But then again…

Easier said than done.  My attempts to breathe life into my running motivation have failed.  What it really comes down to is the fact that I’m currently loving my gym workouts, while running – not so much.  I had a good 13-mile run last Sunday; it was cold and windy, but the sun was out in full force which easily makes up for freezing temps.  I’ll take whatever sunlight I can get – my skin these days is at best ghostly, at worst translucent.  

But alas it looks like that 13-miler may be the totality of my running for this week.  Another bout of polar-vortex weather has made venturing outside for any reason unpleasant. Instead I’ve had a good week of weight-training, including a lower body workout today that left my legs all jello-y.  The high-intensity, effort-to-failure of lifting is refreshing after the months of high-mileage running I did last year.  And I’m getting sucked into the gym culture – five different kinds of protein powder grace my cupboards, and my chrome tabs are increasingly populated with bodybuilding.com articles.  I’m learning about the plethora of ways you can squeeze out more work from your muscles – supersets, drop sets, rest-pause sets, German volume.  Like I said, I’m loving the weight-lifting right now, and who am I to argue with my own preferences?  The day will come when I run Boston (or any other marathon for that matter) all-out and see what I can do, it just won’t be this year.  I’m hoping I can leverage my newfound strength into a great summer of triathlon training.

Speaking of protein powder, I’ve discovered my new favourite dessert after purchasing some graham cracker flavoured muscle milk:

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Costco cheesecake – frozen cherries, greek yogurt and muscle milk graham cracker crumble.

Simple and delicious – frozen cherries, greek yogurt and protein powder.  I mix a little water into the protein powder to give it a crumbly texture (otherwise you risk inhaling it – not in the good way).  

My workout from this morning:

SQUATS

  • 20 front squats with the bar to warm up
  • 4 x 10 @ 100

SUPERSET – SINGLE LEG PRESS, BODYWEIGHT HIGH STEP-UP

ROMANIAN DEADLIFT

  • Warmup – 20 with bar, 20@60
  • 3 x 12 @ 80

SUPERSET – LEG EXTENSION DROP SET, LYING LEG CURL DROP SET

SEATED CALF

GLUTE KICKBACK with Smith Machine

Boston Training

The calendar is inching toward Boston faster than I’d like.  11 weeks out and I’ve yet to make a concerted start at training.  Two main reasons for this:

  1. Winter. To quote Bart Simpson, “I didn’t think it was physically possible, but this both sucks and blows.”  Polar vortex cold, regular cold, snow, snow with wind, more snow, more wind, lots more snow.  We’ve had it easy in previous years, and it’s taken a while to adjust.  But I think we’ve all been sufficiently hardened by January’s weather.  -10° C feels like a resplendent gift from the gods now.
  2. I recently had the opportunity to purchase a one-year gym membership using a corporate discount.  We have a small gym in our condo building, but I haven’t belonged to a commercial gym in years. It’s been quite enjoyable to get back into lifting weights, and it’s an appealing alternative to a frustrating 10 min/mile run through unplowed sidewalks in bone-chilling temps.

Unfortunately neither the weather nor my inclinations have the slightest regard for my goals, commitments, or the steep, non-refundable marathon registration fee.  Pfitzinger has a 12-week training progam, so last week I mustered up some motivation to get out for a few mid-length runs.  Took advantage of some mild but snowy conditions at the end of the week to get 8 and 11 mile runs in on Thursday and Friday, respectively.  Saturday lifted some weights, and then watched in disappointment as it proceeded to snow ALL DAY LONG.  All day.  No breaks. So much snow.

doge_winter

Thankfully it had stopped snowing by Sunday morning, and I headed out for a respectable 15.5 miles.  I like to think that winter miles always count for more than summer miles.  I especially like to think this as I’m huffing and puffing along at 12-minute mile pace in calf-deep snow.

Geesies over Columbia Lake

Geesies over Columbia Lake

I’m trying a strategy I heard recently on a podcast with Matt Fitzgerald: embrace the suckiness of winter.  Taking pride in getting out the door on a -30° day, when there’s a bajillion metric tons of snow, or the sidewalks are treacherous icy death-traps.  Re-framing it as a challenge and a success to be out there on those dark, cold days at 6 am, when there’s nary another soul to be seen.  Seeking out and relishing mornings that are particularly harsh, rather than avoiding them.  Sounds like a good plan; otherwise it’s all too easy to let a bad winter wear you down, and all too easy to become comfortable using “it’s too cold” as an excuse not to run.

