Archives for September 2016

Experimental Imaging Agent Reveals Concussion-Linked Brain Disease in Living Brain

(School of Medicine at Mount Sinai) An experimental positron emission tomography (PET) tracer can effectively diagnose concussion-related brain degeneration while a person is still alive, according to a proof-of-concept study conducted at the Icahn School of Medicine at Mount Sinai and published September 27 in the journal Translational Psychiatry.

Mount Sinai researchers used an experimental imaging agent called [18 F]-T807 (or Avid 1451) with PET to examine the brain of a living, 39-year-old retired National Football League (NFL) player who had experienced 22 concussions and exhibited clinical symptoms consistent with chronic traumatic encephalopathy (CTE), a neurodegenerative brain disease that has been associated with repetitive blows to the head in athletes and soldiers.

T807 is designed to latch onto a protein called tau that accumulates in the brain as a result of repetitive traumatic brain injury. When the new imaging agent (or ligand) lights up a PET scan of the brain of a patient showing buildup of tau in a characteristic pattern, the scan result is interpreted as being consistent with CTE. Until now, evidence for CTE pathology has only been possible by examining brain tissue after death.

CTE has a distinctive pattern of tau deposition that was described in 2015 by an expert panel commissioned by the National Institute of Neurological Disorders and Stroke (NINDS). That panel laid out diagnostic criteria for CTE based on samples of postmortem brain tissue.

The surface of the brain is highly wrinkled. The tau accumulation in CTE appears to trace the highly folded surface of the brain and is especially concentrated at the deepest points in the wrinkles and folds. The NINDS panel used the word “pathognomonic” to describe the CTE tau pathology pattern. This is a technical term that indicates that whenever you see this pattern of tau pathology, the diagnosis can be nothing other than CTE. There can be no confusion with other tau diseases.

“Our study participant’s scan is the first to reveal during life a pattern of tau imaging that outlines the wrinkles and folds of the living brain, just like the ‘pathognomonic pattern’ described by the NINDS panel as diagnostic of a brain with CTE,” says Sam Gandy, MD, Director of the Center for Cognitive Health and NFL Neurological Care Program at the Icahn School of Medicine at Mount Sinai and last author of the study.

“When fully validated, this new ligand has the potential to be used as a diagnostic biomarker and represents an exciting development in the detection and tracking of CTE.”

A link between brain injury and long-term health has gained greater attention in recent years, helped along by evidence of neurofibrillary tangles of tau protein, or tauopathy, that has been clinically confirmed in the postmortem brain tissue of former athletes and soldiers with histories of multiple head traumas. In addition to symptoms such as irritability and extreme mood swings, CTE is associated with the symptoms of various other neurodegenerative diseases, including Alzheimer’s, Parkinson’s and Lou Gehrig’s diseases.

“This research is in its infancy,” says Dara L. Dickstein, PhD, Assistant Professor of Neuroscience, and Geriatrics and Palliative Medicine at the Icahn School of Medicine at Mount Sinai and first author of the study.

“Whether or not the pathology can be reversed or halted is something we have yet to determine and these new tauopathy PET scans may be able to help in this endeavor.”

Under the leadership of Drs. Gandy and Dickstein, and with primary funding support from the Alzheimer’s Drug Discovery Foundation (ADDF), Mount Sinai is one of the few medical centers researching the use of the new ligand in living patients who are believed to have CTE.

The Mount Sinai team is currently studying 24 patients and plans to establish a clinical trial early next year that will employ the new ligand to identify CTE patients who might respond to an anti-tauopathy medicine that is currently being studied at other medical centers for the treatment of Alzheimer’s disease and other neurodegenerative disorders.

“These findings demonstrate that we may now have the first biomarker for the detection of CTE through tau imaging,” says Howard Fillit, MD, ADDF’s Founding Executive Director and Chief Science Officer.

