Since the start of the semester we have accumulated the following stats...
Current Credits: 1,545.03
Current Standing: 807,411 out of 1,356,026
Current RAC credit: 18.81504
Current Standing: 261,580 out of 1,356,026
Monday, May 5, 2008
Sunday, April 27, 2008
Alzheimer’s Heritability, Selection, and Affects of Inbreeding
Heritability
The role of heritability in Alzheimer’s disease is a question that is heavily contemplated and explored by researchers. A study published in the Archives of General Psychiatry worked to quantify the role that genetics played in the onset of the disease. Researchers from the University of Southern California looked at 392 sets of elderly twins over the age of 65. The use of twins allowed scientists to look at both environmental and genetic factors of the disease. In the case of identical (monozygotic) twins, all of their genes are shared, so if the disease is highly genetic than it should be observed in both or neither of the twins. If only one individual had it, it is likely to be more influenced by environmental factors. It was found that identical twins were more likely to both have the disease when compared to non-identical twins, which suggested that genetic factors are relatively significant. The estimated heritability was found to be between 58% and 79%. This study confirmed the Alzheimer’s appears to be heritable and that the genetic factors influence both male and female patients, but there are also some environmental factors that affect the development of the disease. However, what all of the environmental factors maybe are still not completely known.
Alzheimer's risk 'is 80% genetic'. BBC. news.bbc.co.uk/1/hi/health/4686806.stm
Selection
The onset of Alzheimer’s typically occurs later in life, so it seems that selection would have very little to no effect since the phenotype is not exhibited until after the usual reproductive age. It also does not seem plausible that the history of Alzheimer’s in a person’s family history would limit their reproductive prospects either.
Inbreeding
In most cases, only dominate genes have been associated as a possible cause of Alzheimer’s disease. However a study published in Neurology exposed the idea that a recessive gene may play a role in the development of the disease. 821 elderly residents of an Arab community called Wadi Ara in Israel were screened for the disease. It was found that 20% of individuals over 65 had the disease and 60% of individuals over 85 did as well. This was compared to an overall 40% occurrence in the general population. The dominate gene (APOE-4) which is commonly linked with Alzheimer’s was found to be of low occurrence in this population (only 15%). However, the Wadi Ara community is known for its large family size and high frequency of inbreeding (about 44%), which leads researchers to look for a recessive gene that would be exposed by the inbreeding of the population.
This is not an isolated case. Other populations, such as the people of Sangueany in Canada also have a reasonably high rate of intermarriage and a higher occurrence of Alzheimer’s disease. Unfortunately, Americans often refuse to participate in such studies, up to 30%, which limits the research that can be done in the United States regarding the connection between Alzheimer’s and a possibly dangerous recessive allele.
Buckles, Julie. First evidence recessive gene plays role in Alzheimer’s disease. Genome News Network. 2000.
genomenewsnetwork.org/articles/09_00/Alzheimer_recessive.shtml.
Friday, April 4, 2008
Why Should Doctors Know About Evolution??
d To understand the relevance of laboratory studies on animals and how it relates to advancements in human health care:
d To be able to continue to provide effective health care:
d To understand the relevance of laboratory studies on animals and how it relates to advancements in human health care:
- With no understanding of evolution, it would be unclear how laboratory studies on animals correlate with humans. A working knowledge of evolution, however, articulates that all organisms have a single common ancestor. Animals, themselves, have a closer, single common ancestor and share the same genes from this ancestor. This orthology gives an explanation as to why studies on animals relate to humans: all animals have the same general body components, functions, processes, reactions, and development. From this it can be assumed that the results of studies on animals will be similar if applied to humans.
d To be able to continue to provide effective health care:
- Rapidly mutating viruses, such as HIV and influenza, are major health concerns and should be fully understood by doctors. Pathogens reproduce quickly and have a high mutation rate, causing them to be able to evolve more quickly than the host population. Human immune systems, as well as the medicines we are prescribed, select for pathogens that can evade our immune systems if we are reinfected. The more successful genotype then becomes more common, and is therefore resistant to treatment. Doctors must understand how pathogens may evolve, and also be up to date on the current forms of pathogens such as influenza, in order to maintain the effectiveness of treatments and vaccines in the face of the evolving pathogen populations.
