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To identify the specific amino acid sequence within human transforming growth factor-beta 1 responsible for stimulating chemotactic cell migration.

Identification of a chemotactic epitope in human transforming growth factor‐β1 spanning amino acid residues 368–374

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To identify the specific amino acid sequence within human transforming growth factor-beta 1 responsible for stimulating chemotactic cell migration.
Synthesized oligopeptides representing the 12.1 kDa monomer amino acid sequence of human TGF-beta 1.
Assayed chemotactic migration in human peripheral blood neutrophils, monocytes, THP-1 monocyte leukemia cells, and infant foreskin fibroblasts.
Evaluated competitive binding of the synthetic peptides against radiolabeled [125I]hrTGF-beta 1 at TGF-beta cell surface receptors on fibroblasts and THP-1 cells.
A seven-residue peptide containing amino acids 368–374 (Val-Tyr-Tyr-Val-Gly-Arg-Lys), as well as larger carboxy-terminal peptides containing this sequence, stimulated chemotactic migration in neutrophils, monocytes, THP-1 cells, and fibroblasts.
None of the synthetic TGF-beta 1 peptides competed with radiolabeled TGF-beta 1 for binding to TGF-beta cell surface receptors on fibroblasts or THP-1 cells.

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In vitro study demonstrates cell migration induction by a human TGF-beta 1 peptide, suggesting a distinct receptor mechanism for recruitment.

Postlethwaite et al. (1995) studied this question.

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In vitro study demonstrates cell migration induction by a human TGF-beta 1 peptide, suggesting a distinct receptor mechanism for recruitment.