Crisco was the original product made with partially hydrogenated soybean oil, which contains trans fats. Today, Crisco has only small amounts of the fats.
Tony Dejak/ASSOCIATED PRESS
Crisco was the original product made with partially hydrogenated soybean oil, which contains trans fats. Today, Crisco has only small amounts of the fats.
Tony Dejak/ASSOCIATED PRESS
If the Food and Drug Administration has its way, an era of food technology will soon end. The agency announced Thursday it is aiming to ban partially hydrogenated vegetable oils from all food products.
Margaret Hamburg, the FDA commissioner, said at a press conference that her agency has come to the preliminary conclusion that the oils "are not generally recognized as safe for use in food."
If the agency makes this decision final, it will mean a complete ban on this ingredient.
Health concerns about the trans fats in the oil have been mounting for years. The biggest concern? Trans fats raise the risk of heart disease. The Centers for Disease Control and Prevention estimates that an FDA ban on trans fats could prevent an additional 7,000 deaths from heart disease each year and up to 20,000 heart attacks each year.
But it took decades for health officials to arrive at that conclusion.
Partially hydrogenated oil came on the market about a century ago when food scientists figured out how to add hydrogen atoms to a molecule of oil. Typically, it's soybean oil.
Kantha Shelke, a scientist with the Institute of Food Technologists in Chicago, says this makes liquid oil more solid, and stable. Depending on how you add the hydrogen atoms, you can make the oil as solid as you like.
"So we could literally dial the needle to as solid as you wanted, and get the kind of results we were looking for," says Shelke.
These results include cookies or doughnuts that didn't leave a ring of oil behind on a paper towel and don't start tasting rancid after a few weeks.
Also, this oil doesn't have a strong taste of its own so you can use lots of it without ruining the flavor.
"It's really absolutely perfect, and it's also perfect for the American style of shopping: You buy boxes and boxes of crackers, put them in your pantry," says Shelke. "You open this box six months or eight months or a year later, and it would still taste and smell just as good as it was on the day you bought it!"
By the time the government came up with laws regulating food additives, people had been eating this form of oil for decades with no apparent problems.
David Schleifer, a researcher at a nonprofit group called Public Agenda, in New York, says most scientists in the 1980s actually thought this kind of oil was probably safer than lard or palm oil. Schleifer wrote a recent journal article on the history of trans fats.
McDonald's, Schleifer says, previously used beef tallow for frying. "People freaked out about beef tallow because it had saturated fat, and McDonald's responded to that public outcry by replacing beef tallow with trans fat," he says.
Everything changed in the mid-1990s. New studies showed that trans fats raised bad cholesterol and increased the risk of heart disease.
In fact, they were even worse than saturated fats. In 2006, after a campaign by public health advocates, the FDA required food companies to add trans fats to food labels.
Most companies responded by drastically cutting their use of partially hydrogenated oil. That had a big impact on consumption — Americans consumed around 1 gram per day in 2012, down from 4.6 grams per day in 2003.
But not every company has eliminated it from every product.
You can still find trans fats in microwavable popcorn, frozen pies and all kinds of mass-produced baked goods. Often, food companies use just a little bit. If there's less than half a gram of trans fats per serving they can list the amount of trans fats in their products as zero.
A complete ban on trans fats would be a big deal for food manufacturers, says Shelke. She says food companies can drop the trans fats, but their products won't be quite the same.
"They have to go back to re-educating consumers that cookies and consumers don't last forever," says Shelke.
The cookies will have a shorter life, but consumers' lives might be longer.
Hope builds for a drug that might shut down a variety of cancers
PUBLIC RELEASE DATE:
7-Nov-2013
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Contact: Sarah Smith sas2072@med.cornell.edu 646-317-7401 Weill Cornell Medical College
Cancer cells 'go to sleep' when crucial set of molecules is targeted
NEW YORK (November 7, 2013) -- The most frequently mutated gene across all types of cancers is a gene called p53. Unfortunately it has been difficult to directly target this gene with drugs. Now a multi-institutional research team, led by Dr. Lewis Cantley and investigators at Weill Cornell Medical College, has identified a family of enzymes they say is crucial for the growth of cancers that have genetic aberrations in p53. Targeting these enzymes with novel agents might prevent the growth of p53 mutant cancers, thereby benefiting a broad spectrum of cancer patients, including those with breast, ovarian, lung, colorectal and brain tumors.