d To understand the condition of the human population
- The environment in which humans live has evolved much more rapidly than the human population itself. Therefore, it can be speculated that humans are not truly adapted to their current environment. This may be one reason that some of the diseases (such as breast cancer) afflicting humans exist. The lack of adaptation may also explain some human behaviors such as parental care.
d Understanding natural immunity/ repair mechanisms
- The cells in the human body can evolve and change. The cells with better fitness are more likely to survive and therefore may allow the body to rid itself of a fatal genetic disease ( such as adenosine deaminase deficiency).
Knowledge gained from the paper on FFI:
n Katie - I learned that protein misfolding can cause a myriad of different problems/diseases, and that small changes can result in similar diseases. I had never heard of FFI before reading this paper, and was surprised to learn how similar it is Alzheimer's disease. Studying protein misfolding will help to better understand the effects resulting from different protein folding arrangements. This knowledge can then be used, at least theoretically, to help find cures for the resulting diseases. The similarity of some of the diseases may allow a chain reaction to be put into motion with one new cure/find being able to cure multiple diseases with little or no change in the formula.
n Megan - I also have never heard of FFI before now, and I looked into it a bit more. According to Merck Manuals, it occurs in the PrPc protein and another form occurs without the mutation, it is called sporadic fatal insomnia. I think that identifying diseases such as this (both symptoms and causes) may help find cures for existing diseases (such as FFI and Alzheimer's) while also explaining other symptoms and problems that people experience with no explanation for them. It seems as if there are not many families that have the mutation, but it raises the question if there may be more, or simmilar mutations that have other symptoms.
n Hailey - After reading about FFI I felt that protein folding and dementia diseases made more sense to me. I learned about a disease that is much more understood than Alzheimer's but very similar as well. This really clarified and reaffirmed the concept of protein folding and misfolding for me by presenting an interesting example.
Wednesday, March 26, 2008
Question Over Reading of Case Study on FFI
Further reading: http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600072
1. Based on your research into Alzheimer’s disease and your interview, how are these two disorders alike?
Both FFI and Alzheimer’s disease are characterized by degeneration of the brain and accumulation of amyloid plaques. However, FFI amyloid plaques are the result of prion protein fragments and amyloid plaques in Alzheimer’s disease are the result of amyloid precursor protein (APP) fragments. The onset of both diseases does not occur until after child-bearing years. Both diseases cause severe dementia in the end stages and are fatal. The forebrain is the main component affected in both diseases, with the thalamus being most affected by FFI, and the cerebral cortex and hypothalamus being most affected by Alzheimer’s disease. Individuals with either disease exhibit hallucinations, disruption of circadian rhythms (night-day/ sleep-wake cycles), and loss of the ability to speak. The families of individuals suffering from these diseases are forced to provide an increasing amount of care to the individuals as the disease progresses. Another difference is that it is unknown if Alzheimer’s is hereditary where as FFI is hereditary.
2. What are prions?
Prions are proteins (PrPC ) which naturally occur in the human body and are associated mainly with brain tissue. A mutation in the PRNP gene which codes for the prion protein causes an abnormal form of the prion protein to be produced (PRPSC).The abnormal protein somehow is able to convert normal prion proteins into the abnormal form, and these abnormal proteins clump together forming amyloid plaques that damage or destroy nerve cells. (http://ghr.nlm.nih.gov/condition=priondisease)
3. FFI is an autosomal dominant disease, meaning that if an individual inherits just one dominant allele from either parent, they will develop the disease. However, this disease does not manifest itself phenotypically until after reproductive age. So can this disorder be acted on by natural selection? What about Alzheimer’s? What is maintaining these disorders in the population?
