NeoStem: Understanding Research And Its Implications To Clinical Trials

On September 11, a report published in the European Heart Journal Advance Access essentially validated the workings of NeoStem's (NBS) Phase II AMR-001, or at least the approach that NeoStem is using. The report flew somewhat under-the-radar, because a few days later, a negative article on Seeking Alpha questioned AMR-001, and caused NeoStem's stock to fall drastically. As a result, I reached out to NeoStem's Chief Medical Officer and CD34+ cell specialist Dr. Douglas Losordo who clarified the controversy quite nicely and completely tore down the author's argument in this Instablog post.

However, the report in European Heart Journal was quite important to NeoStem, yet no one seemed to notice. One reason is likely because these research reports are written in a way that very few retail investors (or analysts) can understand. Therefore, once more, I reached out to the company, hoping that this seemingly positive research report can be summarized for investors to understand. Hence, here is a short Q&A with the company's PCT segment's CMO Dr. Andrew Pecora, and his take on the report.

Note: I have added a few notes (in bold) for clarification and for important points.

Nichols

How do the results of this study compare with other related studies that have released either final or interim data? From a size, safety, and efficacy point of view.

Dr. Pecora

Pretty much the same. All studies have shown that if an adequate number of CD34 cells are administered (either isolated or admixed with marrow) during the window phase after inflammation has subsided (days 5-12 post acute myocardial infarction (AMI) there is a consistent finding of increased LVEF, preservation of heart muscle function and less adverse remodeling. One study also showed significantly fewer clinical events. (Essentially, Dr. Pecora is saying that when trials are done correctly, and the threshold dose is used, the outcome is consistent, which also goes hand-in-hand with NeoStem's goal in its Phase II trial)

Nichols

Can you elaborate on the significance of this statement within the research report?

"There was no difference in LVEF improvement between patients treated with cell infusion ,7 days from primary PCI compared with =7 days (1.46%, 95% CI: 0.41 to 2.51 vs. 2.69%, 95% CI: 1.80 to 3.58, P 1/4 0.08). Furthermore, we found no difference in LVEF improvement comparing patients with number of injected mono- nuclear BMC of ,108 compared with = 108 (2.80%, 95% CI: 0.79 to 4.80 vs. 0.58%, 95% CI: 20.44 to 1.59, P 1/4 0.05), Table 2. Studies, using MRI as LV function assessment had a smaller treatment effect in LVEF when compared with non-MRI studies (0.16% 95% CI: 20.88 to 1.20 vs. 4.67%, 95% CI: 3.69 to 5.66, P, 0.001)."

Dr. Pecora

This is a meta-analysis so data of this kind will not pick up small differences and probably cannot be used to conclude this fine a point. In regard to the days post PCI we know there is no difference in effect if cells are given day 5 vs. day 8 but there is no effect if given day 3 so one would need to know how the actual day of delivery is weighted in the cut they did (the day administered is very important to outcome). There is no good correlation between the number of mononuclear cells infused which is irrelevant and the number of CD 34 cells which are a constituent of the mononuclear cells and the cells that cause the effect. In addition further confounding this analysis is that the more mononuclear cells infused the more cells there are to get in the way of the CD34 cells. MRI has less variability than standard echo and what is important is not effect size (i.e. how much the LVEF goes up) it is the percentage of patients that do not have a drop in LVEF that matters. What matters is preservation of heart muscle function (preservation of heart muscle function was shown, and is the goal of NeoStem's Phase II study).

Nichols

Can you expand on the importance of the trial size and impact it has on being able to analyze subgroup data?

Dr. Pecora

It is more than adequate for the general effect assessment and conclusion that bone marrow derived cells administered after an AMI via the coronary artery preserve heart muscle function and prevent adverse remodeling

Nichols

From an investor's perspective, what do you feel is the single most important take away from this report?

Dr. Pecora

In regard to AMR-001, in our study we are administering a much greater number of CD34 cells than prior studies and not admixed with mononuclear cells. In our study we have limited entry to patients with persistent cardiac dysfunction (LVEF <48% on day 4), which would indicate that most of our patients fall into the <40% category in this analysis (because the LVEF is taken before day 4 in these studies and tends to improve by day 4). Thus if an effect is observed in most studies used for this meta analysis than our study should result in a similar effect at minimum and could be greater because we are giving a greater number of potent cells to a sicker population.

Final Thoughts

Now, hopefully Dr. Pecora's response made this study easier to follow/understand. Unfortunately, retail investors tend not to pay attention to reports such as this, and only show interest at the end of Phase III trials when a study either "met" or "did not meet" primary and secondary endpoints. However, reports such as this can give you, as an investor, a better idea of future success, or a lack thereof. Then, you aren't as likely to respond to the daily volatility that is created with such stocks, and will feel better about your investment.

