Posts about cell

Looking Inside Living Cells

Johns Hopkins’ molecular biologist Jin Zhang explains how she uses light to see where and when within cells specific molecular processes occur and what happens when they go wrong.

Related: How Lysozyme Protein in Our Tear-Drops Kill BacteriaScience Explained: How Cells React to Invading VirusesNobel Prize in Physiology or Medicine 2012 for Reprogramming Cells to be PluripotentWebcast Exploring Eukaryotic Cells

Science Explained: How Cells React to Invading Viruses

This illustrated webcast introduces the microscopic arsenal of weapons and warriors that play a role in the battle for your health.

TED education has been putting out some good videos which is a wonderful thing to see. It is wonderful to let people everywhere (kids and adults) that are interested in learning (and that have internet access) can learn about the world around us. Traditional educational institutions have not done much with this opportunity to broaden their impact.

The video looks at the cells reaction to a virus infiltrating the cell.

Related: Cells AliveScience Explained: Cool Video of ATP Synthase, Which Provides Usable Energy to UsThis webcast is packed with information on the makeup and function of eukaryotic (animal) cellsCool Animation of a Virus Invading a Person’s BodyCell Aging and Limits Due to TelomeresWebcast of a T-cell Killing a Cancerous Cell

Cell Aging and Limits Due to Telomeres

When cells divide the process fails to copy DNA all the way to the end. Telomeres are are the end of DNA strands, as essentially a buffer of material that won’t cause information to be lost when part of the telomere isn’t copied. As DNA is copied, as new cells are created, the length of telomeres at the end is reduced. Once the telomeres are gone the cell will no longer divide.

The 2009 Nobel Prize in Physiology or Medicine went to 3 scientists for discovering how the chromosomes can be copied in a complete way during cell divisions and how they are protected against degradation. The Nobel Laureates have shown that the solution is to be found in the ends of the chromosomes – the telomeres – and in an enzyme that forms them – telomerase.

There is some debate over the benefit of the mechanism of cells not dividing do to lack of telomere. This can prevent cancerous cells from replicating (once they replicate to the extent that the necessary telomere buffer is gone). It is also seen that as telomeres get shorter the cells become more likely to become cancerous.

Cancer also can stimulate the production of telomerase which can stop telomeres from getting shorter as cells divide and thus allow the cancer cells to keep dividing (thus producing more cancer cell and increasing the amount of cancerous cells). Using telomerase to allow health cells to avoid the limits of division is being researched.

Are Telomeres the Key to Aging and Cancer? (University of Utah)

An enzyme named telomerase adds bases to the ends of telomeres. In young cells, telomerase keeps telomeres from wearing down too much. But as cells divide repeatedly, there is not enough telomerase, so the telomeres grow shorter and the cells age.

Cells normally can divide only about 50 to 70 times, with telomeres getting progressively shorter until the cells become senescent, die or sustain genetic damage that can cause cancer.

shorter telomeres are associated with shorter lives. Among people older than 60, those with shorter telomeres were three times more likely to die from heart disease and eight times more likely to die from infectious disease.

While telomere shortening has been linked to the aging process, it is not yet known whether shorter telomeres are just a sign of aging – like gray hair – or actually contribute to aging.

Related: The Naked Mole Rat is the Only Known Cancerless AnimalWebcast of a T-cell Killing a Cancerous CellRNA interference webcast

Cancer Cells in Blind Mole Rats ‘commit suicide’

Cancer cells in blind mole rats ‘commit suicide’

Blind mole rats don’t get cancer, and geneticists have worked out why — their cells kill themselves with a poisonous protein when they multiply too much.

Blind mole rats, which live in underground burrows throughout Southern and Eastern Africa, and the Middle East, are fascinating creatures. The naked mole rat, in particular, is the only cold-blooded mammal known to man, doesn’t experience pain, and is also arguably the only mammal (along with the Damaraland mole rat) to demonstrate eusociality — that is, they live in large hierarchical communities with a queen and workers, like ants or bees.

They’re also cancer-proof, which was found in 2011 to be down to a gene that stops cancerous cells from forming. The same team thought that two other cancer-proof mole rat species might have similar genes, but instead it turns out that they do develop cancerous cells — it’s just that those cells are programmed to destroy themselves if they become dangerous.

Very interesting research. The results of evolution are amazing. And while turning the medical research discoveries into workable treatments for people is very difficult the continued increase in our knowledge helps us find treatments that work.

Related: Webcast of a T-cell Killing a Cancerous CellSynthetic Biologists Design a Gene that Forces Cancer Cells to Commit Suicide

Evolution Follows a Predictable Genetic Pattern

Far from random, evolution follows a predictable genetic pattern

The researchers carried out a survey of DNA sequences from 29 distantly related insect species, the largest sample of organisms yet examined for a single evolutionary trait. Fourteen of these species have evolved a nearly identical characteristic due to one external influence — they feed on plants that produce cardenolides, a class of steroid-like cardiotoxins that are a natural defense for plants such as milkweed and dogbane.