In the Nov. 7 issue of Cell, investigators pinpoint two cellular enzymes -- Type 2 phosphatidylinositol-5-phosphate 4-kinases α and β (Type 2 PIP kinases) -- as essential for cancer growth when cells have lost p53, the powerful tumor-suppressor gene long dubbed the "guardian of the genome." More than half of all cancers lose this gene, allowing these cancers to grow at will.
The researchers discovered that the Type 2 PIP kinases are not critical for the growth of normal cells but become essential for cell growth when p53 is lost due to mutations or deletions. The scientists showed, in animal and lab studies of human cancer cells, that targeting these molecules effectively shuts down the growth of p53 mutant cancers.
Although the studies were conducted in human breast cancer cells, the researchers believe Type 2 PIP kinase inhibitors could block the growth of cancers with a mutated or missing p53 gene.
"The fact that one can delete the Type 2 PIP kinases in normal human cells or in mice with essentially no effect on cell survival suggests that inhibitors of these enzymes should have little toxicity," says Dr. Cantley, the study's senior author and director of the Cancer Center at Weill Cornell Medical College and NewYork-Presbyterian Hospital.
Dr. Cantley is already leading an effort to develop drugs to shut down these kinases. "Well-designed Type 2 PIP kinase inhibitors may turn the tide on p53 mutant cancer," he says.
A Crucial Link
Dr. Cantley is known for his discovery of the PI 3-kinase oncogene, and pioneering work in teasing apart how the gene contributes to cancer. PI 3-kinases (PI3K) have been linked to a wide variety of cellular functions, including cell growth and proliferation, and most cancers activate PI3K by one or more mechanisms. Dr. Cantley's discovery led to promising avenues for the development of personalized cancer therapies.
Activity of PI3K is in some cases linked to Type 2 PIP kinases, so in this study, Dr. Cantley sought to understand the function of these enzymes. Because the researchers knew that a subset of breast cancers over-express these molecules, investigators looked at their role in HER2-positive breast cancers, which typically are more aggressive tumors.
The researchers, including those from Harvard Medical School, Beth Israel Deaconess Medical Center and other institutions, discovered that the enzymes are silent in cells that have healthy p53. One critical role of p53 is to "rescue" cells that are producing excess reactive oxygen species (ROS), which are byproducts of cells that are growing too rapidly. The oxidative stress produced by ROS can damage cell structures, so p53 attempts to reduce ROS in affected cells. "If, however, ROS levels exceed the capacity of p53s to rescue it, then p53 takes on a second function, which is to kill the cell," Dr. Cantley says.
"That is why cancers often disable p53. If p53 is mutated or gone, then the cell keeps on growing at a very high rate," he says. "And then ROS begins to damage genes, making the cancer even more aggressive."
The Type 2 PIP kinases are the backup rescue system to p53. But they only reduce ROS enough to keep the cells from dying. (Too much ROS will also kill a cell.)
What this means is that cancer cells become "absolutely dependent on these kinases to be able to grow," Dr. Cantley says.
Taking Advantage of "Synthetic Lethality"
But there is a big and important hitch in this scenario, he adds. If the Type 2 PIP kinases are inhibited, and if p53 is deactivated, the cancer cell essentially "goes to sleep," he says. "It just stops dividing and growing. This is called synthetic lethality: You can get by without one gene or another, but if you lose both of them nothing can grow."
Shutting down these enzymes, as the researchers did in their experiments, puts cancer cells to sleep but has no effect on healthy cells. "A normal cell doesn't need Type 2 PIP kinases at all, so inhibitors of these enzymes should not be toxic to humans," Dr. Cantley says.