This week in running – Aug 12-18

Distance – 83 miles

Time – 12 hr 14m

Key runs – First tempo since getting back from vacation.  Not terrible considering that I consumed my weight in craft beer and Farm Burgers while down in Asheville.  6 miles averaging 7:26.  More marathon pace than LT, but I’ll take it.  An ill-conceived mid-run decision to modify my Wednesday out-and-back medium long run into a loop resulted in an impromptu 20-miler.  And my long run today was a warm one, taking big A on one of my favourite KW routes up through the university of Waterloo, Columbia Lake, Laurel Creek, along the rolling hills of Wilmot line, and back via the Boardwalk and Monarch Woods.

Highlights - Saturday we did our usual destination run from the car, this time going back to the Grand River Trail at Freeport. We did this run our first weekend in KW, but only six miles.  This time we continued on to Kuntz Park where we stopped to check out the historic site with some really old graves.   This section of the trail is beautiful, with some nice views of the river and a few rocky sections that make it feel more like a bona-fide trail run.  I’m not going to lie though, I do love the perfectly groomed crushed gravel paths that make up most of the GRT.

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Learning to love natto

In recent years I’ve experimented with different ways of eating – vegetarian/vegan, gluten-free, paleo.  And while the gluten-free thing I’m going to try to stick with, what is increasingly making the most sense is to have a diet that is widely inclusive.  There’s a hypothesis called the triage theory of aging, which reasons that when the body is facing micronutrient deficiencies, it will sacrifice processes that support longevity in order to prevent acute deficiency symptoms.  If these deficiencies are short-term, this is likely not problematic.  But if you’re chronically deficient in a micronutrient, this theory posits that your body will consistently shut down processes that contribute to long-term health in order to carry out those that are necessary to keep you alive day-to-day.   Few people these days suffer from acute vitamin D deficiency (i.e. rickets),  but it could be that many people don’t have levels that are optimal for long-term disease protection.

Eating a wide variety of natural unprocessed foods seems to be the way to go.  Luckily I’m quite fond of food, plants and animals both.      It’s rare that I encounter something that I hear is very healthful that is also distasteful.  But one such food is natto.

I learned about natto from the book “Vitamin K2 and the Calcium Paradox” by Kate Rheaume B.  It’s a well-written book, not heavy on the science but not so simplistic that it feels condescending, like some science-for-the-nonscientist books can be.   I’d heard about K2 prior to reading this book mostly from internet-readings related to the Weston A. Price foundation.  During his world-wide adventures chronicling the health of various aboriginal peoples, he discovered a correlation between a nutrient he termed the “X factor”, and the healthy, normal development of bones, teeth and facial structures.  This X factor was found in things like egg yolks and grass-fed butter.

Later it became clear that the X factor was in fact Vitamin K2, a little-known vitamin overshadowed by it’s more famous sibling, Vitamin K1.  The greater awareness of K1 is due to the salience of its deficiency syndromes – K1 is vital for proper blood clotting, and if you’re acutely deficient, you’ll know it.   With vitamin K2, you may be deficient your whole life and be none the wiser.  Disorders that could be caused by a lifelong K2 deficiency – osteoporosis and atherosclerosis primarily – are often attributed to other factors, like diet and exercise.

K2 indirectly activates enzymes that are responsible for transporting calcium in the body.  Specifically, it’s a cofactor for K-dependent carboxylase, which is itself an enzyme that alters the structure of two other enzymes: osteocalcin and matrix gla protein (MGP).  Osteocalcin draws calcium into bones and teeth, while MGP removes calcium from arteries and veins, where it can accumulate in  plaques.  Without K2, these proteins remain in their inactive (under carboxylated)  form, and calcium ends up in unwanted places (contributing to atherosclerosis) and not in the places we need it like bones (contributing to osteoporosis).

Luckily, K2 is found in delicious things like egg yolks, butter, and cheese.  But these foods have to come from animals well-fed with green plant matter; butter from grain-fed cows and eggs from grain-fed chickens are likely not rich sources of K2.   I do try to buy free-range eggs (though they rarely advertise the chicken’s diet) and grass-fed ghee, and I suppose that supplements are always an option.  But the book highlights the best dietary source of vitamin K2 – natto – accompanied by a rather descriptive passage about how terrible tasting/smelling/feeling it is.

