Differential lectin binding to presumptive cortical cells of the wool follicle bulb
| Autor: | A.E. Dollin, David L. Adelson, M.T. Campbell |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
chemistry.chemical_classification
Sheep biology Wool Cellular differentiation Lectin Cell Biology Cell biology Bulb Microscopy Electron Membrane glycoproteins medicine.anatomical_structure Glycolipid chemistry Biochemistry Lectins biology.protein medicine Extracellular Animals Female Plant Lectins Fibroblast Glycoprotein Skin |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 1477-9137 0021-9533 |
| DOI: | 10.1242/jcs.102.2.353 |
| Popis: | An alpha-D-galactoside-specific lectin from Bandeiraea simplicifolia (BSLI) showed differential binding to cortical cells of the wool follicle bulb. The lectin bound to cells on one side only of the bulb and was completely blocked by alpha-D-galactose. The region of lectin binding extended from presumptive cortical cells at the base of the bulb to cortical cells at the top of the bulb, disappearing as cortical cells entered the fibre cortex. An orthocortex-specific monoclonal antibody was used to show that cortical cells recognised by the lectin lie directly below the fibre orthocortex and presumably give rise to the orthocortex. The results suggest that two distinct populations of presumptive cortical cells are present only two to three cell layers from the base of the bulb in a region where no morphological differences are detectable. The lectin-bound pre-cortical cells appear to give rise to orthocortical cells while cells not bound by lectin presumably give rise to paracortical cells. Electron microscopy showed that the lectin bound to sites on the plasma membrane, probably on the extracellular surface. This suggests that the lectin target may be a membrane glycoprotein or glycolipid. Two polypeptides recognised by BSLI were separated from wool follicle extracts by SDS-gel electrophoresis. These polypeptides migrated at approximately 69 kDa and 17 kDa. However, only the 69 kDa molecule showed the expected loss of binding by BSLI in the presence of alpha-D-galactose. Further work will be required to determine if this glycoprotein is the bulb cell molecule recognised by BSLI.(ABSTRACT TRUNCATED AT 250 WORDS) |
| Databáze: | OpenAIRE |
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