Because it is not possible to replace p53 proteins or the gene in cells that have lost it (many attempts have been made), deactivating Type 2 PIP kinases is the next-best thing, he adds. "This would likely be a very powerful advance in the treatment of many cancers."
###
This work was supported by NIH grant R01 GM041890 and by a Stand Up to Cancer Dream Team Translational Research Grant, a Program of the Entertainment Industry Foundation (SU2C-AACR-DT0209).
Co-authors include first author Dr. Brooke M. Emerling, Gary Bellinger and Rayman Choo-Wing from Weill Cornell Medical College; Dr. George Poulogiannis, Kazumi S. Tsukazawa, Hye-Seok Shim, and Dr. Gina M. DeNicola from Harvard Medical School; Dr. Gerburg M. Wulf, Dr. John M. Asara, Xin Yuan, and Dr. Andrea Bullock from Beth Israel Deaconess Medical School; Dr. Jonathan B. Hurov from Agios Pharmaceuticals; Dr. Eric L. Bell from the Massachusetts Institute of Technology; Dr. Katja A. Lamia from The Scripps Research Institute; Dr. Lucia E. Rameh from Boston University School of Medicine; Dr. Atsuo T. Sasaki from the University of Cincinnati College of Medicine; Dr. Jiaxi Song, Dr. Victoria Brown, and Dr. Sabina Signoretti from Dr. Dana-Farber Cancer Institute.
Weill Cornell Medical College
Weill Cornell Medical College, Cornell University's medical school located in New York City, is committed to excellence in research, teaching, patient care and the advancement of the art and science of medicine, locally, nationally and globally. Physicians and scientists of Weill Cornell Medical College are engaged in cutting-edge research from bench to bedside, aimed at unlocking mysteries of the human body in health and sickness and toward developing new treatments and prevention strategies. In its commitment to global health and education, Weill Cornell has a strong presence in places such as Qatar, Tanzania, Haiti, Brazil, Austria and Turkey. Through the historic Weill Cornell Medical College in Qatar, the Medical College is the first in the U.S. to offer its M.D. degree overseas. Weill Cornell is the birthplace of many medical advances including the development of the Pap test for cervical cancer, the synthesis of penicillin, the first successful embryo-biopsy pregnancy and birth in the U.S., the first clinical trial of gene therapy for Parkinson's disease, and most recently, the world's first successful use of deep brain stimulation to treat a minimally conscious brain-injured patient. Weill Cornell Medical College is affiliated with NewYork-Presbyterian Hospital, where its faculty provides comprehensive patient care at NewYork-Presbyterian Hospital/Weill Cornell Medical Center. The Medical College is also affiliated with Houston Methodist. For more information, visit weill.cornell.edu.
Office of External Affairs
Weill Cornell Medical College
tel: 646.317.7401
email: pr@med.cornell.edu
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Hope builds for a drug that might shut down a variety of cancers
PUBLIC RELEASE DATE:
7-Nov-2013
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Contact: Sarah Smith sas2072@med.cornell.edu 646-317-7401 Weill Cornell Medical College
Cancer cells 'go to sleep' when crucial set of molecules is targeted
NEW YORK (November 7, 2013) -- The most frequently mutated gene across all types of cancers is a gene called p53. Unfortunately it has been difficult to directly target this gene with drugs. Now a multi-institutional research team, led by Dr. Lewis Cantley and investigators at Weill Cornell Medical College, has identified a family of enzymes they say is crucial for the growth of cancers that have genetic aberrations in p53. Targeting these enzymes with novel agents might prevent the growth of p53 mutant cancers, thereby benefiting a broad spectrum of cancer patients, including those with breast, ovarian, lung, colorectal and brain tumors.
In the Nov. 7 issue of Cell, investigators pinpoint two cellular enzymes -- Type 2 phosphatidylinositol-5-phosphate 4-kinases α and β (Type 2 PIP kinases) -- as essential for cancer growth when cells have lost p53, the powerful tumor-suppressor gene long dubbed the "guardian of the genome." More than half of all cancers lose this gene, allowing these cancers to grow at will.
