Repair of hair cells following mild trauma may involve extracellular chaperones.
Sea anemones were subjected to mild trauma consisting of a 2 min immersion in calcium-depleted seawater. The trauma caused a loss of vibration sensitivity that spontaneously recovered within 50 min of returning the anemones to calcium containing seawater. Apparently, recovery is conferred by proteins contained in fraction gamma, a chromatographic fraction of homogenized mucus collected at the base of anemones allowed to recover from similar trauma. On silver stained SDS-PAGE gels, fraction gamma consists of a single band having an estimated mass of 55 kDa. Fraction gamma is alone sufficient to repair hair bundle mechanoreceptors in anemones. Its biological activity is enhanced in the presence of exogenously supplied ATP, but not GTP nor ADP-ribose. Biotinylated fraction gamma binds to hair bundles. The hypothesis that fraction gamma consists of Hsp60 proteins was tested. Commercial antibodies to Hsp60 label a band at 55 kDa in western blots. Hsp60 antibodies label hair bundles in traumatized anemones but not in untreated controls. Dilute Hsp60 antiserum (but not nonimmune serum) delays the spontaneous recovery of vibration sensitivity in anemones subjected to mild trauma. Thus, fraction gamma likely consists of Hsp60, or a Hsp60-like protein, that functions on the extracellular face of the plasma membrane to restore function to traumatized hair bundles.
Department of Biology, The University of Louisiana at Lafayette, Lafayette, LA 70504-2451, USA.
Kamalika
K
Nag
Glen M
GM
Watson
D000818:Animals; D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D007150:Immunohistochemistry; D008465:Mechanoreceptors / Q000293:injuries* / Q000502:physiology*; D018832:Molecular Chaperones / Q000737:chemistry / Q000502:physiology*; D012615:Sea Anemones / Q000737:chemistry / Q000502:physiology*; D012623:Seawater; D014732:Vibration
D018832:Molecular Chaperones