Researchers experiment with the Sam68 protein. Credit: McMaster University

A team of researchers at McMaster University has identified a unique feature of cancer stem cells that can be exploited to kill the deadly cells thought to be the reason that cancer comes back after therapy. Understanding this feature will be useful for delivering more targeted cancer therapeutics to the right patients.

The study, published today in the scientific journal Cell Chemical Biology, reveals that an existing set of drugs is effective in killing cancer stem cells and explains how this led the team to uncovering important details about how these cells are working in human tumors.

"The drugs helped us to understand the biology," said Mick Bhatia, principal investigator of the study and scientific director of the McMaster Stem Cell and Cancer Research Institute. "We've worked backwards, employing a series of drugs used in the clinic to understand a new way that cancer stem cells can be killed."

The researchers found that a particular protein, called Sam68, is an important actor in cancer stem cells, and that this protein allows existing drugs to work on cancer cells, causing them to die.

Bhatia hopes that this information can be used to deliver targeted therapies to the patients who would benefit from them, while sparing others from unhelpful treatments. He believes that treatment of blood cancers like leukemia and other cancers such as prostate, colon and renal will follow the example set in breast cancer, where patients receive treatments tailored to their specific form of the disease.

"In the case of breast cancer, other researchers have found new ways to make existing drugs more effective by only giving them to people who were likely to benefit based on their specific traits and using drugs that target these traits," Bhatia said.

He said while developing a new drug takes an average of about 15 years and comes with a price tag in the hundreds of millions, defining the role of existing drugs to use them better in patients will help to accelerate the process of bringing the right drugs to the right people.

Reference

Mickie Bhatia et al. Sam68 Allows Selective Targeting of Human Cancer Stem Cells. Cell Chemical Biology, June 2017 DOI: 10.1016/j.chembiol.2017.05.026

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Existing Drug Found to be Effective at Killing Cancer Stem Cells - Technology Networks

Katayoon Dehesh, known for her work on how stress signals are sensed in plants, joins an academy whose past members include Charles Darwin and Albert Einstein

By Iqbal Pittalwala on June 26, 2017

Katayoon Dehesh. Photo credit: IIGB, UC Riverside.

By Aurelia Espinoza, IIGB

RIVERSIDE, Calif. Katayoon Dehesh, the director of the Institute for Integrative Genome Biology (IIGB) and the Ernst and Helen Leibacher Endowed Chair in Botany and Plant Sciences at the University of California, Riverside, has been elected to the Leopoldina, the German National Academy of Sciences.

Founded in 1652, the Leopoldina is one of the oldest academies of science in the world, with a membership that has included such luminaries as Marie Curie, Charles Darwin, Albert Einstein, and Max Planck.

Dehesh, a professor of molecular biochemistry,joined UC Riverside in July 2016. Previously she was the Paul Stumpf Endowed Chair in Plant Biochemistry at UC Davis.

She will join the Organismic and Evolutionary Biology section of the Leopoldina, in line with her primary research interests in deciphering the molecular and biochemical regulatory mechanisms underlying stress-induced responses that ensure organismal integrity and environmental adaptation. Specifically, her lab examines how stress signals are sensed in plants and the mechanisms by which they integrate targeted processes.

We are all incredibly proud that Katie has been elected to the German National Academy of Sciences, the Leopoldina, said Natasha Raikhel, former director of IIGB and the Center for Plant Cell Biology. It is a very rare and special privilege and honor. Katies enthusiasm and passion for her science is equaled only by her devotion to helping young scientists succeed. She is fearless and stands up for principles in both science and in life. For this and many other reasons, Katie is a visionary leader for the IIGB.

Dehesh will travel to Germany in May 2018 to formally accept the honor.

She is the recipient of several other awards and honors, including being named a fellow of the American Association for the Advancement of Science; Honorary Professor at South West University, China; Excellence in Education Award, UC Davis; Monsanto Fellow; and the Iran National Award.

