laminin111

Laminin-111, also known as laminin-1, is a heterotrimeric extracellular matrix glycoprotein belonging to the laminin family. It is composed of α1, β1, and γ1 chains (encoded by LAMA1, LAMB1, LAMC1). The molecule forms a cross-shaped structure and participates in basement membrane networks through interactions among LN domains that drive polymerization.

During development, laminin-111 is a prominent component of basement membranes in early embryos and is involved in cell adhesion, migration, survival, and differentiation. It binds to cell surface receptors, notably integrins such as α6β1 and α7β1 and to dystroglycan, mediating stable adhesion and signaling. In tissue morphogenesis, laminin-111 collaborates with other ECM components such as collagen IV, nidogen, and perlecan to form a cohesive basement membrane.

Expression is downregulated as tissues mature, with other laminin isoforms taking precedence in many organs. Genetic disruption of Lama1 in mice results in severe developmental defects and often embryonic lethality, underscoring its essential role.

In research and biotechnology, laminin-111 is widely used as a substrate for cell culture and as a component of basement membrane extracts (e.g., Matrigel contains laminin-111).