Plastic Surgeon Comments on Increased Demand for Breast Augmentation

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Surgeon Comments on Demand for Breast Augmentation
    OTTAWA, ON, April 27, 2012 /24-7PressRelease/ -- Dr. Howard Silverman of Ottawa Plastic Surgery has seen a rise in the number of requests for breast augmentation in Ottawa. This reflects a similar trend in the U.S., as documented by the American Society of Plastic Surgeons (ASPS).

Recently released statistics from the ASPS show a 4% increase in breast augmentation procedures in the United States from 2010 to 2011.

"I've been seeing more breast augmentation patients at my practice because of a number of factors," Dr. Silverman says. "I attribute the increase in Ottawa, and elsewhere, partially to advancements in breast implant options and surgical techniques, which are creating more personalized results."

Dr. Silverman uses the latest in breast implant surgical techniques and offers his patients the newest in highly cohesive round gel implants, the INSPIRA line, which is part of Allergan's NATRELLE collection.

"One of the best ways to achieve beautiful and natural-looking results is to offer the latest cosmetic procedures and products available," Dr. Silverman says. "This holds true not only for breast augmentation. Patients considering procedures such as a tummy tuck in Ottawa are also discovering how new techniques can bring their cosmetic goals within reach.

In January, Dr. Silverman attended the ALLERGAN ACADEMY as part of his continued dedication to providing his patients with the latest advances and optimal care.

"The ALLERGAN ACADEMY was an excellent opportunity for me to further my knowledge of current trends," Dr. Silverman says. "I was able not only to share my experiences with other doctors but also to hear from prominent national and international speakers."

Dr. Silverman also recently travelled to Sweden to observe renowned Swedish plastic surgeon Dr. Charles Randquist, as part of Allergan's initiative to advance breast augmentation skills for top surgeons utilizing their devices.

"Whether a patient is interested in a breast enhancement procedure such as breast augmentation or body contouring after weight loss in Ottawa, it is exciting to see how numerous new advancements are helping people look and feel their best," Dr. Silverman says.

Howard Silverman, M.D. offers breast enhancement, body contouring, facial sculpting, and other types of plastic surgery in Ottawa. He also features medical spa treatments, including BOTOX Cosmetic, injectable fillers, microdermabrasion, laser skin resurfacing, laser hair removal, and laser skin rejuvenation. Dr. Silverman is a board-certified plastic surgeon and board-certified general surgeon whose training includes earning his Doctor of Medicine at the University of Toronto, an Internship in Surgery at the Toronto Hospital, a Residency and Chief Residency in Surgery at Yale University, Connecticut, and a Residency and Chief Residency in Plastic Surgery at Albany Medical College, New York.

Website: http://www.ottawaplasticsurgery.com

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Researchers Discover That Small Shape Changes Lead to Increased Protective Ability in a Disease-Related Protein

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    ASHLAND, OH, March 31, 2012 /24-7PressRelease/ -- Researchers at Ashland University, Miami University (Ohio), and the National Institutes of Health have used a novel approach to show how evolutionary changes in the protein alpha A-crystallin have altered its ability to protect other proteins from damage during periods of physiological stress.

Alpha A-crystallin is a member of the small heat shock protein family, which plays a role in the prevention of human diseases such as Alzheimer's, lens cataracts and cancer. By comparing alpha A-crystallins from six different fish species, the researchers were able to identify two small changes in the protein's structure that affected its stability and ability to buffer other proteins from stress.

"The findings provide a unique perspective on the function of these 'stress proteins' and suggest ways that they could be altered to modify their protective abilities," said lead author Dr. Mason Posner, professor of biology at Ashland University.

The work will be published in PLoS One, a premier open access online journal, on March 29, 2012.

"We have used a classic comparative biology approach to find how nature alters this small heat shock protein to function in different settings," Posner said. "Most work on these proteins focuses on individual species, and usually mammals. By using fishes as a model group, we have shown how comparing multiple species can identify small changes in protein structure with large effects on function, while still maintaining a viable molecule that does not cause disease."

Posner said "Not only does this add to our basic understanding of how small heat shock proteins work, but it validates a technique for identifying small heat shock protein modifications that could have therapeutic applications."

After cloning the gene for one specific small heat shock protein, alpha A-crystallin, from six different fish species living at temperatures from -2 to 40 degrees Celsius, the authors of this study discovered that the protective function and stability of the resulting proteins correlated with the temperature of each fish, Posner said.

Using computer modeling to compare the structures of each protein and evolutionary analysis to reconstruct the likely changes in those structures during each species' evolution, the researchers identified three amino acid changes that could account for differences in protein function.

"By genetically engineering zebrafish alpha A-crystallins with amino acid substitutions found in the Antarctic toothfish, the authors were able to show that two of these three changes alter alpha A-crystallin protective function in a predictable way," he said.

Posner said that "with one small change we were able to produce a zebrafish protein that behaved more like a cold-adapted Antarctic fish protein." While the newly published results were done in vitro, follow up studies will examine the effects of these modified proteins in a live zebrafish, he added.

