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>Response of stratified cultures of human keratinocytes to disruption of proteoglycan synthesis byp‐nitrophenyl‐β‐D‐xylopyranoside
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Response of stratified cultures of human keratinocytes to disruption of proteoglycan synthesis byp‐nitrophenyl‐β‐D‐xylopyranoside
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机译：Response of stratified cultures of human keratinocytes to disruption of proteoglycan synthesis byp‐nitrophenyl‐β‐D‐xylopyranoside
AbstractProteoglycans play a role in regulating proliferation and adhesion of cells to each other and to the basal lamina. Synthesis of proteoglycans is disrupted by β‐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‐β‐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. Cellassociated 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
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