“This may prove significant as an early diagnostic tool for those who suffer repeated traumatic brain injuries. It may also help us better understand the similarities in disease processes between CTE, Alzheimer’s and other neurodegenerative diseases, and determine whether repeated head injuries may lead to the onset of Alzheimer’s.”


Journal Reference:

D L Dickstein, M Y Pullman, C Fernandez, J A Short, L Kostakoglu, K Knesaurek, L Soleimani, B D Jordan, W A Gordon, K Dams-O’Connor, B N Delman, E Wong, C Y Tang, S T DeKosky, J R Stone, R C Cantu, M Sano, P R Hof, S Gandy. Cerebral [18 F]T807/AV1451 retention pattern in clinically probable CTE resembles pathognomonic distribution of CTE tauopathy. Translational Psychiatry, 2016; 6 (9): e900 DOI: 10.1038/tp.2016.175

© 2016 Icahn School of Medicine at Mount Sinai


New Imaging Technique in Alzheimer’s Disease Opens Up Possibilities for New Drug Development

(Lund University) Tau PET is a new and promising imaging method for Alzheimer’s disease. A case study from Lund University in Sweden now confirms that tau PET images correspond to a higher degree to actual changes in the brain. According to the researchers behind the study, this increases opportunities for developing effective drugs.


The brain of an Alzheimer’s patient in a tau PET image. Red indicates the areas with the highest concentration of the tau protein. In the magnifying glass, a microscope enlargement showing the dark red streaks and islands of tau. Illustration: Michael Sch

There are several different methods of producing images showing the changes in the brain associated with Alzheimer’s disease. The tau PET method reveals the presence of a protein in the brain, tau, with the help of a gamma camera and a specially selected radioactive molecule (F-AV-1451).

Tau has an important function in assisting the transport of various substances within the brain’s nerve cells. People with Alzheimer’s disease have raised levels of tau, leading to accumulation of the protein in the brain cells and gradually to cell death.

Lund University and Skåne University Hospital are among other institutions studying patients with the tau PET method for research purposes. Until now, no one has had precise knowledge of how well the new imaging method reproduces the actual changes in a brain affected by Alzheimer’s disease. The current case study, however, shows that image and reality match up well. The study has enabled researchers to compare tau PET images and brain tissue from the same person for the first time. The brain tissue came from a person who died having recently undergone examination with the new imaging method.

“Tau PET can improve diagnostics, but above all, the imaging method can be of great significance in the development of new drugs to combat Alzheimer’s disease,” explains Ruben Smith, researcher at Lund University and physician at Skåne University Hospital. He continues:

“There are new candidate drugs which aim to reduce the accumulation of tau. The imaging method opens up opportunities to investigate the development of the disease at a detailed level, and to observe how tau aggregates are affected by the drugs.”

“The person who was examined had a mutation which led to the same type of accumulation of tau in the brain as in Alzheimer’s disease. A single case study might seem insignificant, but since there are areas with a lot of tau stored and others with less tau in the same brain, it is sufficient to examine one person in order to verify whether the imaging method works,” explains Oskar Hansson, professor at Lund University and consultant at Skåne University Hospital.

Interest from the research community in imaging methods focusing on tau is strong and growing. A reliable reproduction of tau protein in the brain is considered a more relevant marker and a better diagnostic tool than competing methods which are already in use.

The researchers behind the study are now focusing on tracking aggregation of tau in the brain over time and connections with diagnostics using spinal fluid samples.

Tau PET imaging is considered interesting for other, less common, neurological diseases as well, such as frontal lobe dementia and Parkinson’s-like diagnoses such as PSP (progressive supranuclear palsy) and CBD (corticobasal degeneration).

The results are published in the journal Brain and the study was funded by the European Research Council (ERC), the Swedish Research Council, the Swedish Alzheimer’s Fund and the Swedish Brain Fund, among others.


