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Swine flu - everything you need to know

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Posted on : 10:46 PM | By : Biochemistry Den | In : , , , , , ,

The number of cases of swine flu in England continued to fall last week (week ending 9 August). The Health Protection Agency (HPA) estimates there were 25,000 new cases of swine flu in England last week, compared with 30,000 the week before and 100,000 the week before that. Cases of swine flu have fallen in all regions and among all age groups.

The disease is generally mild in most people so far, but is proving severe in a small minority of cases. So far 371 people have been hospitalised in England, while 44 people have died.

Swine flu vaccine

The government has announced that priority for the swine flu vaccine will be given to at-risk groups. These include pregnant women and people with serious underlying health conditions.

Vaccinations for these groups are expected to begin in the autumn. Steps are being taken to extend the vaccination programme to other people once this stage has been completed.

Swine flu - treatment and prevention

If you are in England, you can get antivirals to treat swine flu from a local collection point without seeing your GP. If you are in Scotland, Wales or Northern Ireland, contact your GP or specific helpline. Reduce your risk of catching swine flu by following good hand hygiene – CATCH IT, BIN IT, KILL IT. Antiviral drugs - Tamiflu and Relenza

Swine flu is being treated with antiviral drugs such as Tamiflu and Relenza. Antiviral drugs work by preventing the flu virus from reproducing - to be effective you need to take them within 48 hours of the symptoms beginning. This can reduce the risk of complications and possibly shorten the illness by a day.

If the National Pandemic Flu Service or your GP confirm you have swine flu, you will be told where your nearest antiviral collection point is so your 'flu friend' - a friend or relative who does not have swine flu - can pick up antiviral drugs for you

What Is Swine Flu? How Is Swine Flu Treated?

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Posted on : 2:10 AM | By : Biochemistry Den | In : , , , , , ,

Swine flu (swine influenza) is a disease of pigs. It is a highly contagious respiratory disease caused by one of many Influenza A viruses. Approximately 1% to 4% of pigs that get swine flu die from it. It is spread among pigs by direct and indirect contact, aerosols, and from pigs that are infected but do not have symptoms. In many parts of the world pigs are vaccinated against swine flu.
Most commonly, swine flu is of the H1N1 influenza subtype. However, they can sometimes come from the other types, such as H1N2, H3N1, and H3N2.
The current outbreak of swine flu that has infected humans is of the H1N1 type - this type is not as dangerous as some others.

Avian Influenza (Bird Flu) can also infect pigs

Avian flu and human seasonal flu viruses can infect pigs, as well as swine influenza. The H3N2 influenza virus subtype, a virulent one, is thought to have come from pigs - it went on to infect humans.
It is possible for pigs to be infected with more than one flu virus subtype simultaneously. When this happens the genes of the viruses have the opportunity to mingle. When different flu subtypes mix they can create a new virus which contains the genes from several sources - a reassortant virus.

Although swine influenza tends to just infect pigs, they can, and sometimes do, jump the species barrier and infect humans.

What is the risk for human health?

Outbreaks of human infection from a virus which came from pigs (swine influenza) do happen and are sometimes reported. Symptoms will generally be similar to seasonal human influenzas - this can range from mild or no symptoms at all, to severe and possibly fatal pneumonia.
As swine flu symptoms are similar to typical human seasonal flu symptoms, and other upper respiratory tract infections, detection of swine flu in humans often does not happen, and when it does it is usually purely by chance through seasonal influenza surveillance. If symptoms are mild it is extremely unlikely that any connection to swine influenza is found - even if it is there. In other words, unless the doctors and experts are specifically looking for swine flu, it is rarely detected. Because of this, we really do not know what the true human infection rate is.

Examples of known swine flu infecting humans

Since the World Health Organization's (WHO's) implementation of IHR (2005) in 2007, they have been notified of swine influenza cases from the USA and Spain.
In March/April 2009 human cases of influenza A swine fever (H1N1) were first reported in California and Texas. Later other states also reported cases. A significant number of human cases during the same period have also been reported in Mexico - starting just in Mexico City, but now throughout various parts of the country. More cases are being reported in Canada, Europe, and New Zealand - mainly from people who have been in Mexico.

How does a human catch swine influenza?

  • From contact with infected pigs (most common way)
  • From contact with infected humans (much less common way)

In cases when humans have infected other humans close contact was necessary with the infected person, and they nearly always occurred in closed groups of people.

Can I eat pork meat and pork products?