No, this disease cannot be acted on by natural selection because natural selection works on the phenotype of an individual, which appears normal in individuals with FFI until after child bearing years. An individual may have already produced offspring with the mutation before their own maladaptive traits even surfaced. However, genetic testing allows a couple to know if one or both of them possess the genetic abnormality and therefore may pass the gene to offspring. The same is true for Alzheimer’s disease, although Alzheimer’s is thought to be less heritable than FFI. These disorders are maintained in the population due to mutations, as well as the lack of phenotypic manifestation prior to reproductive age.
4. FFI is caused by a single mutation that, in the presence of methionine at amino acid position 129, changes aspartic acid to asparagine. This same mutation, in the presence of valine at position 129, causes a separate prion-disease called Creutzfeldt-Jacob syndrome. In cattle, the homologous syndrome is Mad Cow disease. How can studying protein folding and mis-folding help in understanding diseases like these?
Proteins are formed from long, linear chains of amino acids and fold into shapes that depend on the properties of the amino acids of the chain. Properties such as hydrophobia, hydrophilia, electrical charge, etc, (http://en.wikipedia.org/wiki/Protein_folding#Incorrect_protein_folding_and_neurodegenerative_disease). In the missense mutations that cause prion diseases mentioned above, different amino acids are inserted into the chain of amino acids. When the protein folds, the different amino acid has dissimilar properties to the amino acid that was meant to be in that spot and therefore folds the protein differently. This new folding may cause the protein to have a new function or, most likely, it will cause the protein to be non-functioning.
So studying the properties of amino acids can help to predict how proteins will fold. Also, studying how proteins with known amino acids sequences fold can help predict what properties different amino acids have. If researchers could discover the shapes of all proteins, then early detection of misfolding could be a possibility in the future of science and medicine.
1. Based on your research into Alzheimer’s disease and your interview, how are these two disorders alike?
Both FFI and Alzheimer’s disease are characterized by degeneration of the brain and accumulation of amyloid plaques. However, FFI amyloid plaques are the result of prion protein fragments and amyloid plaques in Alzheimer’s disease are the result of amyloid precursor protein (APP) fragments. The onset of both diseases does not occur until after child-bearing years. Both diseases cause severe dementia in the end stages and are fatal. The forebrain is the main component affected in both diseases, with the thalamus being most affected by FFI, and the cerebral cortex and hypothalamus being most affected by Alzheimer’s disease. Individuals with either disease exhibit hallucinations, disruption of circadian rhythms (night-day/ sleep-wake cycles), and loss of the ability to speak. The families of individuals suffering from these diseases are forced to provide an increasing amount of care to the individuals as the disease progresses. Another difference is that it is unknown if Alzheimer’s is hereditary where as FFI is hereditary.
2. What are prions?
Prions are proteins (PrPC ) which naturally occur in the human body and are associated mainly with brain tissue. A mutation in the PRNP gene which codes for the prion protein causes an abnormal form of the prion protein to be produced (PRPSC).The abnormal protein somehow is able to convert normal prion proteins into the abnormal form, and these abnormal proteins clump together forming amyloid plaques that damage or destroy nerve cells. (http://ghr.nlm.nih.gov/condition=priondisease)
3. FFI is an autosomal dominant disease, meaning that if an individual inherits just one dominant allele from either parent, they will develop the disease. However, this disease does not manifest itself phenotypically until after reproductive age. So can this disorder be acted on by natural selection? What about Alzheimer’s? What is maintaining these disorders in the population?
No, this disease cannot be acted on by natural selection because natural selection works on the phenotype of an individual, which appears normal in individuals with FFI until after child bearing years. An individual may have already produced offspring with the mutation before their own maladaptive traits even surfaced. However, genetic testing allows a couple to know if one or both of them possess the genetic abnormality and therefore may pass the gene to offspring. The same is true for Alzheimer’s disease, although Alzheimer’s is thought to be less heritable than FFI. These disorders are maintained in the population due to mutations, as well as the lack of phenotypic manifestation prior to reproductive age.