Natto is fermented soybeans, along the same lines as miso, tempeh, and soy sauce, all of which have fairly distinctive flavors.  But Natto’s distinctiveness is on a whole other level.  It comes in smallish servings inside little styrofoam packages, with soy sauce and mustard as suggested condiments.  There are two things you notice about it before it even touches your tongue: the smell, and the stringiness.

Natto is fermented by a particular microorganism called natto bacillus.  Legend has it that natto was discovered when a group of soldiers, carrying soybeans in a straw sack, were ambushed, and forced to abandon their food sacks.  When they returned, the beans had been fermented by bacteria living within the straw.  But having no other food at hand, they were forced to eat it; and rather than being totally disgusting, they evidently found it quite agreeable, and thus natto was born.  There may be some truth to this story: natto bacillus is a strain of bacillus subtilis, which (according to wikipedia) is also known as grass or hay bacillus.

One of my coworkers spent a co-op term working in Japan, and one day at lunch I asked him if he had ever tried natto.  This led to a dialogue which ultimately culminated in the creation of  a Natto Challenge, in which he offered to bring some to work the next week for us to try.  So on the following Tuesday we had three little styrofoam containers of the stuff in front of us.

First impressions as the protective wrapper was pulled away from the mass of natto were that it smells awful, and kind of resembles rice krispie squares.   The latter owing to the extreme stringiness of whatever starchy byproduct of the fermentation process holds the beans together.  It was seemingly impossibly to get some natto onto your utensil and up to your mouth without a few string clinging in an unsightly manner to your face.

I’m not going to lie, I found it fairly unpleasant at first.  And adding the sauce and mustard didn’t help much.  And disappointingly, the taste seemed to get worse the more you ate, not better.   As the coop student sitting beside me finished his portion, I was determined to choke down every last bean of my own, though it required a large glass of water and some duck-like swallowing maneuvers to do so.

It seems some people have a natural taste for it, enjoying it daily with rice as a breakfast food.  I wouldn’t go so far as to say I had a natural taste for it, but I didn’t find it quite as repulsive as I had anticipated.  It wasn’t tasty, and I would say it had a slight unpleasant taste.  But the unpleasantness is mild and not overpowering.    By itself, it’s not something I would want to eat with any frequency.  But its mildness leads me to believe that when paired with stronger (and more tasty) flavors, it could become something I wouldn’t mind eating for health purposes.  I’ve read that you can trick yourself into developing a taste for initially unpleasant flavours (like the bitter tastes of coffee or beer) by associating them with calorically dense meals.  Your brain is like “Hey, this taste means I’m going to get lots of calories – I’m going to make you like it so that you’re more likely to seek it out”, or something like that.

Thus today was Natto Challenge day 2, and I must say it was a success.   Big A and I have had a new favorite snack of late, thanks to the appearance of conveniently packaged seaweed snacks at Costco.  We take some rice, add a sliced avocado, crumble some seaweed sheets into it, and finish it off with a splash of soy sauce.  It’s like deconstructed vegetarian sushi, and it’s super tasty.  I decided these strong flavors might mesh well with the mild natto taste.  So I mixed some natto in with warm rice, tossed in the other ingredients and voila:
  It wasn’t bad.  The characteristic natto flavor was really subtle.  Granted it wasn’t as tasty as our original natto-free version of this snack, but it was still good.  I’ll definitely eat it this way again.  I’m curious to see if natto could be worked into a sweet dish as well, or maybe pureed and used in something like pancakes.
And just in case Operation: like natto doesn’t succeed, I’ve ordered some K2 supplements from my favorite online health store, iherb.com.

Velomobile!

A few weeks ago B&N – who have generously been allowing me to inhabit their home for the past three months – received a velomobile to try out.  What’s a velomobile you ask?  No need to reach for google, here’s the awesome video they made.  I have a couple of brief appearances in an ill-fitting helmet that I unsuccessfully tried to put on over top of my winter hat.

Kitchen Projects

With my presentation for the upcoming Canadian Geophysical Union meeting in Banff all polished and done, I decided to take the afternoon to complete a couple of food projects I’ve been passively working on:  wheatgrass juice and kombucha.