If the pork meat and pork food products have been handled properly transmission of swine influenza to humans is not possible. Cooking pork meats to a temperature of 70C (160F) kills the virus. So the answer is YES, pork meat and pork food products are safe to eat.

Where have pigs been infected?

As swine influenza infection among pigs is not an internationally notifiable disease we cannot be completely sure. Swine influenza infection among pigs is known to be endemic in the USA. Outbreaks have also occurred in other parts of North America, South American, Europe, Africa, China, Japan, and other parts of Asia.

Is there a pandemic risk?

People who are not in close contact with pigs generally have no immunity to the swine influenza viruses - they are less likely to be able to prevent a virus infection. If the virus infects enough people in a given area, the risk of an influenza pandemic is significantly greater. Experts say it is very hard to predict what impact a flu pandemic caused by a swine influenza virus would have on the global human population. This would depend on how virulent the virus is, what existing immunity among humans there already is, plus several other factors.

Do we have a specific swine flu vaccine?

No - not for humans.

Will current human flu vaccines help protect people from swine influenza infection?

We really don't know. Influenza viruses are adapting and changing all the time. If a vaccine was made, it would have to be specifically for a current strain that is circulating for it to be effective. The WHO says it needs access to as many viruses as possible so that it can isolate the most appropriate candidate vaccine.

What are the signs and symptoms of swine influenza in humans?

They are similar to those of regular flu, and include:

  • Body aches
  • Chills
  • Cough
  • Diarrhea (less common)
  • Headache
  • Sore throat
  • Temperature (fever)
  • Tiredness (fatigue)
  • Vomiting (less common)

What medications are there?

There are some drugs around that can effectively treat swine flu infection in humans - and many types of flu infections in humans. There are two main types:

  • adamantanes (amantadine and remantadine)
  • inhibitors of influenza neuraminidase (oseltamivir and zanamivir)

Most previous swine influenza human cases recovered completely without the need for medical attention.

What can I do to protect myself?

  • Wash your hands regularly with soap
  • Try to stay healthy
  • Get plenty of sleep
  • Do plenty of exercise
  • Try to manage your stress
  • Drink plenty of liquids
  • Eat a well balanced diet
  • Refrain from touching surfaces which may have the virus
  • Do not get close to people who are sick
  • Stay away from crowded areas if there is a swine flu outbreak in your area

If I am infected, how can I stop others from becoming infected?

  • Limit your contact with other people
  • Do not go to work or school
  • When you cough or sneeze cover your mouth with a tissue. If you do not have a tissue, cover your mouth and nose.
  • Put your used tissues in a waste basket
  • Wash your hands and face regularly
  • Keep all surfaces you have touched clean
  • Follow your doctor's instructions

Mexico City - Some good news

In Mexico City, where a sizeable number of people have become infected with H1N1 swine flu, authorities are urging people with flu symptoms to go straight to their doctors or a local hospital. They insist that the flu is completely treatable if the patient comes in straight away.

What is Swine Flu - Video

The Centers for Disease Control and Prevention (CDC) Influenza Division has produced a video all about swine flu.
This video includes information on the signs and symptoms of swine flu, how swine flu is transmitted, what medicines are available to treat it and steps that people can take to help protect themselves from it. There are also some tips on what to do if you become ill with swine flu.

Map of Swine Flu Outbreaks

If you would like to keep up-to-date with the locations of the latest outbreaks of H1N1, see the map of swine flu outbreaks.

Glucose Intolerance In Animals Reversed By Carnitine Supplements

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Posted on : 2:00 AM | By : Biochemistry Den | In : , , , , , , , , ,

Supplementing obese rats with the nutrient carnitine helps the animals to clear the extra sugar in their blood, something they had trouble doing on their own, researchers at Duke University Medical Center report.

A team led by Deborah Muoio (Moo-ee-oo), Ph.D., of the Duke Sarah W. Stedman Nutrition and Metabolism Center, also performed tests on human muscle cells that showed supplementing with carnitine might help older people with prediabetes, diabetes, and other disorders that make glucose (sugar) metabolism difficult.

Carnitine is made in the liver and recycled by the kidney, but in some cases when this is insufficient, dietary carnitine from red meat and other animal foods can compensate for the shortfall.

After just eight weeks of supplementation with carnitine, the obese rats restored their cells' fuel- burning capacity (which was shut down by a lack of natural carnitine) and improved their glucose tolerance, a health outcome that indicates a lower risk of diabetes.

These results offer hope for a new therapeutic option for people with glucose intolerance, older people, people with kidney disease, and those with type 2 diabetes (what used to be called adult-onset diabetes).