Journal Reference:

Ruben Smith, Andreas Puschmann, Michael Schöll, Tomas Ohlsson, John van Swieten, Michael Honer, Elisabet Englund, Oskar Hansson. 18F-AV-1451 tau PET imaging correlates strongly with tau neuropathology inMAPTmutation carriers. Brain, 2016; 139 (9): 2372 DOI:10.1093/brain/aww163

Copyright Lund University


Dementia: Catching the Memory Thief

(University of Cambridge) It’s over a hundred years since the first case of Alzheimer’s disease was diagnosed. Since then we’ve learned a great deal about the protein ‘tangles’ and ‘plaques’ that cause the disease. How close are we to having effective treatments — and could we even prevent dementia from occurring in the first place?

You may have heard of the ‘dementia tsunami’. It’s heading our way. As our population ages, the number of cases of dementia is set to rocket, overwhelming our health services and placing an enormous burden on our society.

Only, it’s not quite so simple. A study published last year by Professor Carol Brayne from the Cambridge Institute of Public Health suggested that better education and living standards meant people were at a lower risk of developing the disease than previously thought and so, despite our ageing population, numbers were likely to stabilise — and could even perhaps fall slightly.

Of course, even this more optimistic outlook does not hide the fact that millions of people worldwide will be diagnosed with dementia each year and millions are already living with the condition. An effective treatment for the ‘memory thief’ still seems like a distant prospect.

“Dementia isn’t one disease: it’s a constellation of changes in an individual’s brain, with many underlying causes,” says Brayne.

“Most people, by the time they’re in their eighties or nineties, have some of these changes in their brains, regardless of whether or not they ever develop dementia.”

For this reason, Brayne believes we need a radical approach to tackling brain health throughout the course of our lifetime, with a greater emphasis on reduction in the risk of dementia achieved through measures in society that are related to better health in general, such as social and lifestyle changes, in addition to the focus on early therapeutic approaches to preventing or treating the disease through a pharmaceutical approach.

By far the most common and well-known form of dementia is Alzheimer’s disease. Symptoms include memory problems, changes in behaviour and progressive loss of independence.

At a biological level, the disease sees a build-up of two particular types of proteins in the brain: fragments of beta-amyloid clump together in ‘plaques’ between nerve cells, and twisted strands of tau form ‘tangles’ within the nerve cells. These plaques and tangles lead to the death of nerve cells, causing the brain to shrink.

Clinical trials of Alzheimer’s drugs are always going to be difficult, in part because trial participants are patients with advanced stage disease, who have already lost a significant number of nerve cells. But Professor Chris Dobson, who recently helped secure £17 million from the Higher Education Funding Council for England for a new Chemistry of Health Building, including the Centre for Misfolding Diseases, believes that most of the trials to date were destined to fail from the start because of a fundamental lack of understanding of the mechanisms that lead to Alzheimer’s.

Understandably, most of the researchers tackling Alzheimer’s approach the disease as a clinical — or at least a biological — problem.

Dobson instead sees it as also being about chemistry and physics. He argues that the protein tangles and plaques — collectively known as aggregates — are demonstrating a physical property similar to the way in which crystals precipitate out of, say, salty water: all they need is a ‘seed’ to kick off the precipitation and the process runs away with itself.

“In essence,” he says, “biology is trying to suppress molecules behaving in a physical way.”

For his contributions, Dobson has been awarded the 2014 Heineken Prize for Biochemistry and Biophysics.

In 2009, Dobson, together with colleagues Professors Tuomas Knowles and Michele Vendruscolo, published a study that broke down the aggregation process into a combination of smaller steps, each of which could be tested experimentally. It became apparent to the team that drugs were failing in trials because they were targeting the wrong steps.

“And this is still happening,” says Vendruscolo.

“Companies are still putting small molecules into clinical trials that, when we test them using our methods, we find stand no chance.”

They believe there may be a role to play for ‘neurostatins’, which could do for Alzheimer’s what statins already do to reduce cholesterol levels and prevent heart attacks and strokes. In fact, they may have already identified compounds that might fit the bill.

Professor Michel Goedert from the Medical Research Council Laboratory of Molecular Biology admits that there is a gap between our understanding of Alzheimer’s and our ability to turn this into effective therapies.

