In women?s life, one of the most important stages is menopause. It?s the natural and transition period generally happened between the ages of 45 and 55 and could last for five or more years. In this period, women?s mental and physical situation change from the last menstrual period. Some women have problems like hot flashes, vaginal dryness and irritation, and weak bones. But not all women face these health problems; it depends on how you take it up and view it.
When you turn into menopause, you stop producing estrogens; there is a drop in the levels of estrogens in your blood. This fall in hormone levels disrupts your menstrual cycle and produces the other symptoms that are associated with menopause. This time you may have certain symptoms and hormone imbalance and don?t know it! But things you should do is to make it clear what has been going on with your body and deal with those that may affect your health.
The average age of US women at the time of menopause is 51 years.
When occurs younger than 40 years, it is a premature. While occurs in a woman older than 55 years it is considered to be a late one. In the last one to two years of pre-menopause, the decrease in estrogen accelerates. At this stage, many women experience menopause symptoms. While in the post menopause stage, women?s symptoms increase with the age.
If you find it hard to cope with the menopause symptoms, you can turn to your doctor for help. Your doctor can help you make a smooth transition into menopause and beyond by: Letting you know what physical and emotional changes to expect Helping you explore all your options to handle minor or complex issues Working with you to develop an individual strategy, depending on your symptoms and your preferences
Now let?s discuss the changes. The most obvious sleeping problem is that some women sweat heavily and have to get up to change the sheets several times a night. Some women sweat heavily and have to get up to change the sheets several times a night. Also there are vaginal changes, such as dryness and loss of tone. Mood changes such as irritability, depression or anxiety, although it?s possible that these are due to life changes rather than the menopause itself. In addition, your vaginal walls can become thin and dry because the cells lining the vagina will not contain as much estrogen.
Don?t be afraid of this stage of your life. Both short and long-term conditions can be managed with your doctor?s help. Most common used method to deal with menopause symptoms is HRT, which is Hormone replacement therapy. There are many ways of taking HRT, with the most usual being a daily tablet. If you think it necessary, ask your doctor for detailed and specific medical aid.
The humanitarian crisis in the Horn of Africa continues to be desperate. In addition to hunger, there is disease and violence. NBC?s Rohit Kachroo reports.?? ?
As Google inches closer to completing its Motorola Mobility acquisition, it made another strategic move in its mobile plans: today it announced it would sell its 6.5 percent stake in 4G operator Clearwire, for a value of $1.60 per share, or $47 million. The sum represents a substantial discount on the share price of Clearwire, currently trading at $2.27.
Highlights from the American Association for the Advancement of Science annual meeting in Vancouver, February 16-20
Web edition : Wednesday, February 22nd, 2012
New calculations boost carbon released from thawing permafrost
Changes in permafrost as it thaws could release more carbon into the atmosphere than scientists had suspected, new research suggests. When permanently frozen ground thaws, it deepens the ?active layer? of soil from which carbon can percolate, Charles Koven of the Lawrence Berkeley National Laboratory in California reported February 19. Under pessimistic scenarios in which greenhouse gases continue to rise, some 60 to 80 percent of permafrost could disappear by 2100, he said. Calculations of how soil types vary by depth suggest that up to 700 petagrams (700 billion metric tons) of carbon could be vulnerable to decomposition. ?Typically people haven?t thought of the depth distribution of soil carbon, but that?s critical,? Koven said. ?Alexandra Witze
Lab-grown meat ready to eat this year, scientists say
A hamburger made from meat grown in the lab might be ready to eat this October, Mark Post from Maastricht University in the Netherlands reported on February 19. So far, scientists using bovine stem cells have made pieces of skeletal muscle that are about 3 centimeters long. Citing the growing global demand for meat and the environmental costs of raising livestock, Post said ?we need to get alternatives.? Post ? who received ?250,000 (about U.S. $331,000) from an anonymous donor for this project ? thinks that with adequate funding, lab-grown meat products could be commercially available in?10 to 20 years. ?Rebecca Cheung
Contact: Heather Buschman, Ph.D. hbuschman@sanfordburnham.org 858-795-5343 Sanford-Burnham Medical Research Institute
Sanford-Burnham researchers determine the first 3-D structure of the botulinum neurotoxin, together with the protein bodyguard that guides it through the body -- revealing weak spots that could be exploited to develop new counterterrorism measures
LA JOLLA, Calif., February 23, 2012 Researchers at Sanford-Burnham Medical Research Institute (Sanford-Burnham) and the Medical School of Hannover in Germany recently discovered how the botulinum neurotoxin, a potential bioterrorism agent, survives the hostile environment in the stomach on its journey through the human body. Their study, published February 24 in Science, reveals the first 3D structure of a neurotoxin together with its bodyguard, a protein made simultaneously in the same bacterium. The bodyguard keeps the toxin safe through the gut, then lets go as the toxin enters the bloodstream. This new information also reveals the toxin's weak spota point in the process that can be targeted with new therapeutics.