IIGB is a multidisciplinary organization on campus, with faculty members spanning four colleges and over 20 departments. Its mission is to foster interdisciplinary collaborations among researchers on campus and within the scientific community by coupling computational approaches and technological innovations with molecular and cellular biology to solve the complex biological problems facing our society today.

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June 26, 2017 by Erika Ebsworth-Goold Engineers at Washington University in St. Louis and Princeton University developed a new way to dive into the cell's tiniest and most important components. What they found inside membraneless organelles surprised them, and could lead to better understanding of fatal diseases including cancer, Huntington's and ALS. Credit: Washington University in St. Louis

Inside each and every living cell, there are miniscule structures called membraneless organelles. These tiny powerhouses use chemistry to cue the inner workings of a cellmovement, division and even self-destruction.

A collaboration between engineers at Princeton University and Washington University in St. Louis has developed a new way to observe the inner workings and material structure of these vitally important organelles. The research, published today in Nature Chemistry, could lead to a host of new scientific applications, as well as a better understanding of diseases such as cancer, Huntington's and ALS.

"They're like little drops of water: They flow, they have all the properties of a liquid, similar to raindrops," said Rohit Pappu, the Edwin H. Murty Professor of Engineering at Washington University's School of Engineering & Applied Science. "However, these droplets are comprised of protein that come together with RNA (ribonucleic) molecules."

In the past, peering into organelles has proven difficult, due to their tiny size. Clifford Brangwynne, associate professor in chemical and biological engineering at Princeton's School of Engineering and Applied Science, and his collaborators, developed a new techniquecalled ultrafast scanning fluorescence correlation spectroscopy or usFCSto get an up-close assessment of the concentrations within and probe the porosity of facsimiles of membraneless organelles. The approach uses sound-waves to control a microscope's ability to move and then obtain calibration-free measurements of concentrations inside membraneless organelles.

In their research, Brangwynne and his team, including postdoctoral researchers Ming-Tzo Wei and Shana Elbaum-Garfinkle, used cells taken from a roundworm. With usFCS, they were able to measure protein concentrations inside organelles formed by the specific protein, LAF-1. This protein is responsible for producing p-granules, which are protein assemblies responsible for polarizing a cell prior to division. Once the Princeton researchers were able to clearly peek into the organelles and view the LAF-1, what they found surprised them.

"We found that instead of being densely packed droplets, these are very low density, permeable structures," Brangwynne said. "It was not the expected result."

That's when Washington University's Pappu and his graduate research assistant Alex Holehouse tried to make sense of the surprising findings from the Princeton group. Pappu's lab specializes in polymer physics and modeling of membraneless organelles.

"We were able to basically swim inside the organelles to determine how much room is actually available. While we expected to see a crowded swimming pool, we found one with plenty of room, and water. We're starting to realize that these droplets are not all going to be the same," Pappu said.

In the case of the LAF-1 organelles, the researchers found the formation of ultra-dilute droplets derives from information encoded in the intrinsically disordered regions of these protein sequences. The features of that sequence ensure that this protein is a highly floppy molecule, rather like cooked spaghetti, lacking the ability to fold into a specific, well-defined structure. In contrast, in other organelles formed by different proteins, the material properties are more like those of toothpaste or ketchup. Brangwynne and Pappu are continuing to collaborate to figure out how different protein sequences encode the ability to form droplets with very different material properties. This work has direct implications for understanding biological functions of membraneless organelles and for understanding how changes to these material properties give rise to diseases such as neurodegeneration or cancers.

"There is an explosion of engineering applications and transformations for mechanistic cell biology that are on the horizon. These advancements will be accessible as we learn more about the foundation of these organelles and how their amino acid sequence determines material properties and function," Pappu said. "These organelles are doing remarkable things inside cells, and a really neat question is: How can we mimic them?"