Disclosure: I am long NBS. I wrote this article myself, and it expresses my own opinions. I am not receiving compensation for it (other than from Seeking Alpha). I have no business relationship with any company whose stock is mentioned in this article. (More...)

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New understanding of actin filament growth in cells

Main Category: Biology / Biochemistry
Also Included In: Cancer / Oncology;  HIV / AIDS
Article Date: 30 Jul 2013 - 2:00 PDT Current ratings for:
New understanding of actin filament growth in cells

University of Oregon biochemists have determined how tiny synthetic molecules disrupt an important actin-related molecular machine in cells in one study and, in a second one, the crystal structure of that machine when bound to a natural inhibitor.

The accomplishments - done in the name of fundamental understanding, or basic science - provide new windows on the complexities of cellular structure and suggest a potential future route to therapeutic targeting, said Brad J. Nolen, a professor of chemistry and biochemistry at the UO, who was principal investigator on both studies.

The machinery is the actin-related protein 2/3 complex (Arp2/3), a large assembly of seven proteins that stick together. This complex is critical to cell motility - the ability to move and perform myriad duties - and for initializing the construction of a network of filaments known as the actin cytoskeleton that provides structural support for cells.

"In addition to cells having a lot of actin, they also have a lot of proteins that bind to actin to control its dynamics," said Nolen, who has just completed his second year as a Pew Scholar in the Biomedical Sciences. "And that's exactly what the complex does. It binds to the side of pre-existing actin filaments, where it nucleates the growth of new filaments. The Arp2/3 complex is very highly conserved, like actin. All of your cells are chock full of actin much like a yeast cell. There are very few differences between the molecule in yeast and in human cells."

The cell loses control of the actin cytoskeleton in various diseased states, including certain viral infections, such as HIV and cancer, he said.

Nolen, also a member of the UO's Institute of Molecular Biology, began studying the Arp2/3 complex's role in cytoskeletal network formation during postdoctoral research at Yale University, where he was part of a team that in 2009 identified two distinct classes of molecules that inhibited normal activity of the machinery. The discovery, reported in the journal Nature, opened the way for exploring how the complex works.

Reporting in a recent issue of the journal Chemistry & Biology, Nolen and a team of UO researchers, in a series of biochemical, biophysical and X-ray crystallography experiments, exposed the complex to the two tiny synthetic molecules, which turned off actin-filament initiation as anticipated. More importantly, they were able to capture exactly where the molecules docked, or bound, with the much larger macromolecular Arp2/3 complex.

That binding activity, they found, was enough to block the ability of the machinery to align properly for activating filament production. "We found that these small molecules throw a monkey wrench in this macromolecular machine and lock it into the off state," Nolen said. "By locking it into the off state it prevents it from nucleating branched filaments."

What was seen in the Arp2/3 complex, Nolen said, will help to understand precisely how actin is controlled in cells. "Cell motility requires actin inside the cell to constantly be remodeled," he said. "A lot of studies are showing that the Arp2/3 complex is very important for cell motility. So if we can figure out the Arp2/3 complex works, we can better understand how it affects things like cellular motility and, therefore, how we might affect things like metastasis of tumors.

In the second paper, placed online July 28 in advance of regular publication in the journal Nature Structural & Molecular Biology, Nolen and Quing Luan, a research technician in the UO's Institute of Molecular Biology, report the first crystal structure of the Arp2/3 complex while bound with a natural occurring inhibitor, glial maturation factor, known as GMF.

"We have determined the three-dimensional structure of all of the atoms that make up each of the sub-units of the Arp2/3 complex, and we've created a 3-D picture of where this regulator binds to the complex by using X-ray crystallography," Nolen said. "What this tells us is the structural basis for how GMF regulates the Arp2/3 complex. It binds to the complex and blocks the initiation of Y-shaped branches that create new filaments. It also binds to the pre-existing branches and causes them to pop off, so it is involved in the disassembly of these networks."

There is a difference, he noted, in how inhibitor molecules in the two studies worked. The synthetic versions in the first study, while binding to specific locations, did not block separate filament-building activators from also binding to the complex but instead stopped activation by locking the complex into a non-productive position. GMF while bound to the complex, on the other hand, blocked activators from also locking on.

The different results, Nolen said, could guide future efforts therapeutic delivery of molecules, or drugs, to fight disease-related scenarios in damaged cells. His lab is now working with a computational chemist on the design of molecules that might drive desired alterations in the complex and related actin regulators without unintended consequences of toxicity.