The researchers discovered that the Type 2 PIP kinases are not critical for the growth of normal cells but become essential for cell growth when p53 is lost due to mutations or deletions. The scientists showed, in animal and lab studies of human cancer cells, that targeting these molecules effectively shuts down the growth of p53 mutant cancers.
Although the studies were conducted in human breast cancer cells, the researchers believe Type 2 PIP kinase inhibitors could block the growth of cancers with a mutated or missing p53 gene.
"The fact that one can delete the Type 2 PIP kinases in normal human cells or in mice with essentially no effect on cell survival suggests that inhibitors of these enzymes should have little toxicity," says Dr. Cantley, the study's senior author and director of the Cancer Center at Weill Cornell Medical College and NewYork-Presbyterian Hospital.
Dr. Cantley is already leading an effort to develop drugs to shut down these kinases. "Well-designed Type 2 PIP kinase inhibitors may turn the tide on p53 mutant cancer," he says.
A Crucial Link
Dr. Cantley is known for his discovery of the PI 3-kinase oncogene, and pioneering work in teasing apart how the gene contributes to cancer. PI 3-kinases (PI3K) have been linked to a wide variety of cellular functions, including cell growth and proliferation, and most cancers activate PI3K by one or more mechanisms. Dr. Cantley's discovery led to promising avenues for the development of personalized cancer therapies.
Activity of PI3K is in some cases linked to Type 2 PIP kinases, so in this study, Dr. Cantley sought to understand the function of these enzymes. Because the researchers knew that a subset of breast cancers over-express these molecules, investigators looked at their role in HER2-positive breast cancers, which typically are more aggressive tumors.
The researchers, including those from Harvard Medical School, Beth Israel Deaconess Medical Center and other institutions, discovered that the enzymes are silent in cells that have healthy p53. One critical role of p53 is to "rescue" cells that are producing excess reactive oxygen species (ROS), which are byproducts of cells that are growing too rapidly. The oxidative stress produced by ROS can damage cell structures, so p53 attempts to reduce ROS in affected cells. "If, however, ROS levels exceed the capacity of p53s to rescue it, then p53 takes on a second function, which is to kill the cell," Dr. Cantley says.
"That is why cancers often disable p53. If p53 is mutated or gone, then the cell keeps on growing at a very high rate," he says. "And then ROS begins to damage genes, making the cancer even more aggressive."
The Type 2 PIP kinases are the backup rescue system to p53. But they only reduce ROS enough to keep the cells from dying. (Too much ROS will also kill a cell.)
What this means is that cancer cells become "absolutely dependent on these kinases to be able to grow," Dr. Cantley says.
Taking Advantage of "Synthetic Lethality"
But there is a big and important hitch in this scenario, he adds. If the Type 2 PIP kinases are inhibited, and if p53 is deactivated, the cancer cell essentially "goes to sleep," he says. "It just stops dividing and growing. This is called synthetic lethality: You can get by without one gene or another, but if you lose both of them nothing can grow."
Shutting down these enzymes, as the researchers did in their experiments, puts cancer cells to sleep but has no effect on healthy cells. "A normal cell doesn't need Type 2 PIP kinases at all, so inhibitors of these enzymes should not be toxic to humans," Dr. Cantley says.
Because it is not possible to replace p53 proteins or the gene in cells that have lost it (many attempts have been made), deactivating Type 2 PIP kinases is the next-best thing, he adds. "This would likely be a very powerful advance in the treatment of many cancers."
###
This work was supported by NIH grant R01 GM041890 and by a Stand Up to Cancer Dream Team Translational Research Grant, a Program of the Entertainment Industry Foundation (SU2C-AACR-DT0209).
