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The effect of retinoic acid on collagen synthesis by human dermal fibroblasts
Abstract:
The effect of all-trans retinoic acid (RA) on cell proliferation and protein synthesis was examined using neonatal human dermal fibroblasts in culture. Incorporation of [3H]-methylthymidine showed that cell proliferation decreased in response to increasing concentrations of RA. Analysis of proteins secreted into culture medium showed a decrease in the synthesis of both collagen and non-collagenous proteins, paralleling the effect on cell proliferation. Secreted proteins showed increased enzymatic processing of type I procollagen. The enhanced appearance of pc collagens, intermediates in the enzymatic conversion of procollagen to collagen, indicated that retinoic acid increased the activity of procollagen aminoterminal protease. Electrophoretic mobility and mannosylation of fibronectin was unchanged at RA concentrations tested. Cell morphology was unchanged at all concentrations of retinoic acid. The inhibitory effect of RA on cell proliferation is consistent with previous observations. The enhanced activity of procollagen aminoterminal protease may be important in the overall influence of RA on the elaboration of connective tissue.
Insights
All-trans retinoic acid (RA) inhibits neonatal human dermal fibroblast proliferation and reduces collagen and non-collagenous protein synthesis. RA also enhances procollagen processing, impacting connective tissue elaboration.
Area of Science:
- Dermatology
- Cell Biology
- Biochemistry
Background:
- Neonatal human dermal fibroblasts are a key model for studying skin connective tissue.
- All-trans retinoic acid (RA) is known to influence cell behavior and differentiation.
- Understanding RA's effects on fibroblast function is crucial for skin biology.
Purpose of the Study:
- To investigate the impact of all-trans retinoic acid (RA) on neonatal human dermal fibroblast proliferation.
- To analyze the effects of RA on the synthesis and processing of secreted proteins, including collagen.
- To elucidate the specific mechanisms by which RA influences connective tissue elaboration.
Main Methods:
- Cell culture of neonatal human dermal fibroblasts.
- Measurement of cell proliferation using [3H]-methylthymidine incorporation.
- Analysis of secreted proteins via electrophoresis and other biochemical assays.
- Assessment of procollagen processing and enzyme activity.
Main Results:
- RA significantly decreased fibroblast cell proliferation in a dose-dependent manner.
- RA reduced the synthesis of both collagen and non-collagenous proteins.
- RA treatment increased the enzymatic processing of type I procollagen, indicating enhanced procollagen aminoterminal protease activity.
- Fibronectin electrophoretic mobility and mannosylation remained unchanged; cell morphology was unaffected.
Conclusions:
- All-trans retinoic acid (RA) inhibits human dermal fibroblast proliferation and protein synthesis.
- RA enhances the activity of enzymes involved in collagen processing, suggesting a role in connective tissue remodeling.
- The findings highlight RA's complex influence on skin connective tissue metabolism.