"Now that we better understand the structure of the bacterial machinery that was designed for highly efficient toxin protection and delivery, we can see more clearly how to break it," said Rongsheng Jin, Ph.D., assistant professor in Sanford-Burnham's Del E. Webb Neuroscience, Aging and Stem Cell Research Center and senior author of the study.
The Janus-faced toxin
The botulinum neurotoxin is two-faced. On one side, it's the most poisonous substance known to man, causing botulism. Accidental botulinum neurotoxin poisoning is usually food-borne, but it's also considered a potential bioterrorism agent. On the other side, botulinum neurotoxin is also used an effective therapy and popular cosmetic, such as in BOTOX.
The neurotoxin accomplishes both the good and the bad using the same trickparalyzing muscle cells by disrupting their connections with the nerves that tell them how and when to move. But before the neurotoxin can gain access to muscles and the neurons that control them, it must make a remarkable journey through the bodysurviving the digestive enzymes and extreme acidic environment in the stomach, penetrating the small intestine, and entering the bloodstream.
Sneaking a peek at the neurotoxin and its bodyguard
This latest study on the botulinum neurotoxin was the result of a close collaboration between the Jin group and a research group at the Institute of Toxicology at the Medical School of Hannover, led by Andreas Rummel, Ph.D., an expert on clostridial neurotoxins. They used a technique called X-ray crystallography, which uses powerful X-ray beams to produce 3D images of proteins at the atomic level, to study a genetically inactivated, nontoxic version of the botulinum neurotoxin.
These experiments helped the team visualize the atomic structure of all three parts of the toxin: 1) the region that recognizes neurons, 2) the enzyme that acts like a pair of scissors to cut human neural proteins and cause paralysis, and 3) the needle that punches holes to help deliver the enzyme to the nerve terminal. What's more, the researchers also captured the toxin's interaction with a second bacterial protein, called nontoxic nonhemagglutinin (NTNHA).
"We were surprised to see that NTNHA, which is not toxic, turned out to be remarkably similar to botulinum neurotoxin. It's composed of three parts, just like a copy of the toxin itself. These two proteins hug each other and interlock with what looks like a handshake," said Jin.
As the toxin moves through the body, NTNHA acts as its bodyguard, keeping it from being degraded when times are tough in the acidic stomach. However, as this study revealed, the toxin has a weak spot: when the toxin/NTNHA complex punches its way out of the small intestine, it's the change in pH that triggers a conformational change, breaks up the duo, and releases only the unprotected toxin into the bloodstream.
Towards prevention and therapy
According to Jin, this new knowledge about how the botulinum neurotoxin and NTNHA balance the need for strong binding and a timely release could be exploited to outsmart them.
"We now hope we might be able to fool the toxin and its bodyguard using a small molecule that sends the wrong signalmimicking pH change, prematurely breaking up their protective embrace, and leaving the stomach's digestive enzymes and acid to do their job," he said. "We envision this type of therapyeither alone or in combination with other therapies currently in developmentcould be given preventively at a time when botulinum neurotoxin contamination becomes a public health concern."