Pappu says one day, researchers could hack the design principles of organelles to fashion everything from intracellular chemistry labs to tiny drug delivery vehicles and imaging agents. Aside from the practical applications, there are also potential implications for understanding and diagnosing a whole host of diseases.

"It is essential to be able to understand how one can regulate the functions of these droplets," Pappu said. "If we succeed, the impact could be transformative: It's not just cancer, it's neurodegeneration, about developmental disorders, and even the fundamentals of cell biology."

Explore further: Ending a century of intrigue around 'membraneless' cell compartments

More information: Phase behaviour of disordered proteins underlying low density and high permeability of liquid organelles, Nature Chemistry (2017). DOI: 10.1038/nchem.2803

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Detecting diluteness: New experimental and theoretical approaches 'dive into the pool' of membranes organelles - Phys.Org

Crystals are shown stained by various methods within paraffin sections. The arrows indicate two of the most striking crystals in each overview image. Images: Nrnberger et al, doi: 10.1007/s00418-016-1516-6

Giant crystals have been found within the mitochondria of cartilage cells in horses, with nothing similar seen in the cartilage of any other species investigated so far.

Mitochondria are membrane-bound structures that are effectively power generators within a cell, converting oxygen and nutrients into adenosine triphosphate, which powers the cells metabolic activities.

Researchers from Austria and Germany have reported their discovery in the journal Histochemistry and Cell Biology.

The crystals in the mitochondria of chondrocytes the latter being the only cells found in healthy cartilage show dark contrast in transmission electron microscopy imaging a technique in which a beam of electrons is transmitted through a specimen to form an image.

The crystals, which can be so large they result in enlarged mitochondria that can stretch the length of a cell, show a granular substructure of regularly aligned 1 to 2-nanometre small units.

Further analysis revealed a high content of nitrogen, indicating a protein. Their chemical composition has yet to be fully clarified.

Sylvia Nrnberger and her colleagues said the outer shape of the crystals was geometrical, with some profiles revealing hexagonal cross sections.

They were elongated, spanning a length of several micrometres through the whole cell.

In some chondrocytes, several crystals were found, sometimes combined in a single mitochondrion, they reported.

The crystals were preferentially aligned along the long axis of the cells, thus appearing in the same orientation as the chondrocytes in the tissue.

Although no similar structures have been found in the cartilage of any other species investigated, they reported, they have been found in cartilage repair tissue formed within a mechanically stimulated equine chondrocyte construct.

The crystals were mainly located in the surface regions of cartilage, especially in joint regions of well-developed superficial layers, more often in yearlings than in adult horses.

They believe the crystals are related to the high mechanical stress in the horse joint and potentially also to the increased metabolic activity of immature individuals.

Discussing their findings, the study team said crystals in cartilage cells have never been described in other species, with cats and dogs having already been ruled out in previous research. The study team went as far as screening for crystals in cartilage from other species, but found none in chickens, rats, pigs, sheep, calves, or humans.

They noted that crystals within mitochondria have also been seen in other cell types but, in contrast to the crystals seen in horse cartilage, were clearly smaller than the mitochondria, frequently compartmented, and they occupied only a part of the mitochondrial organelle.

Crystals also have often been described within the mitochondria of lower organisms such as protozoa and invertebrates, and have even been seen in other vertebrates, including mammals. However, these crystals have either only an inner crystalline structure or also a crystalline outer shape, and seem more common in the presence of liver and muscle conditions such as ischaemia, protein deficiency or starvation.

They did not seem to be the reason for the size increase of the mitochondria. On the contrary, in the equine chondrocytes the increasing size of the crystals may be the obvious reason for the enlargement of the mitochondria, since the crystals completely fill the intramitochondrial space and stretch the mitochondrion to an enormous size, sometimes to the full length of the cell.

Further, in horse chondrocytes, giant mitochondria only appear in relation with giant crystals.

The crystals presented special characteristics in terms of their size and appearance in chondrocytes, which are cells with low metabolic activity under no particular hormonal influence.

