These high molecular mass proteins play several vital roles.
Laminin is a protein that is a significant component, with basement membrane collagen separating connective tissue and stromal cells from epithelial tissues (lining of the mucosa or organs).
In the case of pathology, muscular dystrophies, neurological disorders (poor myelination of the nerves), and skin or mucous membrane disorders can be observed.
Laminins are a significant component of the basal lamina ECM protein.
In general, laminins are heterotrimeric glycoproteins with binding regions for collagen, integrins, cellular domains, and proteoglycans such as dystroglycan.
It also joins itself to form leaves in the basal lamina.
Laminins are composed of a central alpha chain of approximately 400 kDa with a variable number of spherical regions and two chains of about 200 kDa (beta and gamma) with a-helical and globular helical regions.
Cysteine-rich repeats are prevalent in all laminin chains.
Basement membranes are sheet-like extracellular matrix structures that are the basis for cells to grow.
The composition of the basement membrane is highly selective for the cell surface, and laminins are the essential proteins that surround virtually all cells.
Laminins are essential for embryogenesis, and in the adult body, expression is tissue-specific.
Many binding sites on the full-length laminin molecule can interact with receptors on the cell membrane.
Integrins are essential laminin receptors, and the laminin-integrin interaction triggers vital intracellular signaling pathways.
Laminins regulate cellular responses by binding to specific cell receptors, such as cell anchoring, survival, proliferation, migration, organization, and specialization, leading to improved cell functionality.
Without the correct combination of laminin isoforms, cells and tissues become dysfunctional.
There are 15 different laminins, each consisting of a unique combination of three substrings.
The combination of chains confers some tissue specificity.
Laminins are essential for basement membrane function as most null mutations are lethal.
Like collagens, laminins are structural proteins with a helical region of heptads.
Heptad has a less strict organization than collagens, where the helical domain consists of a rigid building block of three amino acids.
Laminins play a central role in organizing complex basement membrane interactions.
This is seen through the wide range of interaction partners such as syndecan, nidogen, collagen, integrins, dystroglycan, and heparin.
Mutations in different laminin chains are associated with diseases such as Alport syndrome, epidermolysis bullosa, and muscular dystrophies.
The laminin family is significant, and biomarkers are emerging to measure laminins.
The essential role of laminins in the basement membrane can be summarized as follows: even the most unique construction will not last on a poor foundation.
Only full-length and intact lamina molecules can replicate the relevant biological conditions.
Laminins are multidomain, heterotrimeric glycoproteins composed of three subunits; an α chain, β chain, and γ chain.
The assembled laminin molecule forms a cross-type structure.
There are at least 16 distinct isoforms identified in mammals, and their names are derived from their combination of subunits. Therefore the laminin 521 isoform has an alpha-5 / beta-2 / gamma-1 chain composition.
The molecular mechanism underlying laminin-mediated signaling has been suggested to involve the C-terminal region of laminins. Still, integrins and other cellular receptors also interact with some of the N-terminal globular domains.
Biolaminin Biolaminin substrates are the only original full-length recombinant laminins on the market.
A fractionated or truncated laminin molecule, or laminins isolated from tissue, lacks many of the laminin domains that cells need to form the proper extracellular network and stimulate correct cellular signal transductions.
Therefore, only full-length, intact laminin can create a more authentic cell culture environment.
Laminins are a major component of the basement membrane, an intricate network of proteins separating the epithelium, mesothelium, and endothelium from connective tissue.
Laminin is a protein that shares several properties with fibronectin.
For example, it also has a high molecular weight. Laminin protein consists of three subunits, including α, β, and γ chains.
Laminins are also considered glycoproteins since they are functionalized with oligosaccharides.
In the extracellular matrix, laminin can bind to other laminin molecules and other proteins such as collagen, helping to strengthen the structure of the extracellular matrix.
Cells can also bind to laminin through the integrin receptors that they express on their cell membranes.
These properties make laminins attractive as cell culture substrates for both pluripotent stem cells and neuronal cells.
Protocols to differentiate stem cells into mature phenotypes will often require culture on laminin 2D substrates.
Laminin also plays a vital role in developing the nervous system as axons tend to migrate onto this protein, making it attractive for regenerative medicine applications.
Finally, laminin is found in the neural stem cell niche, where it contributes its growth factor-binding properties to specialized structures known as fractons.
Laminins, the first detectable extracellular matrix glycoproteins in the embryo, are found in the basement membrane.
Laminin protein is detected in the infarct area on the third day after myocardial infarction; the concentration peaks on days 7-11 and returns to baseline levels.
The extensive existence of laminins throughout the infarct area suggests that they may directly regulate left ventricular repair after myocardial infarction.
In patients with acute myocardial infarction, the serum laminin level is higher than in those with stable coronary artery disease and those without coronary artery disease.