"We are pursuing the potential clinical value," Nolen said. "It's basic research with a potential long-term payoff, or it may never happen. For now what we've provided is a basic-science tool."

"Researchers at the University of Oregon continue to further our understanding of the dynamic processes that inform multi-level health and well-being," said Kimberly Andrews Espy, vice president for research and innovation and dean of the UO graduate school. "By helping to elucidate the complexities of cellular structure, Dr. Nolen's research may eventually lead to more effective targeting of tumors and other diseases."

Article adapted by Medical News Today from original press release. Click 'references' tab above for source.
Visit our biology / biochemistry section for the latest news on this subject.

Byron Hetrick, Min Suk Han, Luke A. Helgeson, Brad J. Nolen, Small Molecules CK-666 and CK-869 Inhibit Actin-Related Protein 2/3 Complex by Blocking an Activating Conformational Change, Chemistry & Biology, doi: 10.1016/j.chembiol.2013.03.019

Co-authors with Nolen on the Chemistry & Biology paper were postdoctoral researcher Byron Hetrick and graduate students Min Suk Han and Luke Helgeson. The National Institutes of Health (RO1-GM092917 to Nolen and F32-GM097913 to Hetrick, the lead author) and American Heart Association (10SDG2610189 to Nolen) supported the research.

The NIH (RO1-GM092917) and Pew Scholars in the Biomedical Sciences program of the Pew Charitable Trusts supported Nolen for the work in Nature Structural & Molecular Biology. Experiments were done at the Argonne National Laboratory's Advanced Photon Source, a U.S. Department of Energy-funded facility operated by the University of Chicago.

University of Oregon

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Study may advance fundamental understanding of how brain cells communicate

Main Category: Neurology / Neuroscience
Also Included In: Alzheimer's / Dementia;  Parkinson's Disease;  Muscular Dystrophy / ALS
Article Date: 29 Jul 2013 - 0:00 PDT Current ratings for:
Study may advance fundamental understanding of how brain cells communicate

Brain cells talk to each other in a variety of tones. Sometimes they speak loudly but other times struggle to be heard. For many years scientists have asked why and how brain cells change tones so frequently. National Institutes of Health researchers showed that brief bursts of chemical energy coming from rapidly moving power plants, called mitochondria, may tune brain cell communication.

"We are very excited about the findings," said Zu-Hang Sheng, Ph.D., a senior principal investigator and the chief of the Synaptic Functions Section at the NIH's National Institute of Neurological Disorders and Stroke (NINDS). "We may have answered a long-standing, fundamental question about how brain cells communicate with each other in a variety of voice tones."

The network of nerve cells throughout the body typically controls thoughts, movements and senses by sending thousands of neurotransmitters, or brain chemicals, at communication points made between the cells called synapses. Neurotransmitters are sent from tiny protrusions found on nerve cells, called presynaptic boutons. Boutons are aligned, like beads on a string, on long, thin structures called axons. They help control the strength of the signals sent by regulating the amount and manner that nerve cells release transmitters.

Mitochondria are known as the cell's power plant because they use oxygen to convert many of the chemicals cells use as food into adenosine triphosphate (ATP), the main energy that powers cells. This energy is essential for nerve cell survival and communication. Previous studies showed that mitochondria can rapidly move along axons, dancing from one bouton to another.

In this study, published in Cell Reports, Dr. Sheng and his colleagues show that these moving power plants may control the strength of the signals sent from boutons.

"This is the first demonstration that links the movement of mitochondria along axons to a wide variety of nerve cell signals sent during synaptic transmission," said Dr. Sheng.

The researchers used advanced microscopic techniques to watch mitochondria move among boutons while they released neurotransmitters. They found that boutons sent consistent signals when mitochondria were nearby.

"It's as if the presence of mitochondria causes a bouton to talk in a monotone voice," said Tao Sun, Ph.D., a researcher in Dr. Sheng's laboratory and the first author of the study.

Surprisingly, when the mitochondria were missing or moving away from boutons, the signal strength fluctuated. The results suggested that the presence of stationary power plants at synapses controls the stability of the nerve signal strength.

To test this idea further, the researchers manipulated mitochondrial movement in axons by changing levels of syntaphilin, a protein that helps anchor mitochondria to the nerve cell's skeleton found inside axons. Removal of syntaphilin resulted in faster moving mitochondria and electrical recordings from these neurons showed that the signals they sent fluctuated greatly. Conversely, elevating syntaphilin levels in nerve cells arrested mitochondrial movement and resulted in boutons that spoke in monotones by sending signals with the same strength.