4. FFI is caused by a single mutation that, in the presence of methionine at amino acid position 129, changes aspartic acid to asparagine. This same mutation, in the presence of valine at position 129, causes a separate prion-disease called Creutzfeldt-Jacob syndrome. In cattle, the homologous syndrome is Mad Cow disease. How can studying protein folding and mis-folding help in understanding diseases like these?
Proteins are formed from long, linear chains of amino acids and fold into shapes that depend on the properties of the amino acids of the chain. Properties such as hydrophobia, hydrophilia, electrical charge, etc, (http://en.wikipedia.org/wiki/Protein_folding#Incorrect_protein_folding_and_neurodegenerative_disease). In the missense mutations that cause prion diseases mentioned above, different amino acids are inserted into the chain of amino acids. When the protein folds, the different amino acid has dissimilar properties to the amino acid that was meant to be in that spot and therefore folds the protein differently. This new folding may cause the protein to have a new function or, most likely, it will cause the protein to be non-functioning.
So studying the properties of amino acids can help to predict how proteins will fold. Also, studying how proteins with known amino acids sequences fold can help predict what properties different amino acids have. If researchers could discover the shapes of all proteins, then early detection of misfolding could be a possibility in the future of science and medicine.
**This disease was discussed last week on Medical Mysteries: (http://video.google.com/videoplay?docid=760959254431325673&q=fatal+familial+insomnia&total=3&start=0&num=10&so=0&type=search&plindex=0)
The two sisters in this story lost their mother to FFI. One sister chose to be tested for the mutation, while the other sister did not. Would each of you want to know whether or not you had a disease such as this, or would you rather remain unaware?
Katie – I would want to know if I had the disease. If I knew that I would possibly develop the disease then I could get all of my affairs in order while I was still lucid enough to make rational and well thought out decisions. I would also be able to prepare my family for what would happen with the disease began to appear and progress. If I chose not to be tested then I would always be wondering if I had the disease or if and when I would develop the symptoms. But if I was tested and the results showed that I was free of the disease, then I would be freed from constant worry and would be able to more fully enjoy the rest of my life.
Hailey – I would definitely want to be tested for the mutation that causes FFI. Although I would feel a great deal of anxiety if I found that I had it, I think I would feel an even greater sense of anxiety if I did not know. Discovering the presence of this mutation in me and knowing what my future held would be beneficial knowledge. Like Katie said, I could get everything prepared for my family so there would less stress with my death. Also, I could make arrangements for myself for when I reach the stages of the disease that require much care. Overall, getting tested would leave me with more peace of mind than not being tested.
Megan- I don't think that I would want to know if I had the mutation. I think that it would cause me and everyone else around me to live life differently. I am a reasonably care free person, and the last thing that I would want to do is make others worry and walk on egg shells around me. There are any number of things that could happen to me at any time, so even if I knew about the mutation, I still couldn't plan for the future, becuase I don't know what else may happen. If I had the mutation, I would deal with it when I had no other choice. It would already be taking away enough of my time, and I wouldn't want to spend my time before planning for it.
Sunday, February 24, 2008
Memories in the Making Auction
For any who might be interested, or know someone who may be interested, in attending the 2008 Memories in the Making Auction, it will be held Friday, April 18, 2008. Feel free to check out the website for more information.
http://www.alz.org/kansascity/in_my_community_10166.asp
http://www.alz.org/kansascity/in_my_community_10166.asp
Thursday, February 14, 2008
Interview
We chose to interview Kelly Lobe, an expert on Alzheimer's disease, to get a feel for this disease and how it relates to grid computing dealing with protien folding. She is with the Alzheimer's Association: http://www.alz.org/index.asp
2/13/2008:
Q: What is your job title and what do you do?
A: Kelly is the Outreach Coordinator for Spanish speaking individuals. She speaks both English and Spanish and works with Spanish speaking individuals with Alzheimer’s and their families, as well as working with those who speak Spanish that work at Alzheimer’s care facilities, hospice care, etc.