The distribution of the crystals suggested a relation to areas of high mechanical stress, which could locally be the case in defects and in transplanted areas.

Crystals were found especially in yearlings, suggesting also a developmental component, probably due to the anatomical changes and activities during growth.

They said further studies on the composition of the crystals were necessary to understand the origin and reason for their development and physiological correlations.

Members of the study team are affiliated with a range of institutions, including the Medical University of Vienna.

Giant crystals inside mitochondria of equine chondrocytes S. Nrnberger, C. Rentenberger, K. Thiel, B. Schd, I. Grunwald, I. Ponomarev, St. Marlovits, Ch. Meyer, and D. Barnewitz Histochem Cell Biol. 2017; 147(5): 635649. doi: 10.1007/s00418-016-1516-6 PMCID: PMC5400799

The study, published under a Creative Commons License, can be read here.

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What are giant crystals doing within the cartilage cells of horses? - Horsetalk

Postdoc Silvio Temprana and assistant professor Kaoru Saijo received research grants from the Pew Charitable Trusts. Temprana photo by Ken Li. Saijo photo by Mark Hanson of Mark Joseph Studios.

Two young UC Berkeley biomedical scientists received awards last week from the Pew Charitable Trusts to support their research on the brain.

Kaoru Saijo, an assistant professor of molecular and cell biology, will receive a four-year grant to investigate the role of the brains immune cells, called microglia, in the development of depression. Saijo will seek to determine whether mutations that alter gene activity in microglia lead to a sustained inflammatory response in the brain, whether such changes take place in mouse models of depression and whether they affect males and females differently. This may someday lead to new therapeutic strategies for the treatment of neurological diseases in humans.

Saijo was one of 22 early career researchers selected because they have demonstrated the curiosity and courage that drive great scientific advances, said Rebecca Rimel, president and CEO of the Pew Charitable Trusts in a statement. We are excited to help them fulfill their potential.

Silvio Temprana of Argentina was named one of 10 Pew Latin American Fellows in the Biomedical Sciences, each of whom will receive two years of funding to conduct research at laboratories and academic institutions in the United States.

The fellows will conduct their research under the mentorship of some of the most distinguished researchers in biomedical science, including alumni of the Pew Scholars Program in the Biomedical Sciences. An important element of the program is additional funding provided to awardees who return to Latin America to launch their own research labs after the completion of their fellowships.

Temprana is already at work in the lab of Hillel Adesnik, an assistant professor of molecular and cell biology and 2013 Pew biomedical scholar who studies how networks of neurons in the brain encode sensory input in order to drive perception. Temprana plans to manipulate the activity of individual neurons within clusters of networked neurons to determine whether an animals perception can be altered. He hopes his findings will deepen current understanding of information processing in the brain and provide insights into how these processes malfunction in disease.

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Two early career researchers awarded Pew grants - UC Berkeley

June 22, 2017 In this developing backbone of a zebrafish, collapsed inner cells (green) are replaced by newly fluid-filled sheath cells (red) from the outer layer. The remaining cellular debris clumps together in the center of the structure, which is called a notochord. Credit: Jennifer Bagwell, Duke University

Duke researchers have discovered a unique repair mechanism in the developing backbone of zebrafish that could give insight into why spinal discs of longer-lived organisms like humans degenerate with age.

The repair mechanism apparently protects the fluid-filled cells of the notochord, the precursor of the spine, from mechanical stress as a young fish begins swimming. Notochord cells go on to form the gelatinous center of intervertebral discs, the flat, round cushions wedged between each vertebrae that act as shock absorbers for the spine.

The disappearance of these cells over time is associated with degenerative disc disease, a major cause of human pain and disability worldwide.

"It is not difficult to speculate that these same mechanisms of repair and regeneration are present in humans at very early stages, but are lost over time," said Michel Bagnat, Ph.D., senior author of the study and assistant professor of cell biology at Duke University School of Medicine. "If we are going to think about techniques that foster intervertebral disc regeneration, this is the basic biology we need to understand."