Muoio said that soon her team of researchers will begin a small clinical trial of carnitine supplementation in people who fit the profile of those who might benefit from additional carnitine - older people (60 to 80 years) with glucose intolerance.

The study is published in the Aug. 21 issue of the Journal of Biological Chemistry.
The Duke researchers began studying carnitine more closely when abnormalities in the nutrient emerged from blood chemistry profiles of obese and old animals. These chemical profiles report on hundreds of byproducts of cell metabolism called metabolites and give scientists an opportunity to identify markers of disease states.

Carnitine is a natural compound known for helping fatty acids enter the mitochondria, the powerhouses of cells, where fatty acids are "burned" to give cells energy for their various tasks. Carnitine also helps move excess fuel from cells into the circulating blood, which then redistributes this energy source to needier organs or to the kidneys for removal. These processes occur through the formation of acylcarnitine molecules, energy molecules that can cross membrane barriers that encase all cells.

Researchers at Duke had observed that skeletal muscle of obese rats produced high amounts of the acylcarnitines, which requires free carnitine. As these molecules started to accumulate, the availability of free, unprocessed carnitine decreased. This imbalance was linked to fuel-burning problems, that is, impairments in the cells' combustion of both fat and glucose fuel.

"We suspected that persistent increases in acylcarnitines in the rats were causing problems, and we could also see that the availability of free carnitine was decreasing with weight gain and aging," said Muoio. "It appeared that carnitine could no longer do its job when chronic metabolic disruptions were stressing the system. That's when we designed an experiment to add extra carnitine to the rats' diet."

Muoio is also a professor in the departments of medicine, pharmacology and cancer biology.
Other study authors included Robert C. Noland, Sarah E. Seiler, Helen Lum, Olga Ilkayeva, Robert Stevens, and Timothy R. Koves of the Sarah W. Stedman Nutrition and Metabolism Center. Koves is also with the Duke Department of Medicine. Robert M. Lust is with the Department of Physiology at East Carolina University in Greenville, N.C., and Fausto G. Hegardt is with the CIBER division Fisiopatología de la Obesidad y la Nutrición of the Instituto de Salud Carlos III in Spain.

The work was supported by grants from the National Institutes of Health, and the American Diabetes Association, and a John A. Hartford Duke Center for Excellence Award.

Source:
Mary Jane Gore
Duke University Medical Center

The Sperm Cell – Reproductive cell

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Posted on : 6:11 PM | By : Biochemistry Den | In : , , , , , ,

Contrary to belief babies really don’t come from storks. I think we all pretty much know where babies come from. But do we really? To put it in perspective you need a sperm cell and an egg to make a baby.

During sexual intercourse, a mans sperm, which is produced by the testicles travels to the woman’s cervix, it then travels to the fallopian tubes. There are millions of sperm cells swimming to the fallopian tubes but it only takes one to penetrate an egg which is called fertilization. At this point a single life begins.

The question now is where does the sperm come from? Millions of sperm are produced daily by the testicles. Sperm cells undergo natural cell division which leads to its maturation. Half of the sperm cells carry the Y and X chromosome. Y comes from your dad and X comes from your mom. If a Y fertilizes an egg there will be a baby girl and X would be a baby boy.

During ejaculation, sperm goes into the mans vas deferens where fructose, seminal fluids, and other chemicals are secreted. Your sperm and other seminal fluids rush past the bladder through the urethra and out the penis.

Three things are needed for the sperm to enter the woman’s cervix. You need to have an erection, orgasm and ejaculation. Erections take place when the penis is stimulated or when erotic thoughts come into your mind. There is a sudden rush of blood to the erectile tissue chambers in the penis. With all this the penis engorges, making the penis hard, enlarged and elevated.

You need continued stimulation to achieve orgasm and ejaculation. Orgasm is the sexual climax. It is a pleasurable emotional or psychological response that accompanies ejaculation. In a man there are two stages to an orgasm. The first one is ejaculatory inevitability. This take place just second before you ejaculate. You know that you are about to ejaculate and at this point there is no turning back. Your seminal vesicles and your prostate gland begin to throb. The second stage of orgasm is when you involuntarily ejaculate semen in convulsive surges. On average a teaspoon of sperm contains any where between 40 to 150 million sperm.

Now that you have achieved orgasm as a man you have to go through a recovery period. Through out this recovery period you cannot experience another orgasm. This recovery period varies for different men. It can range anywhere from minutes to hours.