Though separated by 300 million years of evolution, these diverse insects — which include beetles, butterflies and aphids — experienced changes to a key protein called sodium-potassium adenosine triphosphatase, or the sodium-potassium pump, which regulates a cell’s crucial sodium-to-potassium ratio. The protein in these insects eventually evolved a resistance to cardenolides, which usually cripple the protein’s ability to “pump” potassium into cells and excess sodium out.

Andolfatto and his co-authors examined the sodium-potassium pump protein because of its well-known sensitivity to cardenolides. In order to function properly in a wide variety of physiological contexts, cells must be able to control levels of potassium and sodium. Situated on the cell membrane, the protein generates a desired potassium to sodium ratio by “pumping” three sodium atoms out of the cell for every two potassium atoms it brings in.

Cardenolides disrupt the exchange of potassium and sodium, essentially shutting down the protein, Andolfatto said. The human genome contains four copies of the pump protein, and it is a candidate gene for a number of human genetic disorders, including salt-sensitive hypertension and migraines. In addition, humans have long used low doses of cardenolides medicinally for purposes such as controlling heart arrhythmia and congestive heart failure.

Cool stuff. It makes sense to me which is nice (it is nice to get confirmation that I find what actually exists is sensible). When things that are true just seem crazy it is a bit disconcerting – like quantum mechanics. It is fun to read stuff that totally shakes up preconceived notions, but even then it is nice once I think understand it to find it sensible.

Related: All present-day Life on Earth Has A Single AncestorCambrian Explosion SongBacteriophages: The Most Common Life-Like Form on EarthMicrocosm by Carl Zimmer

Nobel Prize in Physiology or Medicine 2012 for Reprogramming Cells to be Pluripotent

The Nobel Prize in Physiology or Medicine 2012 was awarded “for the discovery that mature cells can be reprogrammed to become pluripotent.” The prize goes jointly to Sir John B. Gurdon, Gurdon Institute in Cambridge, UK and Shinya Yamanaka, Kyoto University (he is also a senior investigator at the Gladstone Institutes in the USA).

The Nobel Prize recognizes two scientists who discovered that mature, specialised cells can be reprogrammed to become immature cells capable of developing into all tissues of the body. Their findings have revolutionised our understanding of how cells and organisms develop.

John B. Gurdon discovered (in 1962) that the specialisation of cells is reversible. In a classic experiment, he replaced the immature cell nucleus in an egg cell of a frog with the nucleus from a mature intestinal cell. This modified egg cell developed into a normal tadpole. The DNA of the mature cell still had all the information needed to develop all cells in the frog.

Shinya Yamanaka discovered more than 40 years later, in 2006, how intact mature cells in mice could be reprogrammed to become immature stem cells. Surprisingly, by introducing only a few genes, he could reprogram mature cells to become pluripotent stem cells, i.e. immature cells that are able to develop into all types of cells in the body.

These groundbreaking discoveries have completely changed our view of the development and cellular specialisation. We now understand that the mature cell does not have to be confined forever to its specialised state. Textbooks have been rewritten and new research fields have been established. By reprogramming human cells, scientists have created new opportunities to study diseases and develop methods for diagnosis and therapy.

All of us developed from fertilized egg cells. During the first days after conception, the embryo consists of immature cells, each of which is capable of developing into all the cell types that form the adult organism. Such cells are called pluripotent stem cells. With further development of the embryo, these cells give rise to nerve cells, muscle cells, liver cells and all other cell types – each of them specialised to carry out a specific task in the adult body. This journey from immature to specialised cell was previously considered to be unidirectional. It was thought that the cell changes in such a way during maturation that it would no longer be possible for it to return to an immature, pluripotent stage.

Related: 2011 Nobel Prize in Physiology or MedicineNobel Prize in Physiology or Medicine 20082012 Nobel Prize in Chemistry to Robert Lefkowitz and Brian Kobilka

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2012 Nobel Prize in Chemistry to Robert Lefkowitz and Brian Kobilka

The Royal Swedish Academy of Sciences has decided to award the Nobel Prize in Chemistry for 2012 to

  • Robert J. Lefkowitz, Howard Hughes Medical Institute and Duke University Medical Center, Durham, NC, USA
  • and Brian K. Kobilka, Stanford University School of Medicine, Stanford, CA, USA

for studies of G-protein–coupled receptors.

Your body is a fine-tuned system of interactions between billions of cells. Each cell has tiny receptors that enable it to sense its environment, so it can adapt to new situtations. Robert Lefkowitz and Brian Kobilka are awarded the 2012 Nobel Prize in Chemistry for groundbreaking discoveries that reveal the inner workings of an important family of such receptors: G-protein–coupled receptors.

For a long time, it remained a mystery how cells could sense their environment. Scientists knew that hormones such as adrenalin had powerful effects: increasing blood pressure and making the heart beat faster. They suspected that cell surfaces contained some kind of recipient for hormones. But what these receptors actually consisted of and how they worked remained obscured for most of the 20th Century.