“We know much about the causes of inherited forms of Alzheimer’s disease, but this knowledge has so far not led to any therapies,” he says.

“It’s clear now that abnormal protein aggregation is central to Alzheimer’s disease, but we don’t know the mechanisms by which this aggregation leads to neurodegeneration.”

Goedert himself played an instrumental part in studies that implicated the aggregation of tau protein in Alzheimer’s disease and other neurodegenerative diseases, work that led to him being awarded the 2014 European Grand Prix from the Paris-based Foundation for Research on Alzheimer’s Disease.

“I don’t think we should talk of a cure,” says Goedert.

“At best, we will be able to halt the disease. Prevention will be much more important.”

Part of the problem, he says, lies in the fact that there is no absolute way of identifying those at risk of developing Alzheimer’s disease.

The market for an Alzheimer’s drug is massive, which is why pharmaceutical companies are racing to develop new drugs. Goedert doesn’t believe we will ever find a single ‘magic bullet’, but will need to use combination therapies — in the same way that we treat other diseases, such as HIV — with each drug targeting a particular aspect of the disease.

Professor David Rubinsztein from the Cambridge Institute for Medical Research agrees with Goedert that we need to look at preventing Alzheimer’s rather than just focusing on treating the disease. He, too, believes in the concept of neurostatins.

“These compounds would be safe, well tolerated by most people and generally good for you; you could take them for many years before the onset of disease,” he says.

“Then we wouldn’t need to worry about identifying people at highest risk of the disease — everyone could take them.”

Rubinsztein is the academic lead for Cambridge’s new Alzheimer’s Research UK Drug Discovery Institute, part of a £30 million Drug Discovery Alliance that also includes the University of Oxford and University College London. This state-of-the-art institute will fast-track the development of new treatments for Alzheimer’s disease and other neurodegenerative diseases. In particular, the Alliance will look at promising drug targets, assess their validity and develop small molecules that target them. These could then be taken up by pharmaceutical companies for clinical trials, removing some of the risk that results in most ‘promising’ drug candidates failing early on.

Rubinsztein is optimistic about our chances of fighting Alzheimer’s.

“If you could delay the onset of Alzheimer’s, even by three to five years, that discovery would be transformative and massively reduce the number of people getting the disease,” he says.

“We’re not asking to stop the disease, just to delay it. It’s really not such a big ask.”

Cambridge Neuroscience plays a key role in coordinating dementia research across the large and diverse community of neuroscientists in Cambridge, helping scientists and clinicians to work together.


© 2016 University of Cambridge


Online Advice for Preventing Alzheimer’s Disease Often Problematic

(Journal of Alzheimer’s Disease) New University of British Columbia (UBC) research finds that many online resources for preventing Alzheimer’s disease are problematic and could be steering people in the wrong direction.

In a survey of online articles about preventing Alzheimer’s disease, UBC researchers found many websites offered poor advice and one in five promoted products for sale—a clear conflict of interest.

“The quality of online information about preventing Alzheimer’s disease ranges,” said Julie Robillard, assistant professor of neurology at UBC with the Djavad Mowafaghian Centre for Brain Health and the National Core for Neuroethics.

“The few websites offering high-quality information can be hard to distinguish from the many low-quality websites offering information that can be potentially harmful.”

Today, 564,000 Canadians are living with dementia but the number is expected to grow to nearly one million in the next 15 years as the population ages. Alzheimer’s disease is the most common form of dementia but there is a lot of uncertainty about what causes the disease and how to protect yourself from it. Previous research has shown that about 80 per cent of people, and half of older adults, turn to the Internet for health information.

Robillard and undergraduate student Tanya Feng examined almost 300 online articles about preventing Alzheimer’s disease. They found websites with high-quality information often provided high-level advice suggesting individuals consider lifestyle modifications like managing their diabetes and exercising regularly.