"It's known that about one third of all mitochondria in axons move. Our results show that brain cell communication is tightly controlled by highly dynamic events occurring at numerous tiny cell-to-cell connection points," said Dr. Sheng.

In separate experiments the researchers watched ATP energy levels in these tiny boutons as they sent nerve messages.

"The levels fluctuated more in boutons that did not have mitochondria nearby," said Dr. Sun.

The researchers also found that blocking ATP production in mitochondria with the drug oligomycin reduced the size of the signals boutons sent even if a mitochondrial power plant was nearby.

"Our results suggest that local ATP production by nearby mitochondria is critical for consistent neurotransmitter release," said Dr. Sheng. "It appears that variability in synaptic transmission is controlled by rapidly moving mitochondria which provide brief bursts of energy to the boutons they pass through."

Problems with mitochondrial energy production and movement throughout nerve cells have been implicated in Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, and other major neurodegenerative disorders. Dr. Sheng thinks these results will ultimately help scientists understand how these problems can lead to disorders in brain cell communication.

"Our findings reveal the cellular mechanisms that tune brain communication by regulating mitochondrial mobility, thus advancing our understanding of human neurological disorders," said Dr. Sheng.

Article adapted by Medical News Today from original press release. Click 'references' tab above for source.
Visit our neurology / neuroscience section for the latest news on this subject.

Sun et al. "Motile Axonal Mitochondria Contribute to the Variability of Presynaptic Strength," Cell Reports, July 25, 2013. DOI: 10.1016/j.celrep.2013.06.040

This study was funded by the NINDS' Division of Intramural Research. For more information, please visit: http://intra.ninds.nih.gov/

NIH/National Institute of Neurological Disorders and Stroke

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New understanding of how Ebola virus suppresses the human immune system

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Understanding the strength of the mussels' underwater attachments could enable better glues and biomedical interfaces

Main Category: Medical Devices / Diagnostics
Article Date: 25 Jul 2013 - 1:00 PDT Current ratings for:
Understanding the strength of the mussels' underwater attachments could enable better glues and biomedical interfaces

Unlike barnacles, which cement themselves tightly to the surfaces of rocks, piers or ships, the clamlike bivalves called mussels dangle more loosely from these surfaces, attached by a collection of fine filaments known as byssus threads. This approach lets the creatures drift further out into the water, where they can absorb nutrients - although in the process, it exposes them to the risk of being torn away by the force of crashing waves.

But that almost never happens.

Despite the outwardly thin and fragile appearance of these threads, it turns out that in the dynamic, sloshing environment of waves and currents they can withstand impact forces that are nine times greater than the forces exerted by stretching in only one direction.

The secret to these tiny natural bungee cords has now been unraveled by MIT research scientist Zhao Qin and professor of civil and environmental engineering Markus Buehler. Their findings appear this week in the journal Nature Communications.

Byssus threads, they found, are composed of a well-designed combination of soft, stretchy material on one end and much stiffer material on the other. Both materials, despite their different mechanical properties, are made of a protein closely related to collagen, a main constituent of skin, bone, cartilage and tendons.

The team combined computer modeling and laboratory tests on the threads. To carry out their experiments, they placed an underwater cage in Boston Harbor for three weeks, during which time mussels attached themselves to the surfaces of glass, ceramics, wood and clay in the cage. Back in the lab, the mussels, threads and substrates were mounted in a tensile machine designed to test their strength by pulling on them with controlled deformation and recording the applied force during deformation.

"Many researchers have studied mussel glue before," Qin says, referring to the sticky substance that anchors byssus threads to a surface. But the static strength of the glue, and of the thread itself, "is not sufficient to withstand the impact by waves," he says. It's only by measuring the system's performance in simulated wave conditions that he and Buehler could determine how it accomplishes its amazing tenacity.

"We figured there must be something else going on," says Buehler, who heads MIT's Department of Civil and Environmental Engineering. "The adhesive is strong, but it's not sufficient."

The distribution of stiffness along the threads is key, Qin and Buehler found, suggesting that the distribution of intrinsic material properties and the overall architecture of the mussel attachment are important.

The distribution of stiffness in the mussels' threads enables them to be subjected to very large impact forces from waves. About 80 percent of the length of the byssus threads is made of stiff material, while 20 percent is softer and stretchier. This precise ratio may be critical, the researchers found: The soft and stretchy portions of the threads attach to the mussel itself, while the stiffer portion attaches to the rock. "It turns out that the ... 20 percent of softer, more extensible material is critical for mussel adhesion," Qin says.