Q: Why did you decide to work with the Alzheimer’s Association in this field?
A: She had begun Dental School but then discovered she did not want to be a dentist. Always having been interested in working with Senior Citizens, she so decided to go to graduate school to get her degree in Gerontology. While working towards her graduate degree she was required to do an internship which happened to be with the Alzheimer’s Association, and enjoyed it so she stayed. She also has a B.A. in English from UMKC. Her original interest in pursuing her graduate degree was to work with successful aging in a healthy population, and even though they’re not healthy individuals, she does work to help people with Alzheimer’s disease live as normal a life as possible as they get older.
Q: What is it like working with with Alzheimer’s patients and their families?
A: She says that most people believe this kind of work is often overwhelming, sad, and depressing. She admits that sometimes it is, but it is also very fulfilling. Kelly feels she has learned a lot from the people she works with and seems to care a great deal for what she does.
Q: Have you ever heard of grid computing networks?
A: She had not heard of grid computing networks, but I explained to her what project we were doing and somewhat how the grid project works.
Q: What do you think about studying protein folding and protein composition in order to find a cure for diseases such as Alzheimers/ have you ever heard of studying protein misfolding in order to obtain cures?
A: She thinks she has heard of this, but in other terms. She did say she knows one thing researchers are looking at is the role of beta-amyloid proteins in Alzheimer’s disease. (http://www.fasebj.org/cgi/content/abstract/9/5/366 )
Q: Are there any new treatments that you are aware of that can slow the progression of, or lessen symptoms of, Alzheimer’s disease?
A: She said there are some exciting new possibilities to slow the progression of the Alzheimer’s that are in the 3rd phase of testing, but she does not expect them to be out by the end of this year. Also, there is some testing being done on the effects of some diabetes medications that may help Alzheimer’s disease. She feels that this is a good example of how possibly curing one disease may help find a cure for another disease – for instance, curing diabetes or cancer may also help find treatments or cures for Alzheimers. Unfortunately there is not, as of yet, a “magic pill” that will cure Alzheimers, but the medications that are coming out are designed to help slow the progression and therefore let the patients live a longer, more fulfilling life.
Q: What is the average age for diagnosis; at what age do people begin to show signs?
A: The average age of symptom onset is 65 years old. However, there are 5 million people known to have the disease 10% of which are under 65. Those afflicted under 65 have early onset Alzheimer’s disease.
Q: What misconceptions exist about Alzheimer’s?
A: She said there are many misconceptions about Alzheimer’s and it is hard to know where to start. She said the biggest and most problematic, in her opinion, are that having Alzheimer’s means the individual is helpless, that the individual is incapable of feeling joy or being joyous, that all with Alzheimer’s patients are mean and irritable, and she stressed that Alzheimer’s patients DO NOT forget how to love. They still have feelings and are still people, often times the individual is simply trapped behind the disease.
Q: Is there any evidence that Alzheimer’s is a hereditary disease?
A: Family history does matter and can play a factor, but just because a relative has the disease does not guarantee that you will have the disease. However, the younger a person’s age at the onset of symptoms the greater the chance that offspring will develop the disease. Basically… “sometimes yes and sometimes no”.
Q: Where and how do researchers even begin to search for a cure?
A: She said there are many places to begin. For one, begin with the biology of aging – decide what is normal for aging and what is abnormal. Many still believe memory loss is a normal part of aging but that’s not true. Also, look at the role the environment plays on the disease and what manageable elements, (such as diet, etc.), there are in the environments. Advancements in healthcare and diagnostics also play a role. Obviously, those with health care are more likely be diagnosed with a problem than those who have no access to healthcare and must simply live with the symptoms. Finally, advancements in technology could play a huge role in developing a cure.
Q: Have there been any advancements toward a cure? What are they?
A: As previously stated, medications may lead to a cure. Also, there have been many advances in diagnostic tools such as CT scans, PET scans, etc.
Q: Do you think the study of evolution is important in your field? If so how or why?
