Relationship of Collagen‐Tailed Acetylcholinesterase with Basal Lamina Components

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Abstract
In view of their supposed localization in extracellular structures, such as basal lamina, the possible interactions of collagen-tailed forms of acetylcholinesterase from Electrophorus and bovine superior cervical ganglion with matrix proteins: laminin, fibronectin and types IV and V collagens were investigated. Using binding and sedimentation assays, with iodinated or non-radioactive matrix proteins, no significant interaction, in conditions of high or low ionic strength was observed. Whether the collagen tail of acetylcholinesterase asymmetric forms possessed an immunological relationship with known collagen types (I, III, IV, V) was examined from mammalian sources. No specific immunoreactivity was found with any of the 32 sera studied, either with the iodinated Electrophorus or with the native bovine enzyme. The collagen-like tail of acetylcholinesterase is clearly distinct from the classical types of collagen and asymmetric forms of the enzyme do not interact specifically with the matrix proteins studied. This does not exclude the possibility of specific interactions with other components, remaining to be identified.