The study appears June 22, 2017, in Current Biology.

Bagnat likens the notochord to a garden hose filled with water. The hardy structure consists of a sheath of epithelial cells surrounding a collection of giant fluid-filled or "vacuolated" cells. During development, these vacuolated cells rarely pop, despite being under constant mechanical stress. Recent research has suggested that tiny pouches known as caveolae (Latin for "little caves") that form in the plasma membrane of these cells can provide a buffer against stretching or swelling.

To see whether the caveolae protected vacuoles from bursting, his team and collaborators from Germany generated mutants of three caveolar genes in their model organism, the zebrafish. Because these small aquarium fish are transparent as embryos, the scientists could easily visualize any spinal defects triggered by the loss of caveolae.

The researchers found that when the mutant embryos hatched and started swimming, exerting pressure on their underdeveloped backbones, their vacuolated cells started to break up. While the finding confirmed their suspicions, it turned up a puzzling discovery. "In the caveolar mutants, you see these serial lesions up and down the notochord, and yet the mature spine formed normally," said Bagnat. "That was very puzzling to us."

To figure out how that was possible, lead authors Jamie Garcia and Jennifer Bagwell took a closer look at the notochord of mutant fish. They marked the vacuolated cells green and the surrounding epithelial sheath cells red and then filmed the fish shortly after they hatched and started swimming. First, they could see an occasional vacuolated cell break and spill its contents like a water balloon. Then, over the course of fifteen hours, a nearby epithelial sheath cell would move in, crawl over the detritus of the collapsed cell, and morph into a new vacuolated cell.

They performed a few more experiments and found that the repair response was triggered by the release of the cell contents, specifically the basic molecular building blocks known as nucleotides. The researchers then isolated live epithelial sheath cells and treated them with nucleotide analogs to show that they turned into vacuolated cells.

"These cells, which reside in the discs of both zebrafish and man, seem capable of controlling their own repair and regeneration," said Bagnat. "Perhaps it is a continuous release of nucleotides that is important for keeping the disc in good shape."

The study may offer insight not only into the development of back and neck pain, but also into the origins of cancer. Their data suggests that chordomas, rare and aggressive notochord cell tumors, may begin when epithelial sheath cells leave the notochord and invade the skull and other tissues.

Explore further: Stem cells therapy for naturally occurring intervertebral disc disease

More information: "Sheath cell invasion and trans-differentiation repair mechanical damage caused by loss of caveolae in the zebrafish notochord," Jamie Garcia, Jennifer Bagwell, Brian Njaine, James Norman, Daniel S. Levic, Susan Wopat, Sara E. Miller, Xiaojing Liu, Jason W. Locasale, Didier Y.R. Stainier and Michel Bagnat. Current Biology, June 22, 2017. DOI: 10.1016/j.cub.2017.05.035

Journal reference: Current Biology

Provided by: Duke University

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Duke researchers have discovered a unique repair mechanism in the developing backbone of zebrafish that could give insight into why spinal discs of longer-lived organisms like humans degenerate with age.

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Cells in fish's spinal discs repair themselves - Phys.Org

The global cell imagers market to grow at a CAGR of 8.21% during the period 2017-2021.

Global Cell Imagers Market 2017-2021, has been prepared based on an in-depth market analysis with inputs from industry experts. The report covers the market landscape and its growth prospects over the coming years. The report also includes a discussion operating in this market.

According to the report, one of the major drivers for this market is growing prevalence of chronic diseases. Globally, chronic diseases such as cancer, diabetes, arthritis, heart diseases, and stroke are the leading causes of deaths. The prevalence of these diseases is increasing at alarming rates. The CDC estimates that by 2020, the number of new cancer cases is expected to increase by nearly 2 million each year.