Co-authors include first author Dr. Brooke M. Emerling, Gary Bellinger and Rayman Choo-Wing from Weill Cornell Medical College; Dr. George Poulogiannis, Kazumi S. Tsukazawa, Hye-Seok Shim, and Dr. Gina M. DeNicola from Harvard Medical School; Dr. Gerburg M. Wulf, Dr. John M. Asara, Xin Yuan, and Dr. Andrea Bullock from Beth Israel Deaconess Medical School; Dr. Jonathan B. Hurov from Agios Pharmaceuticals; Dr. Eric L. Bell from the Massachusetts Institute of Technology; Dr. Katja A. Lamia from The Scripps Research Institute; Dr. Lucia E. Rameh from Boston University School of Medicine; Dr. Atsuo T. Sasaki from the University of Cincinnati College of Medicine; Dr. Jiaxi Song, Dr. Victoria Brown, and Dr. Sabina Signoretti from Dr. Dana-Farber Cancer Institute.
Weill Cornell Medical College
Weill Cornell Medical College, Cornell University's medical school located in New York City, is committed to excellence in research, teaching, patient care and the advancement of the art and science of medicine, locally, nationally and globally. Physicians and scientists of Weill Cornell Medical College are engaged in cutting-edge research from bench to bedside, aimed at unlocking mysteries of the human body in health and sickness and toward developing new treatments and prevention strategies. In its commitment to global health and education, Weill Cornell has a strong presence in places such as Qatar, Tanzania, Haiti, Brazil, Austria and Turkey. Through the historic Weill Cornell Medical College in Qatar, the Medical College is the first in the U.S. to offer its M.D. degree overseas. Weill Cornell is the birthplace of many medical advances including the development of the Pap test for cervical cancer, the synthesis of penicillin, the first successful embryo-biopsy pregnancy and birth in the U.S., the first clinical trial of gene therapy for Parkinson's disease, and most recently, the world's first successful use of deep brain stimulation to treat a minimally conscious brain-injured patient. Weill Cornell Medical College is affiliated with NewYork-Presbyterian Hospital, where its faculty provides comprehensive patient care at NewYork-Presbyterian Hospital/Weill Cornell Medical Center. The Medical College is also affiliated with Houston Methodist. For more information, visit weill.cornell.edu.
Office of External Affairs
Weill Cornell Medical College
tel: 646.317.7401
email: pr@med.cornell.edu
Follow WCMC on Twitter and Facebook
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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.
Everyone is already all over this whole 3D printing thing. But 3D painting? It's a much emptier field. GE is experimenting with such a technology called "cold spray" that slowly builds up layers of metal by spraying metal powder at extremely high velocities. Instead of recreating works of art, the process is used to repair worn metal components, adding years or potentially decades to their life span. Unlike 3D printing which is severely limited in the size of the objects it can create, 3D painting is only limited by the spread of its spray. That means it could potentially be used to create or repair large structures, and not just prototype scale models of them. In particular, the process is being looked at as a way to repair parts used in oil and gas drilling. It could even be done on the scene and, unlike welding, there's no heat involved -- so there's very little chance for a fire or explosion. (And who wouldn't like to make our gas and oil wells safer.) For a quick demo of the process, check out the video after the break.
FILE - In this Oct. 30, 2013, file photo, President Barack Obama speaks at Boston's historic Faneuil Hall about the federal health care law. Obama says he's sorry Americans are losing health insurance plans he repeatedly said they could keep under his signature health care law. But the president stopped short of apologizing for making those promises in the first place. "I am sorry that they are finding themselves in this situation based on assurances they got from me," he said in an interview Thursday, Nov. 7 with NBC News. (AP Photo/Stephan Savoia, File)
FILE - In this Oct. 30, 2013, file photo, President Barack Obama speaks at Boston's historic Faneuil Hall about the federal health care law. Obama says he's sorry Americans are losing health insurance plans he repeatedly said they could keep under his signature health care law. But the president stopped short of apologizing for making those promises in the first place. "I am sorry that they are finding themselves in this situation based on assurances they got from me," he said in an interview Thursday, Nov. 7 with NBC News. (AP Photo/Stephan Savoia, File)
WASHINGTON (AP) — President Barack Obama says he's sorry Americans are losing health insurance plans he repeatedly said they could keep under his signature health care law. But the president stopped short of apologizing for making those promises in the first place.
