LAMB1

Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the beta chain isoform laminin, beta 1. The beta 1 chain has 7 structurally distinct domains which it shares with other beta chain isomers. The C-terminal helical region containing domains I and II are separated by domain alpha, domains III and V contain several EGF-like repeats, and domains IV and VI have a globular conformation. Laminin, beta 1 is expressed in most tissues that produce basement membranes, and is one of the 3 chains constituting laminin 1, the first laminin isolated from Engelbreth-Holm-Swarm (EHS) tumor. A sequence in the beta 1 chain that is involved in cell attachment, chemotaxis, and binding to the laminin receptor was identified and shown to have the capacity to inhibit metastasis.

LAMB1

Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface.

Animal organ morphogenesisManual Assertion Based On ExperimentIBA:GO_Central
Basement membrane assemblyManual Assertion Based On ExperimentIBA:GO_Central
Cell adhesionManual Assertion Based On ExperimentTAS:HGNC-UCL
Cell migrationManual Assertion Based On ExperimentIBA:GO_Central
Endodermal cell differentiationManual Assertion Based On ExperimentIEP:UniProtKB
Neuron projection developmentManual Assertion Based On ExperimentIDA:UniProtKB
Neuronal-glial interaction involved in cerebral cortex radial glia guided migrationManual Assertion Based On ExperimentIMP:UniProtKB
OdontogenesisManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of cell migrationManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of epithelial cell proliferationManual Assertion Based On ExperimentTAS:HGNC-UCL
Substrate adhesion-dependent cell spreadingManual Assertion Based On ExperimentIDA:BHF-UCL
Tissue developmentManual Assertion Based On ExperimentIBA:GO_Central

Secreted, extracellular space, extracellular matrix, basement membrane
Major component.

Lissencephaly 5 (LIS5):
An autosomal recessive brain malformation characterized by cobblestone changes in the cortex, more severe in the posterior region, and subcortical band heterotopia. Affected individuals have hydrocephalus, seizures, and severely delayed psychomotor development.