A: Yes, in the sense of humans adapting to a changing trends in the world. For instance, the conditions and environment of the world are different today then they were when the first person was diagnosed with this disease. Also, she feels that since in a way all life is connected, then if a discovery is made in another species it may be beneficial to helping us make advancements toward a cure in our species.
Q: Do you have any interesting stories?
A: She said she had many interesting stories, but it was hard to pick just a few. She chose to tell me about this new program that they have at the Alzheimer’s Association called Project Lifesaver. Alzheimer’s patients are prone to wandering, so this project uses tracking devices that can be activated if a person goes missing in order to find them. They are not used for monitoring around the clock as spying devices, but they do dramatically cut down the time it takes to find a wandering individual. Without the device it takes on average 9 hours to find a missing person, but with the device it normally takes only about 20 minutes. She really supports and promotes this program because it is so critical to find individuals quickly to ensure they are safe. Kelly is also a trained rescue and recovery worker.
There is another program called Memories in the Making that is an art program designed to dispel misconceptions about Alzheimers disease. It keeps people connected and active and requires no artistic talent. The patients make pictures of whatever they decide. Often the pictures are past memories that show that the individuals long term memory is still very keen, they just have problems with short term memory. She said there was one person who had been either a veterinarian or taxidermist and he began drawing these very detailed and beautiful pictures of animals. Each spring they have an auction to sell some of the better art which helps support the foundation and the search for a cure.
Q: What do you think is the best way that average people can help in the research of cures for diseases?
A: Kelly says the best way is to speak up. Talk to your own families, elected officials, etc. Get out and vote for officials who will help the cause and also vote and advocate more funding for research projects and foundations. Also, remind people that anyone can ask for help, and people don’t just have to deal with their symptoms themselves.
Q: What is the normal time frame from diagnosis to end stage disease or end of life.
A: It ranges from 2 – 20 years depending on environment, other health conditions, etc., with the average being about 8 – 10 years. Younger individuals, those with early onset Alzheimer’s, tend to deteriorate more quickly.
Q: Is any one area of the brain more affected than another from the disease?
A: The hippocampus, (short term memory), is the first part of the brain to be damaged and the disease progresses forward. The next major area to be damaged is the frontal lobe. Eventually the entire brain succumbs to damage, however. (Inside the Brain: Interactive tour of the brain and Alzheimer’s disease: http://www.alz.org/alzheimers_disease_4719.asp )
** We want to thank Kelly so much for her time!!
We chose to interview Kelly Lobe, an expert on Alzheimer's disease, to get a feel for this disease and how it relates to grid computing dealing with protien folding. She is with the Alzheimer's Association: http://www.alz.org/index.asp
2/13/2008:
Q: What is your job title and what do you do?
A: Kelly is the Outreach Coordinator for Spanish speaking individuals. She speaks both English and Spanish and works with Spanish speaking individuals with Alzheimer’s and their families, as well as working with those who speak Spanish that work at Alzheimer’s care facilities, hospice care, etc.
Q: Why did you decide to work with the Alzheimer’s Association in this field?
A: She had begun Dental School but then discovered she did not want to be a dentist. Always having been interested in working with Senior Citizens, she so decided to go to graduate school to get her degree in Gerontology. While working towards her graduate degree she was required to do an internship which happened to be with the Alzheimer’s Association, and enjoyed it so she stayed. She also has a B.A. in English from UMKC. Her original interest in pursuing her graduate degree was to work with successful aging in a healthy population, and even though they’re not healthy individuals, she does work to help people with Alzheimer’s disease live as normal a life as possible as they get older.
Q: What is it like working with with Alzheimer’s patients and their families?
A: She says that most people believe this kind of work is often overwhelming, sad, and depressing. She admits that sometimes it is, but it is also very fulfilling. Kelly feels she has learned a lot from the people she works with and seems to care a great deal for what she does.
Q: Have you ever heard of grid computing networks?
A: She had not heard of grid computing networks, but I explained to her what project we were doing and somewhat how the grid project works.