Lefkowitz started to use radioactivity in 1968 in order to trace cells’ receptors. He attached an iodine isotope to various hormones, and thanks to the radiation, he managed to unveil several receptors, among those a receptor for adrenalin: β-adrenergic receptor. His team of researchers extracted the receptor from its hiding place in the cell wall and gained an initial understanding of how it works.

The team achieved its next big step during the 1980s. The newly recruited Kobilka accepted the challenge to isolate the gene that codes for the β-adrenergic receptor from the gigantic human genome. His creative approach allowed him to attain his goal. When the researchers analyzed the gene, they discovered that the receptor was similar to one in the eye that captures light. They realized that there is a whole family of receptors that look alike and function in the same manner.

Today this family is referred to as G-protein–coupled receptors. About a thousand genes code for such receptors, for example, for light, flavour, odour, adrenalin, histamine, dopamine and serotonin. About half of all medications achieve their effect through G-protein–coupled receptors.

The studies by Lefkowitz and Kobilka are crucial for understanding how G-protein–coupled receptors function. Furthermore, in 2011, Kobilka achieved another break-through; he and his research team captured an image of the β-adrenergic receptor at the exact moment that it is activated by a hormone and sends a signal into the cell. This image is a molecular masterpiece – the result of decades of research.

Related: More details on the research2011 Nobel Prize in Chemistry2009 Nobel Prize in Chemistry: the Structure and Function of the RibosomeThe Nobel Prize in Chemistry 2008

Science Explained: Cool Video of ATP Synthase, Which Provides Usable Energy to Us

This webcast shows animations of ATP synthase structure and the mechanism for synthesizing ATP. Biology is incredibly cool. Too bad they didn’t have stuff like this when I was in school, instead biology was mainly about memorizing boring lists of stuff.

ATP (adenosine tri-phosphate) transports chemical energy within cells. When one of the phosphates is released by ATP energy is given off (and ATP becomes ADP (adenosine di-phosphate) + Pi (inorganic phosphate). And then the synthase structure can then turn it back into ATP to be used again.

The human body, which on average contains only 250 grams of ATP, turns over its own body weight equivalent in ATP each day.

Related: ATP synthase lecture notes University of IllinoisWebcast on the makeup and function of eukaryotic cellsScience Explained: PhotosynthesisVideo showing malaria breaking into cell

Exploring Eukaryotic Cells

This webcast is packed with information on the makeup and function of eukaryotic cells, which are the type of cells found in animals. It is part of a interesting series of science webcasts by Crash Course. The webcast style might be a bit too hyperactive and flippant for some but the content is quite interesting and the videos they are are of similar style and quality so if you like this one you can subscribe to their channel. They offer quite a few webcasts on science but they also offer webcasts on history.

Related: Plants, Unikonts, Excavates and SARsHow Cells AgeMidichloria mitochondrii

Cool Animation of a Virus Invading a Person’s Body

Flu Attack! How A Virus Invades Your Body

First, some new viruses get caught in mucus and other fluids inside your body and are destroyed. Other viruses get expelled in coughs and sneezes. Second, lots of those new viruses are lemons. They don’t work that well. Some don’t have the right “keys” to invade healthy cells so they can’t spread the infection. And third, as the animation shows, your immune system is busy attacking the viruses whenever and wherever possible.

That is why most of the time, after a struggle (when you get a fever and need to lie down), your immune system rebounds, and, in time, so do you.

A health body with a strong immune system is able to fight off viruses, and other health issues more easily. Also when you body has run across a specific virus before it is ready to fight it. It has cataloged that virus and is on the look out for it and is prepared to produce specialized cells to attack it. The flu vaccinations you get are priming your body to be ready to attack if that virus is found. Those antibodies take about 2 weeks to build up in sufficient numbers to offer protection against the flu. Viruses are constantly mutating which helps them evade your detectors. This stuff is so amazing. And your body is just doing this stuff every day while you watch youtube or play basketball or…

Related: Antigen Shift in Influenza VirusesLearning How Viruses Evade the Immune SystemHow to Stay Healthy: Avoiding the Flu

Webcast of a T-cell Killing a Cancerous Cell

Very cool. Very good job by University of Cambridge to make this kind of material available openly online. I find this kind of video amazing. Every day you body has this going on all day long. How amazing.

This is what it looks like when cancer gets smacked down by a T cell

This was shot by University of Cambridge medical researcher Alex Ritter, and is 92 times faster than real time.

Cells of the immune system protect the body against pathogens. If cells in our bodies are infected by viruses, or become cancerous, then killer cells of the immune system identify and destroy the affected cells. Cytotoxic T cells are very precise and efficient killers. They are able to destroy infected or cancerous cells, without destroying healthy cells surrounding them.

Related: Using Bacteria to Carry Nanoparticles Into CellsHow Cells AgeVideo showing malaria breaking into cellSynthetic Biologists Design a Gene that Forces Cancer Cells to Commit Suicide

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