The latest trend gaining momentum in the market is extensive use of automation in live cell imaging. Cell imaging is an important tool for the efficient study of cell biology and discovery of drugs. Hence, the automation of cell imaging can reduce the time spent by researchers on tasks such as sample loading, which allows them to spend time on analyzing and interpreting the results obtained from cell imaging. Automated microscopy solutions are offered by most vendors and are being increasingly deployed in various diagnostic centers and research laboratories. These solutions increase the overall lab output as they assist in analyzing more samples.

Further, the report states that one of the major factors hindering the growth of this market is technical and economic challenges of super resolution. To achieve better results and generate more insights about cellular processes, there has been an immense need to develop imaging equipment that provide better resolution. However, the various approaches used to achieve this have been ineffective to solve real-world problems. Issues related to resolution have been the most common cited challenge among key opinion leaders at various annual conferences held to discuss advancements and issues related to microscopy.

Key vendors:

Other prominent vendors:

Key Topics Covered:

Part 01: Executive summary

Part 02: Scope of the report

Part 03: Research Methodology

Part 04: Market landscape

Part 05: Market segmentation by application

Part 06: Market segmentation by product type

Part 07: Market segmentation by end-user

Part 08: Geographical segmentation

Part 09: Decision framework

Part 10: Drivers and challenges

Part 11: Market trends

Part 12: Vendor landscape

Part 13: Key vendor analysis

Part 14: Appendix

For more information about this report visit https://www.researchandmarkets.com/research/xlpqcb/global_cell

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Global Cell Imagers Market 2017-2021 - Research and Markets - PR Newswire (press release)

LONDON--(BUSINESS WIRE)--Technavio analysts forecast the global cell imagers market to grow at a CAGR of more than 8% during the forecast period, according to their latest report.

The research study covers the present scenario and growth prospects of the global cell imagers market for 2017-2021. The market is segmented on the application (cell biology, stem cells, development biology, and drug discovery) and product (equipment, consumables, and software). The market is further segmented on end-user (hospitals and diagnostics labs, pharmaceuticals and biotechnology companies, and academic and research institutes), and geography (the Americas, EMEA, and APAC).

The global cell imagers market is expected to witness strong growth during the forecast period due to the growing prevalence of chronic diseases, increasing demand for HCS techniques, and increased focus on cell-based research. The growth of allied industries such as pharma and biotech will drive the growth of the market further. Also, the increase in the number of research and testing facilities, particularly in the fields of pharmaceutical and biotechnology, will lead to a rise in demand for cell imagers.

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Technavio research analysts highlight the following three factors that are contributing to the growth of the global cell imagers market:

Growing prevalence of chronic diseases

Chronic diseases such as cancer, diabetes, arthritis, heart diseases, and stroke are the leading causes of deaths globally. The prevalence of these diseases is increasing at alarming rates. The CDC estimates that by 2020, the number of new cancer cases is expected to increase by nearly 2 million each year.

Amber Chourasia, a lead lab equipment research analyst at Technavio, says, According to various studies conducted on disease patterns in 2015, cardiovascular diseases were responsible for approximately 15-20 million deaths and cancer was responsible for approximately seven to 10 million deaths worldwide. The growing burden of chronic conditions drives the demand for advanced healthcare and cell imaging systems, which can reduce the burden by intervening at critical diagnostic stages and assist in better disease prevention, diagnosis, and treatment.

Increasing demand for high content screening techniques

HCS or HCA is a set of analytical methods that utilize automated microscopy, multi-parameter image processing, and unique visualization tools to generate quantitative data from cells. In their most basic form, these techniques measure one signal averaged over multiple cells that are present within a microplate. The signal could be the expression of a reporter gene or levels of molecules such as adenosine triphosphate (ATP).

Fluorescence imaging is a method that is used for visualizing samples in a high-throughput format and aspects such as the spatial distribution of targets, and the morphology of cells and organelles are reported, adds Amber.