Q: What do you think about studying protein folding and protein composition in order to find a cure for diseases such as Alzheimers/ have you ever heard of studying protein misfolding in order to obtain cures?
A: She thinks she has heard of this, but in other terms. She did say she knows one thing researchers are looking at is the role of beta-amyloid proteins in Alzheimer’s disease. (http://www.fasebj.org/cgi/content/abstract/9/5/366 )
Q: Are there any new treatments that you are aware of that can slow the progression of, or lessen symptoms of, Alzheimer’s disease?
A: She said there are some exciting new possibilities to slow the progression of the Alzheimer’s that are in the 3rd phase of testing, but she does not expect them to be out by the end of this year. Also, there is some testing being done on the effects of some diabetes medications that may help Alzheimer’s disease. She feels that this is a good example of how possibly curing one disease may help find a cure for another disease – for instance, curing diabetes or cancer may also help find treatments or cures for Alzheimers. Unfortunately there is not, as of yet, a “magic pill” that will cure Alzheimers, but the medications that are coming out are designed to help slow the progression and therefore let the patients live a longer, more fulfilling life.
Q: What is the average age for diagnosis; at what age do people begin to show signs?
A: The average age of symptom onset is 65 years old. However, there are 5 million people known to have the disease 10% of which are under 65. Those afflicted under 65 have early onset Alzheimer’s disease.
Q: What misconceptions exist about Alzheimer’s?
A: She said there are many misconceptions about Alzheimer’s and it is hard to know where to start. She said the biggest and most problematic, in her opinion, are that having Alzheimer’s means the individual is helpless, that the individual is incapable of feeling joy or being joyous, that all with Alzheimer’s patients are mean and irritable, and she stressed that Alzheimer’s patients DO NOT forget how to love. They still have feelings and are still people, often times the individual is simply trapped behind the disease.
Q: Is there any evidence that Alzheimer’s is a hereditary disease?
A: Family history does matter and can play a factor, but just because a relative has the disease does not guarantee that you will have the disease. However, the younger a person’s age at the onset of symptoms the greater the chance that offspring will develop the disease. Basically… “sometimes yes and sometimes no”.
Q: Where and how do researchers even begin to search for a cure?
A: She said there are many places to begin. For one, begin with the biology of aging – decide what is normal for aging and what is abnormal. Many still believe memory loss is a normal part of aging but that’s not true. Also, look at the role the environment plays on the disease and what manageable elements, (such as diet, etc.), there are in the environments. Advancements in healthcare and diagnostics also play a role. Obviously, those with health care are more likely be diagnosed with a problem than those who have no access to healthcare and must simply live with the symptoms. Finally, advancements in technology could play a huge role in developing a cure.
Q: Have there been any advancements toward a cure? What are they?
A: As previously stated, medications may lead to a cure. Also, there have been many advances in diagnostic tools such as CT scans, PET scans, etc.
Q: Do you think the study of evolution is important in your field? If so how or why?
A: Yes, in the sense of humans adapting to a changing trends in the world. For instance, the conditions and environment of the world are different today then they were when the first person was diagnosed with this disease. Also, she feels that since in a way all life is connected, then if a discovery is made in another species it may be beneficial to helping us make advancements toward a cure in our species.
Q: Do you have any interesting stories?
A: She said she had many interesting stories, but it was hard to pick just a few. She chose to tell me about this new program that they have at the Alzheimer’s Association called Project Lifesaver. Alzheimer’s patients are prone to wandering, so this project uses tracking devices that can be activated if a person goes missing in order to find them. They are not used for monitoring around the clock as spying devices, but they do dramatically cut down the time it takes to find a wandering individual. Without the device it takes on average 9 hours to find a missing person, but with the device it normally takes only about 20 minutes. She really supports and promotes this program because it is so critical to find individuals quickly to ensure they are safe. Kelly is also a trained rescue and recovery worker.