Posner said additional future work will examine whether similar modifications can be used to alter human small heat shock proteins.

Two of the co-authors on this study were undergraduate research students from Ashland University, a medium sized comprehensive Masters university in Ohio with a tradition of strong undergraduate research. The study was funded by the National Eye Institute of the National Institutes of Health.

Contact Information:
Mason Posner, Professor of Biology
mposner@ashland.edu; 419-289-5691
www.masonposner.com
Article Embargoed until 3/29/2012 at 5 PM Eastern Time
Publication will be available on 3/29/2012 at: http://dx.plos.org/10.1371/journal.pone.0034438

Ashland University, ranked in the top 200 colleges and universities in U.S. News and World Report's National Universities category for 2012, is a mid-sized, private university conveniently located a short distance from Akron, Cleveland and Columbus, Ohio. Ashland University values the individual student and offers a unique educational experience that combines the challenge of strong, applied academic programs with a faculty and staff who build nurturing relationships with their students.

Website: http://www.ashland.edu

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ashland university, undergraduate research, ashland university researchers, student research, alpha a-crystallin, toothfish, alzheimer's, lens cataracts, cancer, protein structure, stress proteinsRead more Press Releases from Steve Hannan:

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Researchers Discover That Small Shape Changes Lead to Increased Protective Ability in a Disease-Related Protein

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The remote server returned an unexpected response: (417) Expectation failed.

    ASHLAND, OH, March 31, 2012 /24-7PressRelease/ -- Researchers at Ashland University, Miami University (Ohio), and the National Institutes of Health have used a novel approach to show how evolutionary changes in the protein alpha A-crystallin have altered its ability to protect other proteins from damage during periods of physiological stress.

Alpha A-crystallin is a member of the small heat shock protein family, which plays a role in the prevention of human diseases such as Alzheimer's, lens cataracts and cancer. By comparing alpha A-crystallins from six different fish species, the researchers were able to identify two small changes in the protein's structure that affected its stability and ability to buffer other proteins from stress.

"The findings provide a unique perspective on the function of these 'stress proteins' and suggest ways that they could be altered to modify their protective abilities," said lead author Dr. Mason Posner, professor of biology at Ashland University.

The work will be published in PLoS One, a premier open access online journal, on March 29, 2012.

"We have used a classic comparative biology approach to find how nature alters this small heat shock protein to function in different settings," Posner said. "Most work on these proteins focuses on individual species, and usually mammals. By using fishes as a model group, we have shown how comparing multiple species can identify small changes in protein structure with large effects on function, while still maintaining a viable molecule that does not cause disease."

Posner said "Not only does this add to our basic understanding of how small heat shock proteins work, but it validates a technique for identifying small heat shock protein modifications that could have therapeutic applications."

After cloning the gene for one specific small heat shock protein, alpha A-crystallin, from six different fish species living at temperatures from -2 to 40 degrees Celsius, the authors of this study discovered that the protective function and stability of the resulting proteins correlated with the temperature of each fish, Posner said.

Using computer modeling to compare the structures of each protein and evolutionary analysis to reconstruct the likely changes in those structures during each species' evolution, the researchers identified three amino acid changes that could account for differences in protein function.

"By genetically engineering zebrafish alpha A-crystallins with amino acid substitutions found in the Antarctic toothfish, the authors were able to show that two of these three changes alter alpha A-crystallin protective function in a predictable way," he said.

Posner said that "with one small change we were able to produce a zebrafish protein that behaved more like a cold-adapted Antarctic fish protein." While the newly published results were done in vitro, follow up studies will examine the effects of these modified proteins in a live zebrafish, he added.

Posner said additional future work will examine whether similar modifications can be used to alter human small heat shock proteins.

Two of the co-authors on this study were undergraduate research students from Ashland University, a medium sized comprehensive Masters university in Ohio with a tradition of strong undergraduate research. The study was funded by the National Eye Institute of the National Institutes of Health.

Contact Information:
Mason Posner, Professor of Biology
mposner@ashland.edu; 419-289-5691
www.masonposner.com
Article Embargoed until 3/29/2012 at 5 PM Eastern Time
Publication will be available on 3/29/2012 at: http://dx.plos.org/10.1371/journal.pone.0034438

Ashland University, ranked in the top 200 colleges and universities in U.S. News and World Report's National Universities category for 2012, is a mid-sized, private university conveniently located a short distance from Akron, Cleveland and Columbus, Ohio. Ashland University values the individual student and offers a unique educational experience that combines the challenge of strong, applied academic programs with a faculty and staff who build nurturing relationships with their students.

Website: http://www.ashland.edu

---
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Press Release Keywords:
ashland university, undergraduate research, ashland university researchers, student research, alpha a-crystallin, toothfish, alzheimer's, lens cataracts, cancer, protein structure, stress proteinsRead more Press Releases from Steve Hannan:

View the original article here