The researchers identified a few common red flags for low-quality information, such as websites recommending products for sale alongside the content. They found this type of conflict of interest in one in five websites. Other signs of low-quality information included websites with very specific recommendations and nutritional information.

“Many red flags were not specific to what they were saying, but rather how they were saying it,” said Feng. “For example, using strong language like ‘cure’ or ‘guarantee’, promoting their own products, and relying on anecdotal evidence instead of empirical research is suggestive of poor-quality information in online dementia information.”

The researchers say this type of information can also be costly with people sinking money into products with little or no scientific evidence to show that they are effective. More concerning, however, is that the advice can cause anxiety and may impact the physician-patient relationship. Patients may sometimes feel they cannot trust their physician if they disagree with the recommendations or patients may not inform their physicians that they have changed their daily habits.

The researchers are developing a tool called QUEST, a simple test of six questions that anyone can use to help people recognize high-quality information online.

The study was published today in the Journal of Alzheimer’s Disease.

This research was funded by the Canadian Institutes for Health Research, the British Columbia Knowledge Development Fund, the Canadian Foundation for Innovation and the Vancouver Coastal Health Research Institute.

Click here for the video “How to weed out bad information online and tips on preventing Alzheimer’s disease”.


Journal of Alzheimer’s Disease is published by IOS Press

Copyright © 2016


Project Aims to Increase Access to Dementia Capable Care for LGBT Seniors

(Alzheimer’s Association) According to the Services & Advocacy for GLBT Elders (SAGE) organization, there are an estimated 1.5 to 3 million lesbian, gay, bisexual, and transgender (LGBT) elders nationwide. A recent report by the Institute for Multigenerational Health shows why LGBT adults are an at-risk and vulnerable population. Those over the age of 50 are more likely to be single and live alone. They may be at higher risk of experiencing isolation because they are more than four times as likely as heterosexual older adults to be childless.

In addition, caregiving support is limited for many LGBT older adults as a result of reduced family support and fear of discrimination in healthcare and legal services. That in turn can lead to depression, poor nutrition and poverty, which lessen the quality of life for both older LGBT adults and elders of color. Research suggests that marginalized elders are also at a higher risk for abuse, neglect, and exploitation.

San Francisco has the largest, most diverse, and fastest growing population of LGBT older adults in the country. With the LGBT population expected to double by 2030, there will be a significant increase in the need for dementia care in that community. The only way to address this surge is to facilitate LGBT dementia competency in mainstream services.

That is why the Alzheimer’s Association, in collaboration with Openhouse and Family Caregiver Alliance, will be providing trainings to health and social service providers through the San Francisco LGBT Dementia Care Project. The project will also connect LGBT seniors and adults with disabilities to services, programs and support available where they live.

The LGBT Dementia Care project is graciously funded by the San Francisco Department of Adult and Aging Services. It will serve as a starting point to increase access to culturally sensitive dementia care and support to the LGBT community regionally, and eventually statewide.

According to the Journal of Gerontological Social Work, there have been many instances of social services exhibiting homophobic and heterosexist beliefs that provoke fear and anxiety in LGBT older adults when accessing healthcare and social services. Multiple surveys show LGBT older adults consistently report a lack of confidence in the gay friendliness of service providers, which accounts for their lower rates of service use.

In a recent survey, researchers looked at a diverse representation of 616 LGBT San Francisco residents, aged 60 to 92-years-old. The findings suggest that nearly 60% of the participants live alone and 40% do not have the minimum income necessary to meet their basic needs. Only 15% have children; 60% of whom indicated that their children are not available to help them if needed. Two-thirds of those surveyed are neither partnered nor married. They also reported not having a will, powers of attorney for health care and finances, and revocable/irrevocable trust.

When it comes to services and programs, the results show a high rate of unmet need in health promotion, door-to-door transportation, caregiver support, day programs, housing assistance, in-home care, and telephone or online referrals. Despite the apparent need, many participants reported not using services because they feel these are difficult to access, not LGBT friendly, and often times too expensive. LGBT-welcoming healthcare would reduce the serious risks the community faces.