Dale has been married for 20 years and studies topics of this sort. You can check out some of his ever growing blogs at http://relationshiptidbits.blogspot.com/ or http://stcajo-readshortstories.blogspot.com/ and http://fishingtutor.blogspot.com/

Cellular maturity and apoptosis in human sperm: creatine kinase, caspase-3 and Bcl-XL leve

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Posted on : 6:08 PM | By : Biochemistry Den | In : , , , , , , , ,

The relationship between human sperm maturity and apoptosis is of interest because of the persistence of immature sperm in ejaculates in spite of various apoptotic processes during spermatogenesis. We assessed sperm maturity by HspA2 chaperone levels, and plasma membrane maturity by sperm binding to immobilized hyaluronic acid (HA). We also utilized objective morphometry.

Sperm were stained with three antibody combinations: active caspase-3/creatine kinase (CK, a marker of cytoplasmic retention), caspase-3/the antiapoptotic Bcl-(XL), and CK/Bcl-(XL). In semen, 13% of sperm stained with CK, caspase-3 or Bcl-(XL), and 28% had stained with two markers.

In the mature HA-bound sperm fraction, <4% were single- or double-stained. Regarding sperm regions, CK staining, whether alone or as double staining, occurred in the head and midpiece (15-20%), whereas caspase-3 and Bcl-(XL) were primarily (>80% of sperm) in the midpiece.

Morphometrical attributes of clear, single- and double-stained sperm, in line with their more pronounced maturation arrest, showed an incremental increase in head size (due to cytoplasmic retention) and shorter tail length. We hypothesize that during faulty sperm development, three alternatives may occur: (i) elimination of aberrant germ cells by apoptosis; (ii) in surviving immature cells, caspase-3 is activated, and in response the antiapoptotic Bcl-(XL), and perhaps HspA2, provide protection; (iii) in a third type of immature sperm, in addition to the CK, caspase-3 and Bcl-(XL) expression, there are related manifestations of increased head size and shorter tail length.

Thus, immature sperm may vary in the type of developmental arrest and in protection mechanisms for apoptosis. These variations are likely to explain the persistence of immature sperm in the ejaculate.

Sperm Cell Development and Motility Linked To The Presence of Protein MIF

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Posted on : 6:07 PM | By : Biochemistry Den | In : , , , , , , ,

New evidence is helping to confirm what many fertility doctors already knew; That the health and quality of a man's sperm cells are one of the biggest components to successfully conceiving.

The health of a man's sperm is so important because it truly is survival of the fittest. You have thousands of sperm cells competing for the chance to penetrate and fertilize the female egg. Compound this fact with the numerous variables that stand in the sperm cells way and you have an extremely difficult mission. The factors that dictate your success as well as your fertility rate are outlined in greater detail in the next section.

Factors of Importance-The Battle of Conception

First the environment of the female reproductive system is very acidic, and in order for the sperm cells to survive in this environment long enough to find the female egg they need a protective barrier. This protective barrier is the seminal fluid which contains the sperm cells. It not only acts as a barrier but also acts as a fuel on which the sperm cells feed off of. So in order to have strong and healthy sperm cells you also need a healthy dose of semen.

Next the sperm cells themselves must be of high quality with key traits like motility and mobility. What this means is that the sperm cells should show signs of being strong swimmers and the ability to swim in a forward motion. There should also be few signs of sperm abnormalities including: low sperm count low semen volume, poor swimming ability, crooked tails and malformed sperm cells and the presence of a large number of dead sperm cells.

What researchers have recently found is a correlation between the health and quality of a man's sperm cell and the presence of a particular protein that is found in the immune system. This protein was crucial to the continued strength and health of the sperm cells because it helped increase the sperms motility. Again what this confirms is the importance of a healthy body and the role that key amino acids (the building blocks of protein), nutrients, vitamins and minerals have in the health of the male sexual health system.

If you ensure that your body is receiving enough of these key elements as part of your diet then you are on your way to maintaining a healthy fertility level with healthy sperm cells. If you are unsure as to whether you are receiving the adequate nutrients adding a specially formulated supplement will help.

To read more about the latest on the protein MIF and the role it plays in the male reproductive system or to learn more about all natural supplements designed just for the male reproductive system please visit Sperm Cell Development Based on Protein MIF

Bacteria Pack Their Own Demise

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Posted on : 2:38 AM | By : Biochemistry Den | In : , , ,

Numerous pathogens contain an 'internal time bomb', a deadly mechanism that can be used against them. After years of work, VIB researchers at the Vrije Universiteit Brussel (VUB) were able to determine the structure and operating mechanism of the proteins involved. This clears the road for finding ways to set the clock on this internal time bomb and, hopefully, in the process developing a new class of antibiotics. The research was accepted for publication by journal Molecular Cell.

