Laminin
[1][2] Laminins are heterotrimeric proteins with a high molecular mass (~400 to ~900 kDa) and possess three different chains (α, β, and γ) encoded by five, four, and three paralogous genes in humans, respectively.The trimeric proteins intersect, composing a cruciform structure that is able to bind to other molecules of the extracellular matrix and cell membrane.[11] Laminin alpha4 is distributed in a variety of tissues, including peripheral nerves, dorsal root ganglion, skeletal muscle, and capillaries; in the neuromuscular junction, it is required for synaptic specialisation.[citation needed] Laminins are enriched at the lesion site after peripheral nerve injury and are secreted by Schwann cells.Neurons of the peripheral nervous system express integrin receptors that attach to laminins and promote neuroregeneration after injury.Abnormal laminin-332, essential for epithelial cell adhesion to the basement membrane, leads to junctional epidermolysis bullosa, characterized by generalized blisters, exuberant granulation tissue of the skin and mucosa, and pitted teeth.The majority of transcripts that harbor an internal ribosome entry site (IRES) are involved in cancer development via corresponding proteins.A crucial event in tumor progression, referred to as the epithelial-to-mesenchymal transition (EMT) allows carcinoma cells to acquire invasive properties.Furthermore, no other LamB1 mRNA species arising from alternative transcription start sites or polyadenylation signals were detected that account for its translational control.[17] The various laminin isoforms are practically impossible to isolate from tissues in pure form due to extensive cross-linking and the need for harsh extraction conditions, such as proteolytic enzymes or low pH, that cause degradation.Beside different types of globular domains each laminin subunit contains, in its first half, consecutive repeats of about 60 amino acids in length that include eight conserved cysteines.
familyglycoproteinsextracellular matrixbasement membranebasal laminacell differentiationmigrationadhesionheterotrimericmolecular massparalogousin vivomuscular dystrophyjunctional epidermolysis bullosanephrotic syndromeisoformLaminin-111type IV collagenentactinfibronectinperlecanintegrinsplasma membranedystroglycanpeptidetissuesperipheral nervesdorsal root ganglionskeletal muscleneuromuscularsynapticstructurepentraxinretinal ganglion cellsretinatectumSchwann cellsperipheral nervous systemneuroregenerationcongenital muscular dystrophyalpha-dystroglycanintegrin alpha7cancerinternal ribosome entry siteepithelial-to-mesenchymal transitioncollagenscell culturestem cellsrecombinantInterProPDBsumPROSITEconservedprotein domainstrimerdomainscoiled-coilextracellularproteinsheparan sulphateproteoglycanCaenorhabditis elegansrepeatsamino acidscysteinesN-terminusEGF-like modulenidogenbasement membranescollagenC-terminalbinding sitessulphatidescell surface receptorcell adhesionsignallingdifferentiationpolymeriseNetrinscell signallinggeneticsubunitsCELSR1CELSR2CELSR3CRELD1CRELD2MEGF10CNTNAP1CNTNAP2CNTNAP4COL5A1COL5A3COL9A1COL11A1COL11A2COL12A1COL14A1COL15A1COL16A1COL18A1COL19A1COL20A1COL21A1COL22A1COL24A1COL27A1EGFLAMSubstrate adhesion moleculesLaminin databaseList of target antigens in pemphigoidBibcodeEuropean Bioinformatics InstituteMedical Subject HeadingsUniProtPDBe-KBProteinscleroproteinstype ICOL1A1COL1A2type IICOL2A1type IIItype VCOL5A2