In their simulations, Qin and Buehler systematically tested other ratios of the material composition and found that the 80-20 ratio of stiff to soft leads to the smallest reaction force. Having more of the softer material increases the reaction force because the material cannot effectively slow down deformation. Moreover, having more stiff material in byssus threads has other advantages, as it prevents the mussels from being pulled too far out by waves, which "would make it easier to hit other objects" and be damaged, Qin says.

These findings, Qin and Buehler say, could help in the design of synthetic materials that share some of these properties. For example, surgical sutures used in blood vessels or intestines are subjected to pulsating or irregular flows of liquid; the use of materials that combine stiffness and stretchiness, as byssus threads do, might provide advantages. The researchers say there may also be applications for materials to attach instruments to buildings, or sensors to underwater vehicles or sensing equipment in extreme conditions.

Article adapted by Medical News Today from original press release. Click 'references' tab above for source.
Visit our medical devices / diagnostics section for the latest news on this subject.

Written by David Chandler, MIT News Office

Massachusetts Institute of Technology

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Health Tips & Info : Understanding a Food Calorie Counter.

Utilizing a food calorie counter is an effective approach in reaching the weight that you have always wanted. With a food calorie counter, you have a reliable guide that you can consult when you want to gain weight, lose weigh, or even maintain your current weight. To use the food calorie counter method, what you need to do is measure the number of calories that you have consumed and manage your food intake depending on what your weight plan is. Here are several things that are worth knowing about a food calorie counter and how it works.


A calorie is a unit of energy and it indicates the amount of energy that we obtain from ingesting a certain food. The calories that we obtain from food are then used as a source of energy that allows us to do various things. Furthermore, calories are also employed by out body systems in order for them to function. For example, we burn calories whenever we breathe. However, whenever we eat too much, our body does not use up all the calories we have obtained from eating. Because of this, our bodies converts the leftover calories into fat, which also increases our weight. 


A food calorie counter will allow us to know if what we are eating are less than or beyond what our bodies would normally need to function everyday. The knowledge of how much calories we put in our bodies will give as an idea of the necessary changes that we need to do in our diet in order to attain a weight goal.


A lot of people do not prefer this method of losing or gaining weights since they believe that measuring your calories is very hard to do, thus they go for more specific dieting systems instead. However, with a food calorie counter, you need not be denied of the foods that you wish to eat if you aim to lose weight. What you only need to manage is the amount of each specific food. Additionally, there are many internet sources that you can consult when utilizing a food calorie counter.


By Current Health Articles

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Health Tips & Info : Understanding Gestational Diabetes Mellitus.

For the majority of women, carrying a child is the greatest blessing one can ever experience. It is a joyous time for both expectant parents because it is a celebration of another life. Even though a lot of women go through discomforts while pregnant, these are quickly managed since most of these minor pains ease off typically right after the first trimester. Unluckily for a couple of women, pregnancy is considered a problematic time because of complications that need a whole lot of attention and consideration. And one particular common complication of pregnancy is gestational diabetes mellitus or GDM, also known as gestational diabetes in pregnancy.Gestational diabetes mellitus is defined as glucose intolerance that affects pregnant women. It occurs in around 4 percent to 10 percent of women that are pregnant and often goes away after delivery. Women who are likely to suffer from GDM are the following: pregnant women who are obese, women who are 25 years and older, women who have history of GDM with previous pregnancies, history of giving birth to a big baby (usually 9 lbs. or more) and family history of type 2 diabetes.The symptoms of gestational diabetes mellitus are usually ignored because they are confused with the normal discomforts of pregnancy. The most prevalent symptoms of gestational diabetes are: increased frequency of urination, increased thirst and increased hunger. However, there are tests available in order to know whether these symptoms are brought about by hormonal imbalances that normally occur during pregnancy or if these are already signs of gestational diabetes mellitus.Oral glucose tolerance test (OGTT) measures the response of insulin to glucose loading. This type of procedure is typically done during the 24th to 28th week of pregnancy. This gestational diabetes test necessitates the pregnant woman to fast at least eight hours before heading to the lab. Later on, she will be requested to consume a sweetened liquid with 50- to 200-g of sugar. A small amount of blood sample will then be extracted at .25, 1, 2 and 3 hours intervals. Gestational diabetes mellitus is confirmed if the 2-hr value is 200 mg/dL or greater.Being healthy is always a priority when one is pregnant. It’s worthwhile to have regular checkups so that your doctor can keep track of your condition and try everything that’s possible to help you and your little one become satisfied and healthy.

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