1. Introductory sentence explaining the topic area
2. Main aim and hypothesis being tested
3. General methods used
4. Results obtained
5. Conclusion
Provide a short written comment that describes the strengths and weaknesses of each abstract.
Osteogenesis Imperfecta (OI) is characterized by brittle bones caused by defective collagen. The most common cause is a mutation in the COL1A1 or COL1A2 genes coding for the α1 and α2 collagen proteins. The aim of this study was to compare collagen secreted by skin fibroblast cells from a patient with suspected OI, to a control sample. It is hypothesised that collagen from the patient will be larger in size, and thus have slower mobility, than the control. Skin fibroblasts were treated with ascorbic acid to stimulate collagen production. Procollagen was extracted from the culture medium by precipitation and treated with pepsin to remove the non-helical sequences. The collagen was separated using SDS-PAGE electrophoresis on a 7.5% acrylamide gel. The α1 and α2 chains (95kDa and 92kDa respectively) were not present in either sample. Truncated collagen chains were present in the control at 70 kDa and 50kDa, and 75kDa and 55 kDa in the patient sample. While there is a slight difference in size between samples, the presence of bands at lower than expected sizes and the low resolution of the gel do not allow a definitive diagnosis of OI. Further investigation using genetic sequencing is required.
1. Introductory sentence explaining the topic area
2. Main aim and hypothesis being tested
3. General methods used
4. Results obtained
5. Conclusion
Provide a short written comment that describes the strengths and weaknesses of each abstract.
Osteogenesis Imperfecta (OI) is characterized by brittle bones caused by defective collagen. The most common cause is a mutation in the COL1A1 or COL1A2 genes coding for the α1 and α2 collagen proteins. The aim of this study was to compare collagen secreted by skin fibroblast cells from a patient with suspected OI, to a control sample. It is hypothesised that collagen from the patient will be larger in size, and thus have slower mobility, than the control. Skin fibroblasts were treated with ascorbic acid to stimulate collagen production. Procollagen was extracted from the culture medium by precipitation and treated with pepsin to remove the non-helical sequences. The collagen was separated using SDS-PAGE electrophoresis on a 7.5% acrylamide gel. The α1 and α2 chains (95kDa and 92kDa respectively) were not present in either sample. Truncated collagen chains were present in the control at 70 kDa and 50kDa, and 75kDa and 55 kDa in the patient sample. While there is a slight difference in size between samples, the presence of bands at lower than expected sizes and the low resolution of the gel do not allow a definitive diagnosis of OI. Further investigation using genetic sequencing is required.