It's in the genes

For years, Nathalie De Jonge, Remy Loris and their colleagues of the VIB Department of Molecular and Cellular Interactions at VUB, have applied their relentless dedication to the study of the precise structure and function of the toxin-antitoxin complex, a system that had not been the focus of much interest in the past. Only in the last couple of years the rest of the scientific world come to realize its importance and as a result the number of papers in this field has exploded.

All living creatures, people as well as bacteria, store their genetic information in the same way, i.e. in the DNA. Every human cell contains 46 neatly folded DNA strands that together measure two meters, while bacteria have to make do with around one millimetre of DNA. A piece of DNA containing the recipe for one characteristic, such as "how to make citric acid" or "how to make hair curl," is called a gene. Humans have several tens of thousands of genes.

Toxin and antitoxin

If your genetic information becomes damaged, you have a good chance of becoming ill or even dying. This is also true for bacteria, which over time developed a handy way of providing extra protection to important genes – the toxin-antitoxin (T-A) system. These T-A genes are tucked in near the genes to be protected. T-A genes contain instructions for both a toxin and its antitoxin. As long as the cell is producing both, all is well. However, if for some reason the piece of DNA where the T-A gene is located gets damaged or lost, the production of toxin and antitoxin comes to a halt and a time bomb starts ticking. Because the toxin is more stable than the antitoxin, it is broken down more slowly by the cell's clean-up mechanisms. Once the antitoxin is all gone, there is still enough toxin left to kill the bacterium. The upshot for the species is that bacteria that loses their T-A gene – and probably have sustained damage to the important genes just next to it – can no longer reproduce.

Our best-known intestinal residents, Escherichia coli bacteria, more commonly known as E.coli, have such a T-A system in five different locations in their DNA, while Mycobacterium tuberculosis bacteria even have them in 60 locations.

A difficult feat

The T-A mechanism has been known for a while, but nobody clearly understood the workings of the proteins carrying out the instructions of the T-A gene. The VIB researchers clarified in detail both the appearance of the toxin and antitoxin, the mechanism of their interaction and the forms they take while in action – a difficult feat to pull off, requiring the simultaneous use of a whole range of different technologies. One of the difficulties for instance lay in the fact that part of the antitoxin lacks a fixed structure. This formlessness keeps it from being brought into view.

Future

Now that we finally know how the time bomb functions (or more exactly, one of the time bombs, as there are several closely related T-A systems), biomedical scientists can start looking for substances to start the time bomb of pathogens ticking, i.e. substances that imitate the toxin protein, block the antitoxin protein, or disrupt the interaction between the toxin and antitoxin. In time, a new class of antibiotics might come out of it – though Nature mostly has a countermove up its sleeve against any move scientists do.

Virus Linked To Some Cases Of Common Skin Cancer

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Posted on : 2:37 AM | By : Biochemistry Den | In : , , , , ,

A virus discovered last year in a rare form of skin cancer has also been found in people with the second most common form of skin cancer among Americans, according to researchers at the Ohio State University Comprehensive Cancer Center - James Cancer Hospital and Solove Research Institute.

The researchers examined tissue samples from 58 people with squamous cell carcinoma (SCC), a highly curable form of skin cancer that is expected to affect more than 200,000 Americans this year.

They identified the virus in more than a third of the patients and in 15 percent of the tumors tested. In addition, all of the virus found in tumor cells had a mutation that could enable the viral DNA to integrate into the DNA of the host cell.

“This is indirect evidence that the virus might play a role in causing some cases of squamous cell carcinoma,” says principal investigator Amanda E. Toland, assistant professor of molecular virology, immunology and medical genetics and a researcher with the Ohio State University Comprehensive Cancer Center - James Cancer Hospital and Solove Research Institute.

The findings are published in a recent issue of the Journal of Investigative Dermatology.

The virus was first discovered in patients with Merkel cell carcinoma, a rare, aggressive skin cancer that occurs mainly in the elderly and people with a suppressed immune system. The people in the new study all had a healthy immune system.

“Originally it was thought that this virus caused only this rare skin cancer, but our findings indicate that it is a lot more prevalent than we initially thought.”

To learn if people with SCC harbored the virus, Toland, working closely with first author and graduate research associate Amy Dworkin and Ohio State pathologists O. Hans Iwenofu and Sara B. Peters, examined DNA samples from SCC tumors, from normal-appearing skin adjacent to the tumor, when available; from white blood cells, and from cells washed from the mouth.

