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The interactions between the COOH terminus of the adhesion protein L1 and the N terminus of L1 may provide a molecular basis for the directionality of cell-cell adhesion. The interactions are hypothesized to involve the amino acid sequence of the COOH-terminal 16 residues of L1 and the amino acids Pro-Ile-Val-Pro-Asp-Val of L1. The peptide hormone relaxin is known to accelerate cell-cell adhesion in rat myometrium by a mechanism that also involves interactions between the N-terminal and COOH-terminal portions of L1. Relaxin was used as a model to test the possible interaction between the COOH-terminal portion of L1 and the N terminus of L1. The peptide did not cause a direct interaction between the COOH-terminal portion of L1 and the N terminus of L1. The first six residues of the N terminus of L1 are critical for the relaxation-induced cell-cell adhesion. Thus, while the COOH-terminal portion of L1 can interact with the N terminus of L1, other regions of L1 must be involved in the interaction.
174 B.R. 46 (1994)
In re Larry E. HALL, Debtor.
Larry E. HALL, Plaintiff,
v.
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