In addition to health risks, those who live alone, those with lower incomes, and those with less education are at a higher risk for housing instability. Not surprisingly, safe, stable, and affordable housing was identified as an important concern in San Francisco among those surveyed. Two-thirds of them reported being worried they may need to relocate due to health and financial problems. Fostering nondiscriminatory practices in housing assistance and other programs is a necessary step in addressing the disparities in this population.

If you are a health or social service provider, or a member of the San Francisco LGBT community, and would like to learn more about the services available, call us at 800.272.3900.

Helpful information related to this post:

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Alzheimers and Dementia Blog – Alzheimer’s Association of Northern California and Northern Nevada © 2016. All Rights Reserved.


The Shape-Shifting Protein Behind Alzheimer’s Disease

(Washington University in St. Louis) Researchers have known that the peptide amyloid beta plays a role in causing Alzheimer’s disease, but they are still working to determine how it becomes toxic.

Jan Bieschke, a biomedical engineer at Washington University in St. Louis, and collaborators in Germany have found that amyloid beta must change its internal structure into a long, flat structure called a beta sheet to be absorbed into the cell and become toxic. Results of the research were published Sept. 9 in the Journal of Biological Chemistry.


Bieschke, assistant professor of biomedical engineering in the School of Engineering & Applied Science, and his collaborators found that the amyloid beta protein structure that was able penetrate the cell had a specific type of beta sheet in which its peptides stacked onto each other, similar to a layer cake.

“Somewhere on this aggregation pathway, this type of structural element is formed for the amyloid beta to get into the cell,” Bieschke said.

“There is a two-step process: amyloid beta can bind to the membrane and form aggregates while on the surface of the cell, then it gets taken up into the cell.”

Alzheimer’s researchers have had a long-standing debate on whether amyloid beta is toxic before entering the nerve cell or after entering the cell. Amyloid beta can interfere with the mitochondria, or the cell’s energy powerhouse. This causes the cell to stop breathing and leads to eventual cell death. Studies of patients with late-stage Alzheimer’s disease reveal the death of many nerve cells in the brain.

With this knowledge, Bieschke and his collaborators can investigate what happens next to amyloid beta once inside the cell and how it interacts with the mitochondria.

“We will determine if we can see and measure the interaction with the mitochondria membrane, and if these structures are interacting with mitochondria the same way as with the outer cell membrane,” he said.

“Another question we will ask is: Can we manipulate the uptake or formation of these structures so they cannot enter the cell? This may be a therapeutic strategy to help future patients with Alzheimer’s.”


by Beth Miller

© 2016 Washington University in St. Louis


Mediterranean Diet: A Heart-healthy Eating Plan

(Mayo Clinic) The heart-healthy Mediterranean is a healthy eating plan based on typical foods and recipes of Mediterranean-style cooking. Here’s how to adopt the Mediterranean diet.

If you’re looking for a heart-healthy eating plan, the Mediterranean diet might be right for you. The Mediterranean diet incorporates the basics of healthy eating — plus a splash of flavorful olive oil and perhaps even a glass of red wine — among other components characterizing the traditional cooking style of countries bordering the Mediterranean Sea.

Most healthy diets include fruits, vegetables, fish and whole grains, and limit unhealthy fats. While these parts of a healthy diet remain tried-and-true, subtle variations or differences in proportions of certain foods may make a difference in your risk of heart disease.

Benefits of the Mediterranean Diet

Research has shown that the traditional Mediterranean diet reduces the risk of heart disease. In fact, an analysis of more than 1.5 million healthy adults demonstrated that following a Mediterranean diet was associated with a reduced risk of death from heart disease and cancer, as well as a reduced incidence of Parkinson’s and Alzheimer’s diseases.