The investigators detected the virus in 26 of 177 SCC samples, 11 of 63 adjacent-skin samples, and one sample from a mouthwash. They found no viral DNA in any of the blood samples from 57 patients. In all, 21 of 58 SCC patients, or 36 percent, tested positive for the virus.

By sequencing the viral DNA from 31 normal and tumor samples, the researchers showed that the same mutation was present in all the viruses tested from tumors, and in 60 percent of the viruses tested from adjacent healthy-looking tissue.

“That suggests that the virus may develop a mutation that causes it to integrate into host-cell DNA, and, therefore, may play a role in causing the cancer,” Toland says.

Next, Toland wants to test normal skin in healthy individuals to learn how common this virus is in people generally and to learn whether the virus actually integrates with the host DNA.

“If it proves to be a cancer-causing virus, and if it proves to be common in the general population, it might be something we should begin screening people for,” she says.

Funding from the American Cancer Society supported this research. Ohio State researchers Stephanie Y. Tseng and Dawn C. Allain were also involved in this study.


New Drug Target For Kaposi's Sarcoma

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Posted on : 2:34 AM | By : Biochemistry Den | In : , , , ,

UCSF researchers have identified a new potential drug target for the herpes virus that causes Kaposi’s sarcoma, re-opening the possibility of using the class of drugs called protease inhibitors against the full herpes family of viruses, which for 20 years has been deemed too difficult to attain.

The new drug target, which is known as a protease dimer, could serve as a model for developing new therapeutics for diseases ranging from cancer to Alzheimer’s, the researchers say. Findings are reported in the Advance Online Publication section of the Nature Chemical Biology web site.

Most current antiviral drugs target the active sites of viral proteins, where enzymes and receptors work in a lock-and-key approach to either activate or deactivate that particular protein, the researchers explained. Traditionally, drug development has focused on inhibiting that lock-and-key action to prevent the enzyme, or receptor from being effective.

Some viral enzymes known as proteases, however, including those for HIV and the herpes virus family, take the form of a dimer, or two identical halves – much like a fully opened clamshell – in their most stable state. Those proteases play an essential role in making the virus infectious, but require the two clamshell halves to bind together to be activated, according to the paper.

The HIV protease was successfully targeted for drug development in the 1980s, by blocking the active site on the surface of the dimer, but the herpes virus protease dimer has consistently eluded efforts to disrupt it at its active site, the researchers said.

The UCSF team set out to find ways to instead prevent the two halves of the dimer from connecting at that clamshell joint, to prevent it from activating. What they found was a new target on the unstable, monomer form of the protease, which responded well to a chemical inhibitor.

“If you disrupt the protein-protein interactions, you don’t need the key to a specific lock,” said Charles S. Craik, PhD, senior author on the paper and a professor of pharmaceutical chemistry in the UCSF School of Pharmacy. “Instead, we’re essentially preventing the lock from being made in the first place.”

Craik, who also led a team that identified HIV protease inhibitors in the late 1980s, said the “Nature Chemical Biology” paper validates this new site as a viable option for small-molecule drugs to treat Kaposi’s, as well as other members of this viral family.

“All known herpes virus proteases are structurally similar,” Craik explained. “The inhibitor we found knocks out not only KS, but also the cytomegalovirus protease, so the site we’ve identified here could be a target for a broad-acting inhibitor against the entire viral family.”

To their knowledge, the researchers said, this is the first small-molecule inhibitor of a herpes virus protease to not only act outside the active site, but also to select for the partially unfolded protein to keep it from forming the dimer interface.

Herpes viruses make up one of the most prevalent viral families, including eight human viruses that cause a variety of devastating illnesses, the researchers said. Those include mononucleosis (Epstein-Barr virus), shingles (Varicella zoster virus), genital herpes (herpes simplex), retinitis (cytomegalovirus) and cancer (Kaposi’s sarcoma). While therapies exist for these viruses, they often have negative side effects and are facing rising viral resistance.

In addition to validating herpes virus proteases as suitable targets, Craik said this research was also among the first to use computational design to identify and create a potential drug to target that protease interface.

Using high-throughput screening, the team screened a library of 182 compounds that it had specifically and rationally designed to mimic the protease interface. The work identified six molecules that inhibited the Kaposi’s sarcoma virus protease activity by at least 50 percent, including one that was highly potent.

