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Scientists Spot a Live 'Ghost Fish' for the First Time

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No, it’s not a subversive promo for Sony’s new Ghostbusters remake: Earlier this month, the National Oceanic and Atmospheric Administration (NOAA) announced that a member of the rarely seen Aphyonidae family of eel-like fish was caught alive on camera for the first time during an exploration at Mariana Trench Marine National Monument east of the Philippines.

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The 4-inch-long fish—known for its translucent skin and unpigmented eyes—was found about 8200 feet below the ocean’s surface. While specimens from the Aphyonidae family have usually been caught by accident, the discovery marks the first time one has been seen alive.

Bruce Mundy, fishery biologist at the NOAA, calls the ghost fish sighting one of the “bucket list” items for his profession. If you’re charmed by ocean life that looks vaguely like Casper, be sure to check out the translucent octopus found by the NOAA earlier this year.

[h/t LiveScience]

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Women Suffer Worse Migraines Than Men. Now Scientists Think They Know Why
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Migraines are one of medicine's most frustrating mysteries, both causes and treatments. Now researchers believe they've solved one part of the puzzle: a protein affected by fluctuating estrogen levels may explain why more women suffer from migraines than men.

Migraines are the third most common illness in the world, affecting more than 1 in 10 people. Some 75 percent of sufferers are women, who also experience them more frequently and more intensely, and don't respond as well to drug treatments as men do.

At this year's Experimental Biology meeting in San Diego, researcher Emily Galloway presented new findings on the connection between the protein NHE1 and the development of migraine headaches. NHE1 regulates the transfer of protons and sodium ions across cell membranes, including the membranes that separate incoming blood flow from the brain.

When NHE1 levels are low or the molecule isn't working as it's supposed to, migraine-level head pain can ensue. And because irregular NHE1 disrupts the flow of protons and sodium ions to the brain, medications like pain killers have trouble crossing the blood-brain barrier as well. This may explain why the condition is so hard to treat.

When the researchers analyzed NHE1 levels in the brains of male and female lab rats, the researchers found them to be four times higher in the males than in the females. Additionally, when estrogen levels were highest in the female specimens, NHE1 levels in the blood vessels of their brains were at their lowest.

Previous research had implicated fluctuating estrogen levels in migraines, but the mechanism behind it has remained elusive. The new finding could change the way migraines are studied and treated in the future, which is especially important considering that most migraine studies have focused on male animal subjects.

"Conducting research on the molecular mechanisms behind migraine is the first step in creating more targeted drugs to treat this condition, for men and women," Galloway said in a press statement. "Knowledge gained from this work could lead to relief for millions of those who suffer from migraines and identify individuals who may have better responses to specific therapies."

The new research is part of a broader effort to build a molecular map of the relationship between sex hormones and NHE1 expression. The next step is testing drugs that regulate these hormones to see how they affect NHE1 levels in the brain.

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Scientists Accidentally Make Plastic-Eating Bacteria Even More Efficient
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In 2016, Japanese researchers discovered a type of bacteria that eats non-biodegradable plastic. The organism, named Ideonella sakaiensis, can break down a thumbnail-sized flake of polyethylene terephthalate (PET), the type of plastic used for beverage bottles, in just six weeks. Now, The Guardian reports that an international team of scientists has engineered a mutant version of the plastic-munching bacteria that's 20 percent more efficient.

Researchers from the U.S. Department of Energy's National Renewable Energy Laboratory and the University of Portsmouth in the UK didn't originally set out to produce a super-powered version of the bacteria. Rather, they just wanted a better understanding of how it evolved. PET started appearing in landfills only within the last 80 years, which means that I. sakaiensis must have evolved very recently.

The microbe uses an enzyme called PETase to break down the plastic it consumes. The structure of the enzyme is similar to the one used by some bacteria to digest cutin, a natural protective coating that grows on plants. As the scientists write in their study published in the journal Proceedings of the National Academy of Sciences, they hoped to get a clearer picture of how the new mechanism evolved by tweaking the enzyme in the lab.

What they got instead was a mutant enzyme that degrades plastic even faster than the naturally occurring one. The improvement isn't especially dramatic—the enzyme still takes a few days to start the digestion process—but it shows that I. sakaiensis holds even more potential than previously expected.

"What we've learned is that PETase is not yet fully optimized to degrade PET—and now that we've shown this, it's time to apply the tools of protein engineering and evolution to continue to improve it," study coauthor Gregg Beckham said in a press statement.

The planet's plastic problem is only growing worse. According to a study published in 2017, humans have produced a total of 9 billion tons of plastic in less than a century. Of that number, only 9 percent of it is recycled, 12 percent is incinerated, and 79 percent is sent to landfills. By 2050, scientists predict that we'll have created 13 billion tons of plastic waste.

When left alone, PET takes centuries to break down, but the plastic-eating microbes could be the key to ridding it from the environment in a quick and safe way. The researchers believe that PETase could be turned into super-fast enzymes that thrives in extreme temperatures where plastic softens and become easier to break down. They've already filed a patent for the first mutant version of the enzyme.

[h/t The Guardian]

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