The Dietary Guidelines for Americans recommends the Mediterranean diet as an eating plan that can help promote health and prevent disease. And the Mediterranean diet is one your whole family can follow for good health. mcdc6_pyramid_mediterranean

Key Components of the Mediterranean Diet

The Mediterranean diet emphasizes:

  • Eating primarily plant-based foods, such as fruits and vegetables, whole grains, legumes and nuts
  • Replacing butter with healthy fats, such as olive oil
  • Using herbs and spices instead of salt to flavor foods
  • Limiting red meat to no more than a few times a month
  • Eating fish and poultry at least twice a week
  • Drinking red wine in moderation (optional)

The diet also recognizes the importance of being physically active, and enjoying meals with family and friends.

Focus on Fruits, Vegetables, Nuts and Grains

The Mediterranean diet traditionally includes fruits, vegetables and grains. For example, residents of Greece average six or more servings a day of antioxidant-rich fruits and vegetables.

Grains in the Mediterranean region are typically whole grain and usually contain very few unhealthy trans fats, and bread is an important part of the diet. However, throughout the Mediterranean region, bread is eaten plain or dipped in olive oil — not eaten with butter or margarine, which contains saturated or trans fats.

Nuts are another part of a healthy Mediterranean diet. Nuts are high in fat, but most of the fat is healthy. Because nuts are high in calories, they should not be eaten in large amounts — generally no more than a handful a day. For the best nutrition, avoid candied or honey-roasted and heavily salted nuts.

Choose Healthier Fats

The focus of the Mediterranean diet isn’t on limiting total fat consumption, but rather on choosing healthier types of fat. The Mediterranean diet discourages saturated fats and hydrogenated oils (trans fats), both of which contribute to heart disease.

The Mediterranean diet features olive oil as the primary source of fat. Olive oil is mainly monounsaturated fat — a type of fat that can help reduce low-density lipoprotein (LDL) cholesterol levels when used in place of saturated or trans fats. “Extra-virgin” and “virgin” olive oils (the least processed forms) also contain the highest levels of protective plant compounds that provide antioxidant effects.

Canola oil and some nuts contain the beneficial linolenic acid (a type of omega-3 fatty acid) in addition to healthy unsaturated fat. Omega-3 fatty acids lower triglycerides, decrease blood clotting, and are associated with decreased incidence of sudden heart attacks, improve the health of your blood vessels, and help moderate blood pressure. Fatty fish — such as mackerel, lake trout, herring, sardines, albacore tuna and salmon — are rich sources of omega-3 fatty acids. Fish is eaten on a regular basis in the Mediterranean diet.

What about Wine?

The health effects of alcohol have been debated for many years, and some doctors are reluctant to encourage alcohol consumption because of the health consequences of excessive drinking. However, alcohol — in moderation — has been associated with a reduced risk of heart disease in some research studies.

The Mediterranean diet typically includes a moderate amount of wine, usually red wine. This means no more than 5 ounces (148 milliliters) of wine daily for women of all ages and men older than age 65 and no more than 10 ounces (296 milliliters) of wine daily for younger men. More than this may increase the risk of health problems, including increased risk of certain types of cancer.

If you’re unable to limit your alcohol intake to the amounts defined above, if you have a personal or family history of alcohol abuse, or if you have heart or liver disease, refrain from drinking wine or any other alcohol.

Putting it All Together

The Mediterranean diet is a delicious and healthy way to eat. Many people who switch to this style of eating say they’ll never eat any other way. Here are some specific steps to get you started:

  • Eat your veggies and fruits — and switch to whole grains.Avariety of plant foods should make up the majority of your meals. They should be minimally processed — fresh and whole are best. Include veggies and fruits in every meal and eat them for snacks as well. Switch to whole-grain bread and cereal, and begin to eat more whole-grain rice and pasta products. Keep baby carrots, apples and bananas on hand for quick, satisfying snacks. Fruit salads are a wonderful way to eat a variety of healthy fruit.
  • Go nuts. Nuts and seeds are good sources of fiber, protein and healthy fats. Keep almonds, cashews, pistachios and walnuts on hand for a quick snack. Choose natural peanut butter, rather than the kind with hydrogenated fat added. Try blended sesame seeds (tahini) as a dip or spread for bread.
  • Pass on the butter. Try olive or canola oil as a healthy replacement for butter or margarine. Lightly drizzle it over vegetables. After cooking pasta, add a touch of olive oil, some garlic and green onions for flavoring. Dip bread in flavored olive oil or lightly spread it on whole-grain bread for a tasty alternative to butter. Try tahini as a dip or spread for bread too.
  • Spice it up. Herbs and spices make food tasty and can stand in for salt and fat in recipes.
  • Go fish. Eat fish at least twice a week. Fresh or water-packed tuna, salmon, trout, mackerel and herring are healthy choices. Grill, bake or broil fish for great taste and easy cleanup. Avoid breaded and fried fish.
  • Rein in the red meat. Limit red meat to no more than a few times a month. Substitute fish and poultry for red meat. When choosing red meat, make sure it’s lean and keep portions small (about the size of a deck of cards). Also avoid sausage, bacon and other high-fat, processed meats.
  • Choose low-fat dairy. Limit higher fat dairy products, such as whole or 2 percent milk, cheese and ice cream. Switch to skim milk, fat-free yogurt and low-fat cheese.

© 1998-2016 Mayo Foundation for Medical Education and Research. All rights reserved.


Genetic ‘Switch’ Identified as Potential Target for Alzheimer’s Disease

(Imperial College London) A team at the MRC Clinical Sciences Centre (CSC), based at Imperial College London, has found an important part of the machinery that switches on a gene which may protect against Alzheimer’s Disease.

Working in collaboration with scientists at the Hong Kong University (HKU) and the Erasmus University in Rotterdam, CSC associate professor Richard Festenstein explored the steps by which this Neuroglobin gene is gradually switched on, or up-regulated.

Neuroglobin has previously been shown to protect against Alzheimer’s disease in mice in which it makes the protective Neuroglobin. It is thought that the gene might play a protective role early in the disease in patients, but appears to be down-regulated as the disease progresses. It may therefore prove useful in developing new ways to try to prevent or treat this common cause of dementia, for which there is currently no cure.

Professor Festenstein and Dr Tan-Un from HKU, with help from Professor Sjaak Phillipsen at the Erasmus University, examined how the Neuroglobin gene ‘folds up’ in the cell using a technique called chromosome conformation capture. In results published today in the journal Nucleic Acids Research, they showed that a particular region of DNA, outside the coding region of the Neuroglobin gene itself, loops round to make contact with the start of the gene.

They tested the ability of this newly-identified DNA region to switch on the Neuroglobin gene using two approaches. First, they linked the DNA region directly to another so-called ‘reporter’ gene, and demonstrated simply that it does indeed act as an up-regulator. Second, they used the new ‘Crispr’ technique of gene editing to completely remove this section of DNA from the cell, and showed that the Neuroglobin gene was no longer switched on.

Together, the results gave the team confidence that this newly-identified DNA region is indeed a powerful switching mechanism of the Neuroglobin gene.

As Neuroglobin is thought to be protective in Alzheimer’s, it may be possible in the future to use this ‘switch’ in developing new treatments, such as gene therapy.

Such therapeutic approaches require a compact ‘chunk’ of DNA to be most efficient. Importantly, the team pinpointed the position of the new regulatory region, and found that it is some distance away from the Neuroglobin gene itself.

It may now be possible to remove the less relevant sections of DNA in between the Neuroglobin gene and its regulator to create an efficient therapeutic gene therapy unit. It may be that this target may prove useful not only in Alzheimer’s but also in other neurodegenerative diseases.


Journal Reference:

Kian Cheng Tan-Un et al. Identification of a novel distal regulatory element of the human Neuroglobin gene by the chromosome conformation capture approach. Nucleic Acids Research, September 2016 DOI: 10.1093/nar/gkw820

MRC Clinical Sciences Centre, Hammersmith Hospital Campus