That discovery potentially opens myriad opportunities for drug discovery, Craik said, by making target receptors that were biologically validated, but then deemed undruggable, more attractive. Protein-protein interactions have been researched as drug targets against a range of diseases, from certain cancers to neurodegenerative diseases. This advance could enable researchers to reconsider those targets, he said.

The lead investigator on the paper was Tina Shahian, with the Graduate Group in Biochemistry and Molecular Biology at UCSF. Co-authors were Gregory M. Lee and Ana Lazic, both in the UCSF Department of Pharmaceutical Chemistry; and Leggy A. Arnold, Priya Velusamy, Christina M. Roels and R. Kiplin Guy, all with the Department of Chemical Biology and Therapeutics at St. Jude Children’s Research Hospital, Memphis, TN.

The CMV protease expression plasmid for this work was provided by Wade Gibson, a professor in the Department of Pharmacology and Molecular Sciences at Johns Hopkins School of Medicine. The work was funded by grants from the National Institutes of Health, the American Lebanese and Syrian Associated Charities and St. Jude Children’s Research Hospital.

Wood Glue Inspired by Mussels Chemist's Glue Borrows Unique Amino Acid from Mollusk

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Posted on : 2:31 AM | By : Biochemistry Den | In : , , , , , ,

Chemists combined an exotic form of an amino acid -- used by mussels to stick to rocks -- with soy flour to make a new, high-strength adhesive. The new glue helps in manufacturing natural-looking plywood without cancer-causing chemicals such as formaldehyde.

CORVALLIS, Ore.--Many people look for natural or green products for their homes. But even something as natural-looking as wood furniture or cabinets can contain cancer-causing chemicals like formaldehyde. Now, a scientist has created a non-toxic wood adhesive. And his inspiration didn't come from the forest. It came from the Oregon coast.

Pounding waves are no match for the mighty mussel, that produces strong, flexible threads that cling to rocks. This small shellfish inspired a big idea for wood chemist Kaichang Li.

"This thing is really amazing," Li, of Oregon State University in Corvallis, tells DBIS. He noticed mussels secrete a unique amino acid called dihydroxyphenylalanine. He found a way to add that amino acid to soy flour -- a product that's rich in protein, plentiful and non-toxic.

"Now the soy protein becomes a really good, very strong adhesive," Li says, wood glue so strong that plywood made with it stays stuck even after hours of boiling.

Oregon State University licensed the new glue to a plywood manufacturer who then sells the wood to furniture and cabinet makers.

Rick Fields, President of Neil Kelly Cabinets in Portland, Ore., says: "We're very excited about it. It's going to add a whole new dimension to our green and healthy approach to cabinet making." He is confident the new glue is safer for customers and says it shouldn't add to the cost of the cabinets.

BACKGROUND: Researchers have developed a new group of adhesives for wood products inspired by the ability of mussels to cling to rocks using thread-like tentacles. These threads are proteins that retain powerful adhesive properties even in water. By adding these amino acids to more common proteins, like soy flour, the scientists have produced new wood adhesives. The researchers are also exploring ways to create new adhesives from tree bark or decayed wood.

ADVANTAGES: The new wood adhesives are natural and environmentally friendly, unlike the formaldehyde-based adhesives currently used to make some wood products, especially plywood, particleboard, and laminated veneers. They are also stronger and more water resistant.

USES: The new glue is being used to make environmentally friendly particle board-the main wood used to make kitchen cabinets and other wood products. They may replace the formaldehyde-based wood adhesives currently used to make some wood composite products such as plywood, particleboard, and laminated veneer lumber products.

WHAT IS BIOMIMICRY? Biomimicry is a field in which scientists, engineers, and even architects study models and concepts found in nature, and try to use them to design new technologies. Here are some well-known examples of biomimicry:

  • Velcro was inspired by cockleburs, which cling tenaciously to clothing and animal fur.
  • The design for the Eastgate Building in Harare, Zimbabwe -- the country's largest commercial and shopping complex -- is based on the region's termite mounds.
  • Both Leonardo da Vinci and the Wright brothers studied the flight of birds when designing their flying machines.
  • Alexander Graham Bell designed his telephone receiver around the principles of the human ear.
  • Sonar was inspired by how whales, dolphins and bats emit high-pitched sounds and analyze the returning echoes to help them navigate.

WHERE IT'S BEING SOLD: Columbia Forest Products of Portland, the nation's largest producer of decorative plywood, has exclusive rights to use the glue in plywood.