"I am sorry that they are finding themselves in this situation based on assurances they got from me," he said in an interview Thursday with NBC News.
He added: "We've got to work hard to make sure that they know we hear them, and we are going to do everything we can to deal with folks who find themselves in a tough position as a consequence of this."
The president's apology comes as the White House tries to combat a cascade of troubles surrounding the rollout of the health care law often referred to as "Obamacare." The healthcare.gov website that was supposed to be an easy portal for Americans to purchase insurance has been riddled by technical issues. And with at least 3.5 million Americans receiving cancellation notices from their insurance companies, there's new scrutiny aimed at the way the president tried to sell the law to the public in the first place.
Much of the focus is on the president's promise that Americans who liked their insurance coverage would be able to keep it. He repeated the line often, both as the bill was debated in Congress and after it was signed into law.
But the measure itself made that promise almost impossible to keep. It mandated that insurance coverage must meet certain standards and that policies that fell short could no longer be sold except through a grandfathering process, meaning some policies were always expected to disappear.
The White House says under those guidelines, fewer than 5 percent of Americans will have to change their coverage. But in a nation of more than 300 million people, 5 percent is about 15 million people.
Officials argue that those people being forced to change plans will end up with better coverage and that subsidies offered by the government will help offset any increased costs.
"We weren't as clear as we needed to be in terms of the changes that were taking place," Obama told NBC. "And I want to do everything we can to make sure that people are finding themselves in a good position, a better position than they were before this law happened."
The president's critics have accused him of misleading the public about changes that were coming under the law, which remains unpopular with many Americans and a target for congressional Republicans.
Obama dismissed that criticism, saying "I meant what I said" and insisting that his administration was operating in "good faith." He acknowledged that the administration "didn't do a good enough job in terms of how we crafted the law" but did not specify what changes might be made.
Sign-ups for the new health care marketplaces opened Oct. 1. People have six months to enroll before facing a penalty.
Some lawmakers — including Democrats — have called on the White House to delay the penalty or extend the enrollment period because of the website woes that have prevented many used from signing up. Obama said he remains confident that anyone who wants to buy insurance will be able to do so.
"Keep in mind that the open enrollment period, the period during which you can buy health insurance is available all the way until March 31," he said. "And we're only five weeks into it."
New version lets you use Google's IM app to send and receive texts
As promised at last week's Google+ event, the new version of Hangouts capable of sending and receiving text messages is now rolling out through Google Play. The update to brings things up to speed with the version of Hangouts on the Nexus 5, which is the default SMS app on that device. When you first load up the updated Hangouts you'll be presented with a fullscreen message asking if you want to enable SMS support — tap yes and your messages are imported into the app, and you'll receive future SMS notifications through Hangouts instead of your preloaded SMS app. Tap "Maybe later" and things will stay as they are.
For the most part, the texting experience through Hangouts 2.0 on any other device is the same as it is on the Nexus 5 — SMS conversations are shown in a list alongside your other, and you can choose whether you want to communicate over Hangouts or SMS when starting a new conversation. Want out? At any point you can go to Settings > SMS > Turn on SMS to enable or disable SMS in Hangouts.
As usual the update is being rolled out gradually across the Android user base, so don't be surprised if you don't see it immediately. If you're updating today, be sure to hit the comments and let us know whether you're opting into SMS in Hangouts or not.
What are the most striking features of the new version of Office Web Apps? The ones that aren't there.
It isn't the fact that the Save button has been nixed (shades of Google Docs!) or that multiple users can edit the same document in real time and not stomp all over each other's work. It's how little -- as opposed to how much -- variation there is between OWA and its desktop counterparts.
That small margin makes a big difference.
Better collaborative editing than the desktop Tony Bradley at PCWorld covers in detail all the new goodies in OWA, which still consists only of Word, Excel, and PowerPoint. The biggest is simultaneous co-authoring: Many users can log into OWA, open the same document, and work on it simultaneously. Flags within the document tell you where each user is.
