Hyaluronic Acid-Receptor Binding Demonstrated by Synthetic Adhesive Proteoglycan Peptide Constructs and by Cell Receptors on the Marine Sponge Microciona prolifera

• Published in: The Biological bulletin (Lancaster) Vol. 195; no. 2; pp. 216 - 218
• Main Authors: Kuhns, W. J., Fernandez-Busquets, X., Burger, M. M., Ho, M., Turley, E.
• Format: Journal Article
• Language: English
• Published: United States Marine Biological Laboratory 01.10.1998; University of Chicago Press
• Subjects: Adhesives; Amino Acid Sequence; Animals; Antibodies; Aquatic life; Basic amino acids; Biotin - chemistry; Cell Adhesion Molecules - chemistry; Cell Adhesion Molecules - metabolism; Cell aggregation; Cell and Developmental Biology; Cell membranes; Cell receptors; Cellular biology; Cellular signal transduction; Dyes; Hyaluronan Receptors - chemistry; Hyaluronan Receptors - immunology; Hyaluronan Receptors - metabolism; Hyaluronic acid; Hyaluronic Acid - immunology; Hyaluronic Acid - metabolism; Immunoblotting; Immunohistochemistry; Invertebrates; Ligand binding (Biochemistry); Ligands; Marine; Mice; Microciona prolifera; Nerves; Peptides; Peptides - chemical synthesis; Peptides - immunology; Peptides - metabolism; Physiological aspects; Porifera - immunology; Porifera - metabolism; Porifera - physiology; Proteoglycans; Proteoglycans - chemistry; Proteoglycans - metabolism; Reagents; Receptors; Signal Transduction; Sponges; Sponges (Animals)
• ISSN: 0006-3185; 1939-8697
• DOI: 10.2307/1542847

A study was undertaken to determine the functions of the hyaluronic acid (HA) and the receptor for HA mediated motility (RHAMM) on the ligand binding to the Microciona sponge aggregation factor (MAF) and on cellular signal transduction. HA was known to be present on MAF core peptide and the cell membrane. Results revealed that the MAF HA binding sequence, in combination with the RHAMM on cell membranes, acted as anchorage terminals for HA molecules and produced a conduit for signal transduction that specify motility.