Response of stratified cultures of human keratinocytes to disruption of proteoglycan synthesis by p-nitrophenyl-beta-D-xylopyranoside
| Autor: | John G. Haggerty, Leonard M. Milstone, Randolph H. Bretton |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Keratinocytes
Physiology Macromolecular Substances Clinical Biochemistry Perlecan Epithelium Glycosaminoglycan chemistry.chemical_compound Cell–cell interaction medicine Humans Chondroitin sulfate Glycosides Cells Cultured biology Sulfates Chondroitin Sulfates Osmolar Concentration Cell Biology Heparan sulfate Molecular biology Culture Media carbohydrates (lipids) medicine.anatomical_structure Biochemistry Proteoglycan chemistry biology.protein Basal lamina Proteoglycans Heparitin Sulfate Keratinocyte Cell Division Heparan Sulfate Proteoglycans |
| Zdroj: | Journal of cellular physiology. 158(1) |
| ISSN: | 0021-9541 |
| Popis: | Proteoglycans play a role in regulating proliferation and adhesion of cells to each other and to the basal lamina. Synthesis of proteoglycans is disrupted by beta-xylosides, which serve as alternate substrate sites for glycosaminoglycan chain attachment and therefore prevent glycosylation of the core protein. We have investigated the effects of p-nitrophenyl-beta-D-xylopyranoside (PNP-xyloside) on cultured human keratinocytes. Stratified cultures were incubated for 7 days with PNP-xyloside (0.05-2.0 mM). Concentrations as low as 0.05 mM increased the secretion of free chondroitin sulfate by 10-15-fold over untreated cultures. Cell-associated proteoglycan decreased as PNP-xyloside concentration increased. At 2 mM PNP-xyloside, heparan sulfate as well as chondroitin sulfate addition to core proteins was disrupted: the core protein of epican, a heparan sulfate form of CD44 found on keratinocytes, was detected immunologically but lacked heparan sulfate. 2.0 mM PNP-xyloside reduced the number of attached cells by 20-25% after 7 days, but had little effect on morphology or protein synthesis. These results indicate that intact proteoglycans are not critical for maintaining epidermal keratinocyte stratification, cell-cell adhesion, or growth. |
| Databáze: | OpenAIRE |
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