Scurvy and lathyrism (specifically osteolathyrism) are both diseases involving abnormalities of collagen cross linking. Explain the cause (related to collagen) of each disease, what the effect is on collagen, and the consequences of the collagen defect or problem in each disease?

answer

watching

318

views

For unlimited access to Homework Help, a Homework+ subscription is required.

You have 0 free answers left.
Get unlimited access to 3.8 million step-by-step answers.

Get unlimited access

Already have an account? Log in

Patrina SchowalterLv2

18 Apr 2018

Unlock all answers

Get 1 free homework help answer.

Already have an account? Log in

Related questions

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 Î±1 and Î±2 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 Î±1 and Î±2 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 IN THIS PARAGRAPH.

The study of Osteogenesis Imperfecta and what causes it is important and the diagnosis of it is very important especially to those who may be affected by the illness. The diagnosis is what we are focusing on, the illness is caused by most commonly caused by the mutation in the collagen genes, specifically Î±1 collagen. This leads us to try to find this illness in a young boy, called Alexander Brown. We are trying to find out if this young boy has the illness commonly known as brittle bone disease, and we do this by extracting the collagen from normal un-affected cells and Alexanders cells, purifying the collagen and then running it through a Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) to separate out the various sizes of proteins left in the collagen. After running this SDS-PAGE we were able to compare the unaffected patterns of size to the cells collected from Alexander Brown however there can be no firm conclusions drawn from these results, the image taken of the SDS PAGE was blurred and pixelated as well as being very blue.

One of the most important structural components to any livingcell is Collagen. Itâs the most abundant protein in mammals and itsvarious forms are involved in everything from mitosis to boneformation. Its unique structural elements and various forms allowsit to be utilized in all cells.

Instructions: For this Worksheet, you will needto do several things:

Define the different structural motifs associated withcollagen.

Provide a detailed explanation for how it is synthesized, howcollagen strands form and what their uses are. Be sure to includeseveral examples of uses.

Research the disease states provided and explain how they arerelated to collagen in the body.

Structural Motifs:

Molecular components -

Trimeric structure -

Macromolecules -

Synthesis -

Formation -

Common uses -

Associated Disease states-

EhlersâDanlos syndromes -

Ullrich congenital muscular dystrophy-