Little-known Protein Found To Be Key Player in Building and Maintaining Healthy Cells

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Posted on : 2:28 AM | By : Biochemistry Den | In : , , , , , , ,

Italian and U.S. biologists have report that a little-understood protein previously implicated in a rare genetic disorder plays an unexpected and critical role in building and maintaining healthy cells. Even more surprising, their report in the journal Nature shows that the protein, called "atlastin," does its work by fusing intracellular membranes in a previously undocumented way.


"If you'd asked me a year ago whether this was possible, I would have said, 'No,'" said study co-author James McNew, associate professor of biochemistry and cell biology at Rice University. "In fact, that's exactly what I told (co-author) Andrea Daga when we first spoke about the idea a year ago."

McNew has spent the past 15 years studying SNARE proteins, a specialized family of proteins that carries out membrane fusion. It's a vital process that happens thousands of times a second in every cell of our bodies.

"It is fitting that the discovery of a new protein capable of fusing membranes comes 10 years after the demonstration that SNAREs can fuse lipid bilayers," said Daga, a researcher at the Eugenio Medea Scientific Institute in Conegliano, Italy.

In the new study, Daga's and McNew's research teams used fruit flies to study how atlastin functions. The atlastin in fruit flies is very similar to the human version of the protein and serves the same function.

"Prior to this, there were only two defined ways in which you could take biological membranes and put them together in a specific way," said McNew, a faculty investigator at Rice's BioScience Resesarch Collaborative. "Atlastin is the third, and it's the only one that requires enzymatic activity, so it's distinctly different."

Using a range of tests on purified proteins, live fruit flies and cell cultures, the Italian and U.S. teams examined the effect of both an overabundance and a scarcity of atlastin on cell function and on fruit fly development. They also created mutant versions of the protein to see how it functioned -- or failed to function -- when some parts were disabled.

The tests showed that cells with extra atlastin had an overdeveloped endoplasmic reticulum (ER), a system of interconnected membrane tubes and chambers that's critical for normal cell function. The tests also showed too little atlastin led to a fragmented ER. Flies with defective atlastin were sterile and short-lived.

"The endoplasmic reticulum is an ever-changing environment," McNew said. "It grows. It retracts. It expands. It collapses. It's highly dynamic, and for that to be the case, there has to be a mechanism by which it can grow new pieces and connect those pieces together. That's where the fusion comes in."

Daga said the discovery will lay the foundation for a deeper understanding of both basic biological processes and disease.

"We hope the findings lead to a better understanding of hereditary spastic paraplegia (HSP), the genetic disorder that atlastin has been linked with," Daga said.

HSP is a rare genetic condition that affects fewer than one million people worldwide. It's marked by a partial paralysis of the lower extremities due to defects in the body's longest cells, the neurons that run from the spine through the legs.

Daga said atlastin's role in building and maintaining a healthy ER may help HSP researchers better understand why neurons are affected first.

"This is the first clue," Daga said. "We have the definition of what the protein does. Now we need to explore how it does that, and what it means."

Co-authors include Genny Orso, Diana Pendin, Jessica Tosetto and Andrea Martinuzzi, all of Eugenio Medea Scientific Institute; Song Liu, Tyler Moss and Joseph Faust, all of Rice; Anastasia Egorova of Consorzio Mario Negri Sud in Santa Maria Imbaro, Italy; and Massimo Micaroni, now of the University of Queensland in Brisbane, Australia.

The research was supported by the National Institutes of Health, the G. Harold and Leila Mathers Charitable Foundation, Telethon Italy, the Italian Ministry of Health and the Foundation Compagnia di San Paolo

Biochemistry e-books -1

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Posted on : 12:50 AM | By : Biochemistry Den | In : , ,

The study of the substances and chemical processes which occur in living organisms. It includes the identification and quantitative determination of the substances, studies of their structure, determining how they are synthesized and degraded in organisms, and elucidating their role in the operation of the organism.

It have many importance in daily life. Maximum biological clarifications are done by only with Biochemistry.

Few e-Text books are given in this post for your reference for students and lecturers. please use Free Download Manager.

Biochemistry e-books


1) Biochemistry 3 ed - Lippincott ---- Download

2) Oxford_dictionary _of _biochemistry-revised ---- Download

3) Lipid Biochemistry-An Introduction --- Download

4) Protein biochemistry and proteomics --- Download

5) Dairy Chemistry and Biochemistry --- Download

6) Biochemistry Introduction Manual --- Download

7)
Biochemistry The Molecular Basis of Life - Trudy McKee, James R McKee --- Download

8) Biochemistry Complete Guide --- Download

9) Biochemistry Berg, Tymoczkao & Stryer 5th Edn --- Download

10) Biochemistry kaplana 2004 --- Download

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