While organizing the kitchen, I found a bag of wheat berries from my vegan days of soaking and sprouting grains.   Since I’m avoiding grains (especially gluten-containing ones) at the moment, I decided that growing wheatgrass was a good way to make use of them.  So I put some soil in a nice decorative tray, covered some pre-soaked berries with dirt and watered generously.   The fully-grown wheatgrass is actually quite pretty, and decidedly grassy in appearance, smell and taste.

It’s been over 6 inches tall for a few days now, so it was high time for me to harvest it.   Yep, it really just looks like a plate of lawn-mower trimmings:

The grass-pile then went into the Magic Bullet with a splash of water, turning into an emerald-green goo with a subtle lawn-mower-on- wet-grass aroma.

I froze some right from the blender in an ice-cube tray, and strained the rest for immediate consumption.

It’s not something I’ll drink for it’s deliciousness, but it’s nice to have some healthy green stuff to throw into smoothies.

My kombucha mother in its new home.

Project number two was kombucha, a fermented cold tea drink.  To make it, you first need a kombucha “mother” – a symbiotic culture of bacteria and yeast (SCOBY).   If you buy raw kombucha, it contains live cultures (like the active bacterial cultures in yogurt), and if you leave a bit of it in the bottle at room temperature for a couple of weeks, a substantial SCOBY will form on top.

To brew your own fresh batch of kombucha, all you have to do is make a large pot of tea, dissolve some sugar in it to feed the culture,  cool it off with some fresh water and throw in the kombucha mother.    Cover it with cloth so that air can circulate through, and let it sit in a warm place for a week or two.

By then the drink should be only mildly sweet, as the culture will have metabolized most of the sugar, producing B-vitamins and acetic acid in its place.  It should also be fizzy from carbon dioxide produced during fermentation.  The kombucha can be bottled and kept in the fridge before drinking.  I’m taking off to Banff for a week, and I hope to return to a thriving SCOBY and some tasty kombucha tea.

Protein Fluff

Recently I discovered the magical art of making protein fluff.   I like having something sweet after dinner, which usually means something fruity, nutty, or chocolately.    I love this dessert for a number of reasons: it’s quick, simple and fun to make,  it contains protein and is satiating, and it’s really tasty.   Big A loves it too, and that’s always a bonus.   Without further ado, here’s the protocol:
You will need:
  • A large mixing bowl
  • One or two cups of frozen raspberries
  • A splash of milk
  • A potato masher, or failing that, a sturdy fork
  • One or two scoops of protein powder
  • Electric beaters or a stand mixer
  1. In a large bowl, combine several cups of frozen raspberries and enough milk to facilitate mashing.  Despite never measuring the relative quantities of raspberries, milk and protein I use, the fluff consistently turns out the same.
  2. With a potato masher or other mashing device, pulverize the raspberries until they more resemble red goo than fruit.
  3. Add in a couple scoops of your favorite-tasting protein powder.  I use a whey protein powder from Costco that tastes pretty good, and its only offense is being sweetened with sucralose.   Hey, at least it’s not aspartame.
  4. Mix together the raspberry mash and the protein powder with a fork.
  5. Using a stand mixer or hand beaters, whip the mixture for at least 5 minutes.   If it’s too dry and the beaters are just moving stuff around rather than homogenizing it, add a bit more milk.  After a while it will turn pink and puff up to roughly twice its original volume.  I tend to just stop when I notice that the mixture changing colour or volume any longer.
  6. Consume the delicious concoction.  Leftovers can be frozen and briefly thawed, which turns it into a sorbet-like treat.

Bees, Obesity and Epigenetics

The three types of honeybees: Queen, worker, and drone.

My father is a beekeeper, and growing up we had beehives in our backyard and, during extraction time, in our house.  Even so, I didn’t learn a lot about the life cycles of bees; my education on honeybees was mostly practical.   Not everyone knows that honeybees, unlike wasps, die when they sting an animal, and so tend to be less aggressive.   If you don’t swat at them or otherwise threaten them, they usually won’t sting you.

So recently when I started to read the book Fruitless Fall about Colony Collapse Disorder (a mysterious phenomenon affecting beehives in which the worker bees all of a sudden abandon the hive, even with live brood and food stores inside) I was struck by how little I knew about honeybees, given that I’d grown up around them.  For instance, I didn’t know that they weren’t native to North America.  Many food crops use honeybees as their primary pollinator, and I’d always just assumed that they were native.  Not so – they were introduced from Europe, and originated from Africa or Southeast Asia.

