LAMA2
Domain
The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domains VI, IV and G are globular.
Function
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.
Involvement in disease
Merosin-deficient congenital muscular dystrophy 1A
MDC1A
Characterized by difficulty walking, hypotonia, proximal weakness, hyporeflexia, and white matter hypodensity on MRI.
None
The disease is caused by variants affecting the gene represented in this entry.
Muscular dystrophy, limb-girdle, autosomal recessive 23
LGMDR23
A form of autosomal recessive limb-girdle muscular dystrophy, a myopathy characterized by proximal and/or distal muscle weakness and atrophy. The age at onset is variable and can range from the first to the sixth decade, although later onset is less common. LGMDR23 is characterized by slowly progressive proximal muscle weakness primarily affecting the lower limbs, increased serum creatine kinase, dystrophic features, gait difficulties, and white matter abnormalities on brain imaging. Age at onset generally ranges from childhood to mid-adulthood. Some patients may have additional neurologic features, including executive deficits, seizures, and peripheral neuropathy.
None
The disease is caused by variants affecting the gene represented in this entry.
Tissue Specificity
Placenta, striated muscle, peripheral nerve, cardiac muscle, pancreas, lung, spleen, kidney, adrenal gland, skin, testis, meninges, choroid plexus, and some other regions of the brain; not in liver, thymus and bone.
Cellular localization
- Secreted
- Extracellular space
- Extracellular matrix
- Basement membrane
- Major component.
Alternative names
LAMM, LAMA2, Laminin subunit alpha-2, Laminin M chain, Laminin-12 subunit alpha, Laminin-2 subunit alpha, Laminin-4 subunit alpha, Merosin heavy chain