Increased focus on cell-based research

Globally, there is an increase in focus on cell-based research as companies, governments, and research institutions have started to realize the importance of cell biology in analyzing cellular systems to reveal new insights and therapies through the early diagnosis and assessment of therapies.

In the US, the National Institute of General Medical Sciences (NIGMS) explicitly stated in its research grant policy that it supports projects involving cell imaging techniques that address areas such as the monitoring of the stages of mitosis, amount of gene expressed, process of messenger ribonucleic acid (mRNA) transport, alterations in nuclear architecture and membranes during cell death or apoptosis, and other processes that occur during cell migration.

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Technavio is a leading global technology research and advisory company. The company develops over 2000 pieces of research every year, covering more than 500 technologies across 80 countries. Technavio has about 300 analysts globally who specialize in customized consulting and business research assignments across the latest leading edge technologies.

Technavio analysts employ primary as well as secondary research techniques to ascertain the size and vendor landscape in a range of markets. Analysts obtain information using a combination of bottom-up and top-down approaches, besides using in-house market modeling tools and proprietary databases. They corroborate this data with the data obtained from various market participants and stakeholders across the value chain, including vendors, service providers, distributors, re-sellers, and end-users.

If you are interested in more information, please contact our media team at media@technavio.com.

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Global Cell Imagers Market - Drivers and Forecasts by Technavio - Business Wire (press release)

June 21, 2017

Researchers at the University of Michigan Life Sciences Institute have identified a new type of rapid-response defense mechanism that helps protect cells from environmental stress while giving slower, well-known protection systems time to act.

"It's like a first responder rushing to an alarm while the larger response team mobilizes," said Natsuko Jin, a postdoctoral research fellow in the lab of LSI faculty member Lois Weisman and lead author of a study scheduled to be published June 21 in the Journal of Cell Biology.

Generally, when cells are put under stress, adaptation mechanisms kick in. They trigger transcriptional machinery and, through gene expression, the cell produces new proteins to respond to the stress and keep itself alive.

In yeast, a single-cell organism often used to study fundamental cellular biology, a much faster type of response was also observedan immediate and short-lived spike in the production of a signaling lipid that is usually seen only in miniscule quantities.

When the scientists short-circuited the yeast's ability to generate this rapid response, the yeast succumbed to an environmental stress at catastrophic rates.

"This is the first time an early protection pathway that works faster than gene expression has been identified," Jin said. "Since many of the key players have been preserved by evolution up into people and other mammals, our investigations suggest this and other types of early protection pathways may exist more broadly, and they may respond to different types of cellular stress."

For this study, the yeast were put into an environment with a high concentration of saltwhat scientists call high osmolarity. Within a few minutes, each cell responds by setting off a signaling cascade that activates a key protein kinaseHog1which travels from the cell's cytoplasm into the nucleus, where it promotes changes in gene expression. These changes in gene expression take between 30 minutes and an hour to start to have an effect, and up to two hours to be fully activated.

Meanwhile, the researchers also observed a sharp, immediate spike in a signaling lipid known as PI3,5P2, which is produced by an organelle called the vacuole in yeast. The yeast vacuole is similar to the lysosome in complex organisms.

"Within one minute you see a five-fold elevation of this lipid," said Weisman, senior author on the study and professor of cell and developmental biology at the U-M Medical School. "Within five minutes, it's a 20-fold increase. Then, without us doing anything else to the cells, it plateaus and drops off."

When regular yeast were put into this high salt, or hyperosmotic, environment for four hours, most did just fine.

When the researchers used genetic manipulation to knock out the well-known, longer-term response pathway that produces Hog1, 30 percent of the cells died.

"Still, 70 percent did just fine," Weisman said.

But when they removed the cell's ability to produce PI3,5P2, 80 percent died.

"So we know it's doing something protective before the gene expression kicks in," she said. "If they don't have it, most die."

Exactly how PI3,5P2 conveys a benefit to the cell is not yet understood, Jin said. The current study examined the upstream regulators of the signaling lipid, and demonstrated they were distinct both in time and space from the action of the Hog1 pathway.