One particularly smart touch here is how Microsoft has set different levels of editing granularity for each document type. For Word, it's a paragraph; for Excel, it's a cell; for PowerPoint, it's a slide. They're good commonsense defaults, and in my conversation with Microsoft's people, they hinted at the possibility that it could be made even more fine-grained.
From a practical standpoint, it's unlikely two people will attempt to edit the same sentence at once. But if Microsoft can nudge the line of thinking a smidge further in that direction, it's a sign of how completely Web apps could be able to eclipse their desktop cousins. For one, the desktop versions of these apps don't have anything like the simultaneous-editing features found in OWA -- a case where the Web app actually sports a feature superior to the desktop app.
This brings up the first of two big questions about OWA. Do Web apps need to displace their desktop counterparts?
The answer may be different depending on whether you're asking Microsoft or end-users. End-users may enjoy the convenience of OWA, but there comes a point where OWA simply can't deliver. The longer and more complex the document, the greater the odds OWA -- or your browser -- will simply gag.
There's little question that Microsoft needs to create a product portfolio off the desktop that's as valuable and rich as the one the company has created on it. But I doubt it can move people off desktop editions of Office and into OWA anytime soon, and not just because OWA's feature set is lacking.
One of the most powerful typhoons ever recorded slammed into the Philippines early Friday, and one weather expert warned, "There will be catastrophic damage."
The U.S. Navy's Joint Typhoon Warning Center shortly before Typhoon Haiyan's landfall said its maximum sustained winds were 314 kilometers per hour (195 mph), with gusts up to 379 kilometers per hour (235 mph).
"195-mile-per-hour winds, there aren't too many buildings constructed that can withstand that kind of wind," said Jeff Masters, a former hurricane meteorologist who is meteorology director at the private firm Weather Underground.
Masters said the storm had been poised to be the strongest tropical cyclone ever recorded at landfall. He warned of catastrophic damage.
Local authorities reported having troubles reaching colleagues in the landfall area.
The local weather bureau had a lower reading on the storm's power, saying its speed at landfall in Eastern Samar province's Guiuan township had sustained winds at 235 kilometers (147 miles) per hour, with gusts of 275 kph (170 mph). The bureau takes measures based on longer periods of time.
Authorities in Guiuan could not immediately be reached for word of any deaths or damage, regional civil defense chief Rey Gozon told DZBB radio. Forecaster Mario Palafox with the national weather bureau said it had lost contact with its staff in the landfall area.
The storm was not expected to directly hit the flood-prone capital, Manila, further north.
The National Disaster Risk Reduction and Management Council said more than 125,000 people had been evacuated from towns and villages in the typhoon's path.
Typhoon Haiyan's wind strength at landfall had been expected to beat out Hurricane Camille, which was 305 kilometers per hour (190 mph) at landfall in the United States 1969, Masters said.
The only tiny bright side is that it's a fast-moving storm, so flooding from heavy rain — which usually causes the most deaths from typhoons in the Philippines — may not be as bad, Masters said.
"The wind damage should be the most extreme in Phillipines history," he said.
The storm later will be a threat to both Vietnam and Laos and is likely to be among the top five natural disasters for those two countries, Masters said. The storm is forecast to barrel through the Philippines' central region Friday and Saturday before blowing toward the South China Sea over the weekend, heading toward Vietnam.
President Benigno Aquino III on Thursday warned people to leave high-risk areas, including 100 coastal communities where forecasters said the storm surge could reach up to 7 meters (23 feet). He urged seafarers to stay in port.
Aquino ordered officials to aim for zero casualties, a goal often not met in an archipelago lashed by about 20 tropical storms each year, most of them deadly and destructive. Haiyan is the 24th such storm to hit the Philippines this year.
The president also assured the public of war-like preparations: three C-130 air force cargo planes and 32 military helicopters and planes on standby, along with 20 navy ships.
"No typhoon can bring Filipinos to their knees if we'll be united," he said in a televised address.
———
Associated Press writers Oliver Teves and Teresa Cerojano in the Philippines and Seth Borenstein in Washington contributed to this report.
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