Lectin-binding properties of the Merkel cell and other root sheath cells in perinatal rat vibrissae.
Surface carbohydrates on the Merkel cell of the outer root sheath (ORS) were investigated in 1- to 4-day-old rat vibrissae by use of rhodamine isothiocyanate (RITC)-conjugated lectins. The red fluorescence of RITC provided a convenient assay for lectin binding to the Merkel cell, which is itself identified by its green fluorescence following selective uptake of the dye quinacrine. In monolayers or suspensions of freshly dissociated ORS cells, the Merkel cell showed high affinity for the alpha-fucose-specific lectin, Ulex europeus agglutinin I (UEA-I), thus revealing a novel feature for a basally located cell. Other high-affinity lectins included concanavalin A (Con A), wheat germ agglutinin (WGA), soybean agglutinin (SBA), and Ricinus communis agglutinin I (RCA-I). In contrast, Dolichos biflorus (DBA), Bandeiraea simplicifolia I and II (BS-I and BS-II), and peanut agglutinin (PNA) virtually excluded the Merkel cell, though PNA-binding sites were unmasked after neuraminidase treatment. Other dispersed ORS cells had varying lectin affinities, and generally binding was inhibited by a competing haptenic sugar. The pattern of lectin binding seen in cryostat and paraffin sections of the vibrissa suggested that the Merkel cells share surface properties with their neighboring basal and/or spinous cells; however, unshared properties are likely to exist since ingrowing mechanosensory nerves recognize the Merkel cells, and not other epidermal cells, as their targets.
D000818:Animals; D000831:Animals, Newborn; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D006197:Hair / Q000166:cytology / Q000378:metabolism; D066298:In Vitro Techniques; D037102:Lectins; D009439:Neuraminidase; D011796:Quinacrine; D051381:Rats; D011919:Rats, Inbred Strains; D012867:Skin / Q000166:cytology / Q000378:metabolism*
D037102:Lectins; D009439:Neuraminidase; D011796:Quinacrine