Glycoprotein of the extracellular matrix. Laminins are found in all basal laminae, and have binding sites for cell surface receptors.
Together with collagen type IV and proteoglycans, laminins form the basement membranes.Other important components of the basal lamina are fibronectins, integrins. Laminins connect integrins to the basal lamina in a protein complex. Fibronectin, however, connects integrins with collagen fibers of different types. Types.
15 isoforms of laminin are known so far. These are distributed tissue-specifically in the animal organism. The laminin molecule consists of an alpha-, a beta- and a γ-protein chain, which assemble in heterotrimeric form to the respective laminin molecule. So far, the following combinations of protein chains have been detected in the different isoforms of lamininis:
- Laminin-1: α1β1γ1 (Laminin-111).
- Laminin-2: α2β1γ1 (laminin-211)
- Laminin-3: α1β2γ1 (laminin-121)
- Laminin-4: α2β2γ1 (laminin-221)
- Laminin-5: α3β3γ2 (laminin-332)
- Laminin-6: α3β1γ1 (laminin-311)
- Laminin-7: α3β2γ1 (laminin-321)
- Laminin-8: α4β1γ1 (laminin-411)
- Laminin-9: α4β2γ1 (laminin-421)
- Laminin-10: α5β1γ1 (laminin-511)
- Laminin-11: α5β2γ1 (laminin-521)
- Laminin-12: α2β1γ3 (laminin-231)
- Laminin-13: α3β2γ3 (laminin-323)
- Laminin-14: α4β2γ3 (laminin-423)
- Laminin-15: α5β2γ3 (laminin-523)