She also said that while the observation that PI3,5P2 spikes under hyperosmotic conditions dates back to the late 1990s, its role had previously been unclear. Jin's investigation started with the desire to understand what causes the spike and what physiological role it might play.

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Continued here:
Newly identified protection mechanism serves as first responder to cellular stress - Phys.Org

June 21, 2017 by Tom Fleischman

Integral membrane proteins, or IMPs, are a major class of proteins that play crucial roles in many cellular processes, including the catalysis of disulfide bonds, which are essential for the function and stability of many proteins such as antibodies, which have significant therapeutic potential.

But IMPs are intrinsically hydrophobic and thus have low solubility in watery environments. Their natural environment is within the lipid bilayer membrane of a cell, which makes it difficult to study their structure and function.

A previously reported method involving standard recombinant DNA techniques and some novel design principles enabled a team of Cornell chemical engineers to make large quantities of functional IMPs simply and inexpensively all without the use of harsh chemicals or detergents, which are typically used today. That team, led by Matt DeLisa, the William L. Lewis Professor of Engineering in the Robert Frederick Smith School of Chemical and Biomolecular Engineering, has now used that protein engineering method to convert a membrane-bound enzyme into a water-soluble biocatalyst that functions directly in the aqueous inner cell.

"You can redesign these tricky proteins, making them water-soluble, and perhaps really surprisingly, they can continue to catalyze their natural biological reactions," said DeLisa, principal investigator for "A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo," published June 19 in Nature Chemical Biology.

"To our knowledge, this is the first example of creating a water-soluble IMP that retains its natural catalytic activity but does so in an entirely new cellular environment," DeLisa said. "And because it's a genetically engineered construct, it can be expressed like any other soluble protein with very little effort or difficulty."

First author is Dario Mizrachi, former postdoctoral associate in chemical and biomolecular engineering who's now an assistant professor at Brigham Young University. Collaborators included Michael-Paul Robinson, doctoral student in chemical and biomolecular engineering, and Mehmet Berkmen of New England Biolabs.

The group's previous work detailed a method they called SIMPLEx (Solubilization of Integral Membrane Proteins with High Levels of Expression), for shielding IMPs from water and enabling the production of large quantities of these difficult-to-make proteins. Using recombinant DNA techniques, they stitched together an artificial membrane protein with an identity crisis one that maintains its biological function, but thinks it's soluble in water.

This latest work is the first application of that technique. The group used their identity-switched IMPs to make disulfide bonds, a type of post-translational modification that occurs in many proteins and influences nearly all aspects of normal cell biology and pathogenesis.

The group targeted the bacterial integral membrane enzyme DsbB, a central biocatalyst in disulfide bond formation, although DeLisa believes the technique is transferrable to myriad other membrane proteins.

Using the SIMPLEx method, the group converted membrane-bound DsbB into a water-soluble biocatalyst that could be readily expressed in the E. coli cytoplasm, where it spawned disulfide-bond formation in a range of protein targets.

Disulfide bonds are key players in many therapeutic proteins, such as monoclonal antibodies. Many cancer drugs employ these molecules, which can mimic or enhance the immune system's attack on tumor cells.

The ability to take the catalyst out of the lipid membrane and put it in the cytoplasm, DeLisa said, allows scientists to make these antibodies in potentially more favorable locations in the cell.

"We could make this pathway in the cytoplasm [or] we could move everything to a different subcellular compartment like the periplasm, or potentially take the entire pathway out of the cell and reconstitute it in a cell-free system," DeLisa said. "The point is, we create a tremendous amount of flexibility in terms of making these bonds by essentially turning a membrane protein into a soluble enzyme."

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More information: Dario Mizrachi et al. A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo, Nature Chemical Biology (2017). DOI: 10.1038/nchembio.2409

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Changing the identity of cellular enzyme spawns new pathway - Phys.Org