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. Author manuscript; available in PMC: 2010 Nov 11.
Published in final edited form as: Curr Pharm Des. 2009;15(12):1277–1294. doi: 10.2174/138161209787846766

Table 1.

Basement Membrane Anchoring and Receptor Interactions

Receptor/Anchor Ligands Nature of Interaction References
Integrin α1β1 Col-I, Col-IV, α1-laminins (α1LN) and α2-laminins (α2LN). [173, 174]
Integrin α2β1 Col-I, Col-IV, α2-laminin LN domains, Perlecan LG domains (endorepellin) [156, 173, 175]
Integrin α3β1 α3- and α5-laminins, nidogens. KD: α5-laminin (3.4 nM*) and α3-Lm (14 nM*); Nidogen-2 > Nidogen-1. [28, 138]
Integrin α6β1 α1-, α3-, α5-laminins. The integrin interacts with LG domains 1–3 & the distal coiled-coil. KD: α5-Lms (0.73 nM*) > α3-Lms (7.5 nM*) ≈ α1-Lms (9.5 nM*) ≫ α4-Lms; α2- and α4-laminin interaction detected by cell adhesion only. [28, 176]
Integrin α6β4 α3- and α5-laminins. Mediates attachment to hemidesmosomes. α3-Lms (12 nM*) > α5-Lms (25 nM*) (LG1–3 domains). [28]
Integrin α7X1β1 α2-laminins (0.6 nM) > α5-Lms (1.2 nM*) (LG1–3/distal coiled-coil) Integrin expressed in muscle, peripheral nerve and other tissues. [28]
Integrin α7X2β1 α1- and α2-laminins. KD: α1-Lms ( 1 nM*) > α2-Lms (2.6 nM*) [28]
Integrin αvβ3/β1 α5-Lms (domain L4b) Possible role in vasculature [177]
α-dystroglycan (αDG) α1-, α2-, α5-laminins, agrin, perlecan. αDG binding is dependent upon O-linked carbohydrate. Reduced/absent DG binding adversely affects only some (e.g. muscle and brain) tissues. KD (muscle agrin) = 2 nM; perlecan-LG= 16 nM; α1-Lm ≈ 20 nM; α2-Lm = 43 nM; α5-Lm = 150 nM; α4-Lm4 ≥ 1 μM (activity resides in LG domains). [152, 178–184]
heparin/heparan sulfates of various cellular proteoglycans Laminins (LG and αLN domains), collagen-IV, agrin (LG), perlecan (LG) Heparan sulfate chains tether growth factors (e.g. FGF-2, TGFβ family members). [30, 31, 141, 185, 186]
galactosyl sulfatide (and related sulfated glycolipids) Laminin-, agrin-, perlecan-LG domains; laminin-LN domains. These glycolipids, expressed in Schwann cell, kidney and other tissues, are thought to mediate and/or enhance anchorage of laminins. The LN interactions may enable the short arms to bind the cell surface in addition to the LG domains.

  1. LG domains: KD agrin (15 nM), perlecan (20–30 nM); α2-Lms (LG4–5 = 6 nM); α1-Lms (LG4–5 = 65 nM); α4-Lms (LG1–3 & 4–5 = 50 & 100 nM); α5-Lms (LG1–3 & 4–5 = 80 & 20 nM).

  2. LN domains: Lmα2 (20 nM); Lmα1 (40 nM) Lmα3B (50 nM); Lmα5 (70 nM).

 [17, 27, 30, 31, 181, 182, 184, 187–192]; Capizzi & Yurchenco, unpublished data (agrin and charge-density effects)
galectins Laminin-111 and other ECM molecules May contribute to cell adhesion and signaling. [193]
receptor tyrosine kinase discoidin-domain receptor-1 (DDR1) Collagens (including collagen-IV) Absence of receptor associated with GBM thickening and hearing loss. [194, 195, 196]
CD44 (chondroitin sulfate PG) Collagen-IV May contribute to cell adhesion. [197]
Extracellular β1,4-gal-transferase Laminin-111 and other ligands May contribute to cell adhesion and signaling. [198]
*

detected in solid-phase binding assay with soluble clasped integrins in 1 mM Mn++.