There is another program called Memories in the Making that is an art program designed to dispel misconceptions about Alzheimers disease. It keeps people connected and active and requires no artistic talent. The patients make pictures of whatever they decide. Often the pictures are past memories that show that the individuals long term memory is still very keen, they just have problems with short term memory. She said there was one person who had been either a veterinarian or taxidermist and he began drawing these very detailed and beautiful pictures of animals. Each spring they have an auction to sell some of the better art which helps support the foundation and the search for a cure.
Q: What do you think is the best way that average people can help in the research of cures for diseases?
A: Kelly says the best way is to speak up. Talk to your own families, elected officials, etc. Get out and vote for officials who will help the cause and also vote and advocate more funding for research projects and foundations. Also, remind people that anyone can ask for help, and people don’t just have to deal with their symptoms themselves.
Q: What is the normal time frame from diagnosis to end stage disease or end of life.
A: It ranges from 2 – 20 years depending on environment, other health conditions, etc., with the average being about 8 – 10 years. Younger individuals, those with early onset Alzheimer’s, tend to deteriorate more quickly.
Q: Is any one area of the brain more affected than another from the disease?
A: The hippocampus, (short term memory), is the first part of the brain to be damaged and the disease progresses forward. The next major area to be damaged is the frontal lobe. Eventually the entire brain succumbs to damage, however. (Inside the Brain: Interactive tour of the brain and Alzheimer’s disease: http://www.alz.org/alzheimers_disease_4719.asp )
** We want to thank Kelly so much for her time!!
Thursday, January 31, 2008
Rosetta at Home
EVOLUTION SERVICE LEARING: Rosetta@home
Kathleen Berry, Megan Connon, Hailey Sheppard
Why Rosetta at Home?
The Rosetta project works to predict and design protein sturcture and protein complexes, that may eventually help in curing HIV/AIDS, cancer, Alzheimer's disease, malaria and many other diseases.
How it works?
This project is the next step beyond the Human Genome project and works to predict the shapes proteins fold into in nature, that can ultimately help in creating new enzymes, drugs, and vaccines to treat a variety of diseases. The folds of a protein are determined by the order of amino acids. To find the natural fold of a protein, the lowest energy fold must be identified. Rosetta uses the following strategy to find the low energy folds…
Rosetta logs the lowest energy shape in the final predicted structure (the trajectory). The trajectory has two stages. One: A simplified representation of amino acids is used to quickly try many different shapes. Two: A full representation is used and smaller changes are made in an attempt to discover the correct arrangement. This is known as “relaxation.”
Five to twenty trajectories are generated per work unit on a single computer and the lowest energy shape is recorded for each one. There are over 39,500 computer users contributing to the project.
LINKS/SOURCES
Kathleen Berry, Megan Connon, Hailey Sheppard
Why Rosetta at Home?
The Rosetta project works to predict and design protein sturcture and protein complexes, that may eventually help in curing HIV/AIDS, cancer, Alzheimer's disease, malaria and many other diseases.
How it works?
This project is the next step beyond the Human Genome project and works to predict the shapes proteins fold into in nature, that can ultimately help in creating new enzymes, drugs, and vaccines to treat a variety of diseases. The folds of a protein are determined by the order of amino acids. To find the natural fold of a protein, the lowest energy fold must be identified. Rosetta uses the following strategy to find the low energy folds…
It starts with an unfolded chain
The chain moves apart into a new shape
The energy of the new shape is calculated
Depending on the energy change, the move is accepted or rejected
1-4 are repeated over and over again
The chain moves apart into a new shape
The energy of the new shape is calculated
Depending on the energy change, the move is accepted or rejected
1-4 are repeated over and over again
Rosetta logs the lowest energy shape in the final predicted structure (the trajectory). The trajectory has two stages. One: A simplified representation of amino acids is used to quickly try many different shapes. Two: A full representation is used and smaller changes are made in an attempt to discover the correct arrangement. This is known as “relaxation.”
Five to twenty trajectories are generated per work unit on a single computer and the lowest energy shape is recorded for each one. There are over 39,500 computer users contributing to the project.
LINKS/SOURCES
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