Moreover, this type of therapy could be designed for oral delivery, rather than injection, making it easier to treat large numbers of people during an outbreak. A similar strategy could be used to deliver other protein-based drugs that usually need to be injected. "Here, protein drugs could be linked to a botulinum neurotoxin fragment and protected with NTNHA. Then we could possibly take them by mouth," Jin said.
###
This research was partly funded by a start-up fund from Sanford-Burnham, the Alfred P. Sloan Foundation, the German Research Foundation, the Robert-Koch-Institute, the National Institute of Allergy and Infectious Diseases, the U.S. Department of Energy, and the U.S. Department of Health and Human Services. The study's co-authors include Shenyan Gu, Sanford-Burnham; Sophie Rumpel, Medical School of Hannover; Jie Zhou, Sanford-Burnham; Jasmin Strotmeier, Medical School of Hannover; Hans Bigalke, Medical School of Hannover; Kay Perry, Cornell University and Argonne National Laboratory; Charles B. Shoemaker, Tufts Cummings School of Veterinary Medicine; Andreas Rummel, Medical School of Hannover; and Rongsheng Jin, Sanford-Burnham.
About Sanford-Burnham Medical Research Institute
Sanford-Burnham Medical Research Institute is dedicated to discovering the fundamental molecular causes of disease and devising the innovative therapies of tomorrow. The Institute consistently ranks among the top five organizations worldwide for its scientific impact in the fields of biology and biochemistry (defined by citations per publication) and currently ranks third in the nation in NIH funding among all laboratory-based research institutes. Sanford-Burnham is a highly innovative organization, currently ranking second nationally among all organizations in capital efficiency of generating patents, defined by the number of patents issued per grant dollars awarded, according to government statistics.
Sanford-Burnham utilizes a unique, collaborative approach to medical research and has established major research programs in cancer, neurodegeneration, diabetes, and infectious, inflammatory, and childhood diseases. The Institute is especially known for its world-class capabilities in stem cell research and drug discovery technologies. Sanford-Burnham is a U.S.-based, non-profit public benefit corporation, with operations in San Diego (La Jolla), Santa Barbara, and Orlando (Lake Nona). For more information, please visit our website or blog. You can also receive updates by following us on Facebook and Twitter.
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AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert! system.
Contact: Heather Buschman, Ph.D. hbuschman@sanfordburnham.org 858-795-5343 Sanford-Burnham Medical Research Institute
Sanford-Burnham researchers determine the first 3-D structure of the botulinum neurotoxin, together with the protein bodyguard that guides it through the body -- revealing weak spots that could be exploited to develop new counterterrorism measures
LA JOLLA, Calif., February 23, 2012 Researchers at Sanford-Burnham Medical Research Institute (Sanford-Burnham) and the Medical School of Hannover in Germany recently discovered how the botulinum neurotoxin, a potential bioterrorism agent, survives the hostile environment in the stomach on its journey through the human body. Their study, published February 24 in Science, reveals the first 3D structure of a neurotoxin together with its bodyguard, a protein made simultaneously in the same bacterium. The bodyguard keeps the toxin safe through the gut, then lets go as the toxin enters the bloodstream. This new information also reveals the toxin's weak spota point in the process that can be targeted with new therapeutics.
"Now that we better understand the structure of the bacterial machinery that was designed for highly efficient toxin protection and delivery, we can see more clearly how to break it," said Rongsheng Jin, Ph.D., assistant professor in Sanford-Burnham's Del E. Webb Neuroscience, Aging and Stem Cell Research Center and senior author of the study.
The Janus-faced toxin
The botulinum neurotoxin is two-faced. On one side, it's the most poisonous substance known to man, causing botulism. Accidental botulinum neurotoxin poisoning is usually food-borne, but it's also considered a potential bioterrorism agent. On the other side, botulinum neurotoxin is also used an effective therapy and popular cosmetic, such as in BOTOX.
