement membrane, leading to compromised tissue integrity and function.

Related Pages[edit]