What is laminin alpha 2 chain?
Merosin is an extracellular matrix protein forming the heavy chain of the skeletal muscle basement membrane protein laminin and is important for maintaining the integrity of the sarcolemma.
What is laminin good for?
Laminin supports growth and differentiation of many cell types including epithelial, endothelial, neural, muscle and liver cells. The optimal concentration for cell culture depends on cell type and specific application.
What does laminin connect to?
Function. Laminins form independent networks and are associated with type IV collagen networks via entactin, fibronectin, and perlecan. They also bind to cell membranes through integrin receptors and other plasma membrane molecules, such as the dystroglycan glycoprotein complex and Lutheran blood group glycoprotein.
Is laminin a structural protein?
Laminins are essential for the function of the basement membrane as most null mutations are lethal. Just as collagens, laminins are structural proteins with a helical region formed by heptads.
Is laminin 2 a heterotrimer?
Laminin 2 (merosin) is a heterotrimer composed of laminin α2, laminin β1, and laminin γ1. The mutations occur in the LAMA2 gene on chromosome 6q22–23 coding for the heavy chain of laminin 2, laminin α2.
What is the function of laminin and merosin?
Laminin, alpha 2. Merosin is an extracellular matrix protein forming the heavy chain of the skeletal muscle basement membrane protein laminin and is important for maintaining the integrity of the sarcolemma. From: Fetal and Neonatal Physiology (Fifth Edition), 2017.
What is the function of Alpha 2 merosin in skeletal muscle?
Laminin, Alpha 2 Merosin is an extracellular matrix protein forming the heavy chain of the skeletal muscle basement membrane protein laminin and is important for maintaining the integrity of the sarcolemma. From: Fetal and Neonatal Physiology (Fifth Edition), 2017
What is the pathophysiology of merosin deficiency?
Merosin or α2 -laminin deficiency has been linked to a congenital muscular dystrophy. Mutations in genes for the contractile proteins myosin and tropomyosin have been found to cause central core and nemaline rod diseases, which are characterized by slowly progressive, lifelong muscle weakness.