The neurotoxin accomplishes both the good and the bad using the same trickparalyzing muscle cells by disrupting their connections with the nerves that tell them how and when to move. But before the neurotoxin can gain access to muscles and the neurons that control them, it must make a remarkable journey through the bodysurviving the digestive enzymes and extreme acidic environment in the stomach, penetrating the small intestine, and entering the bloodstream.
Sneaking a peek at the neurotoxin and its bodyguard
This latest study on the botulinum neurotoxin was the result of a close collaboration between the Jin group and a research group at the Institute of Toxicology at the Medical School of Hannover, led by Andreas Rummel, Ph.D., an expert on clostridial neurotoxins. They used a technique called X-ray crystallography, which uses powerful X-ray beams to produce 3D images of proteins at the atomic level, to study a genetically inactivated, nontoxic version of the botulinum neurotoxin.
These experiments helped the team visualize the atomic structure of all three parts of the toxin: 1) the region that recognizes neurons, 2) the enzyme that acts like a pair of scissors to cut human neural proteins and cause paralysis, and 3) the needle that punches holes to help deliver the enzyme to the nerve terminal. What's more, the researchers also captured the toxin's interaction with a second bacterial protein, called nontoxic nonhemagglutinin (NTNHA).
"We were surprised to see that NTNHA, which is not toxic, turned out to be remarkably similar to botulinum neurotoxin. It's composed of three parts, just like a copy of the toxin itself. These two proteins hug each other and interlock with what looks like a handshake," said Jin.
As the toxin moves through the body, NTNHA acts as its bodyguard, keeping it from being degraded when times are tough in the acidic stomach. However, as this study revealed, the toxin has a weak spot: when the toxin/NTNHA complex punches its way out of the small intestine, it's the change in pH that triggers a conformational change, breaks up the duo, and releases only the unprotected toxin into the bloodstream.
Towards prevention and therapy
According to Jin, this new knowledge about how the botulinum neurotoxin and NTNHA balance the need for strong binding and a timely release could be exploited to outsmart them.
"We now hope we might be able to fool the toxin and its bodyguard using a small molecule that sends the wrong signalmimicking pH change, prematurely breaking up their protective embrace, and leaving the stomach's digestive enzymes and acid to do their job," he said. "We envision this type of therapyeither alone or in combination with other therapies currently in developmentcould be given preventively at a time when botulinum neurotoxin contamination becomes a public health concern."
Moreover, this type of therapy could be designed for oral delivery, rather than injection, making it easier to treat large numbers of people during an outbreak. A similar strategy could be used to deliver other protein-based drugs that usually need to be injected. "Here, protein drugs could be linked to a botulinum neurotoxin fragment and protected with NTNHA. Then we could possibly take them by mouth," Jin said.
###
This research was partly funded by a start-up fund from Sanford-Burnham, the Alfred P. Sloan Foundation, the German Research Foundation, the Robert-Koch-Institute, the National Institute of Allergy and Infectious Diseases, the U.S. Department of Energy, and the U.S. Department of Health and Human Services. The study's co-authors include Shenyan Gu, Sanford-Burnham; Sophie Rumpel, Medical School of Hannover; Jie Zhou, Sanford-Burnham; Jasmin Strotmeier, Medical School of Hannover; Hans Bigalke, Medical School of Hannover; Kay Perry, Cornell University and Argonne National Laboratory; Charles B. Shoemaker, Tufts Cummings School of Veterinary Medicine; Andreas Rummel, Medical School of Hannover; and Rongsheng Jin, Sanford-Burnham.
About Sanford-Burnham Medical Research Institute
Sanford-Burnham Medical Research Institute is dedicated to discovering the fundamental molecular causes of disease and devising the innovative therapies of tomorrow. The Institute consistently ranks among the top five organizations worldwide for its scientific impact in the fields of biology and biochemistry (defined by citations per publication) and currently ranks third in the nation in NIH funding among all laboratory-based research institutes. Sanford-Burnham is a highly innovative organization, currently ranking second nationally among all organizations in capital efficiency of generating patents, defined by the number of patents issued per grant dollars awarded, according to government statistics.
Sanford-Burnham utilizes a unique, collaborative approach to medical research and has established major research programs in cancer, neurodegeneration, diabetes, and infectious, inflammatory, and childhood diseases. The Institute is especially known for its world-class capabilities in stem cell research and drug discovery technologies. Sanford-Burnham is a U.S.-based, non-profit public benefit corporation, with operations in San Diego (La Jolla), Santa Barbara, and Orlando (Lake Nona). For more information, please visit our website or blog. You can also receive updates by following us on Facebook and Twitter.
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AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert! system.
Just why has Minneapolis? Carlson Real Estate Company hired an investment banking firm to review the company?s 5.5-million-square-foot real estate investment portfolio?
It?s a good question. But it?s not one that Matt Van Slooten, president of Carlson Real Estate is ready to answer.
Minnesota Real Estate Journal contacted Carlson to ask why the company in February hired investment banking firm Eastdil Secured to assist it in reviewing and evaluating strategic alternatives for its real estate investment portfolio.
A spokesperson for Carlson said that Van Slooten is not available for interviews on this topic.
It is certain, though, that Carlson might be willing to sell some or all of its real estate holdings if it receives the right bids for its properties.
Carlson?s real estate portfolio includes properties in Minnesota, North Carolina and Arizona. Key properties among the Minnesota portion of the portfolio include the business park surrounding the corporate campus of the Carlson Companies in Minnetonka and the 36-story office tower in downtown Minneapolis that holds the Radisson Plaza Hotel and Plaza Seven Office Tower.
In a press release, Carlson Real Estate Company said that it has directed Eastdil to explore a full range of possibilities that could include a sale or joint-venture arrangement of its real estate business operations or portions of its portfolio.
The company?s Minnesota portfolio is anchored by several properties within Carlson Center, the business park surrounding the Carlson headquarters at the intersection of Interstate-394 and Interstate-494 in the western suburbs of Minneapolis.
CREC also owns a 36-story mixed-use project in downtown Minneapolis containing the Radisson Plaza Hotel and Plaza Seven Office Tower.
Though Van Slooten did not want to hold a telephone interview about Carlson?s arrangement with Eastdil, the company president did release an official statement: ?This is an exciting time for Carlson Real Estate. We are exploring new forms of financial arrangements from what we?ve had in the past, with the goal of maximizing the potential of our real estate business.?
Carlson Real Estate Company has operated as a separate business from Carlson?s other operating groups for more than 25 years.
Tags | Carlson Real Estate Company
? 2012 Real Estate Communications Group. Duplication or reproduction of this article not permitted without authorization from the Real Estate Publishing Group. For information on reprint or electronic pdf of this article contact Mark Menzies at 312-644-4610 or menzies@rejournals.com
AP - Rick Santorum is looking for another upset or two, while Mitt Romney is hoping to keep his leading rival at bay in the run-up to the 20th debate of the race for the Republican presidential nomination.
As Google inches closer to completing its Motorola Mobility acquisition, it made another strategic move in its mobile plans: today it announced it would sell its 6.5 percent stake in 4G operator Clearwire, for a value of $1.60 per share, or $47 million. The sum represents a substantial discount on the share price of Clearwire, currently trading at $2.27.![[ Back to EurekAlert! ]](https://lh3.googleusercontent.com/blogger_img_proxy/AEn0k_sNif1EUz0LAQFnKYrGks0pMgIC89cHjVCTYhQDDSqEGXaFftixQvKCZB2b8grzTjdWKjyX5v9l8EkWyXN9qXP5HTiPkCn0YmLKi7izlCg=s0-d){kind=small}
Public release date: 23-Feb-2012
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