And when a book I was reading about epigenetics began with an example of the Queen honeybee, I realized that I didn’t even know how Queens were born, or how they were replaced when a hive’s Queen died.   And it turns out the process by which a new Queen is produced is pretty cool.

For some background, there are three kinds of honeybees: workers, drones, and Queens.   Drones are the male bees, derived from unfertilized eggs.  They don’t have stingers, and they don’t forage food for the hive – their sole purpose it to locate Queen bees while they are outside the hive and impregnate them, after which they die.   Queens are the egg-laying bees in the hive, and typically there is only one of them at a time.  Worker bees are female too, but their lives are spent caring for the brood and foraging for pollen, and they are usually sterile.

Since both worker and Queen bees are female, how does an egg or larvae know whether to grow up into a worker or a Queen?  Interestingly, it’s all about what they eat.  Workers and Queen bees are genetically identical; it is differences in what they are fed early in life that cause epigenetic changes controlling their phenotype.  When a future worker bee is in its larval stage, it is fed royal jelly for three days.  Royal jelly is a secretion from the worker bees’ glands that contains B-vitamins, amino acids, simple sugars, fatty acids, minerals and enzymes.    After three days, they’re taken off this nutrient-rich feed and given nectar instead.  But the larvae destined to become queen bees are given large amounts of royal jelly for a longer period of time, and this triggers the development of ovaries and other physical and behavioural differences.  This effect is produced by the methylation of DNA, one of the main ways in which gene expression is regulated.

While an organism’s genome is fixed, the way in which it is expressed is not.  Our DNA can be altered in different ways so that genes can be effectively turned on and off in response to changes in the environment and varying metabolic demands.   Our contact with the physical environment – through the foods we eat, the air we breathe, the toxins we’re exposed to, and even the temperatures we experience – acts as information to our genes about what kind of world we’re living in.  If we’re not eating very much food, our body thinks we’re living in a time of scarcity, and it up-regulates energy-storing hormones like insulin.   And these epigenetic changes are heritable: mothers who conceived children during famines had children with a greater propensity toward obesity, along with higher blood-glucose and insulin levels.  This makes sense – the newborn’s epigenetics responds to information passed on by the mother’s diet; the baby needs to be prepared to be born into an energy-scarce environment.  Even ailments like asthma may have an epigenetic component – if the mother smoked during pregnancy, or lived in a city with severe air pollution, it could signal that the environment is highly toxic, and the fetus would do well to be born with acute, fast-acting responses to airborne irritants.

A really striking effect of epigenetics can be seen with Agouti mice.  These are mice that have been genetically engineered with the so-called agouti gene, which endows them with yellow fur, a voracious appetite (leading ultimately to obesity), and an unfortunate vulnerability to cancer and diabetes.  When Agouti mice mate, they typically produce obese little yellow Agouti offspring.  But if the Agouti mothers are fed a diet rich in folic acid and other chemicals which are methyl donors, their babies are brown-furred, skinny, and healthy.  The agouti gene is turned off through methylation, and it can no longer be transcribed.

Epigenetics can have a profound effect on behaviour too.  Rats whose mothers are highly nurturing as pups – licking them and tending to them often – grow up to be calm, relaxed, mellow adult rats.  But pups who have been largely ignored by their mothers grow up to be anxious, neurotic adults.  Again, these behavioural differences arise because the mother’s actions transmit information to the newborn rat pup about the environment.  If the mother is nurturing, the baby rat gets the signal that the environment is safe and food is readily available.  If the mother is neglectful (presumably because she is concerned with protecting her babies or finding food), the message is sent to the pup that the environment is dangerous or food is scarce.   In such an environment, anxiousness or nervousness may be advantageous.  A rat with a false sense of security is more likely to be killed in a predator-filled environment than one that is skittish and careful.

Happily, the dynamic nature of epigenetics means that it’s not written in stone as our pure genetics are.  Healthy eating, moderate exercise, happy thoughts, friends, minimizing stress – I think pretty much all the things that are generally recognized as elements of a healthy, contented life are going to have a positive epigenetic effect.   But it’s nice to know that we have a bit of genetic momentum, and the good things we do for ourselves can continue to help our children and grandchildren.

Recent reading

As my husband can surely attest to, I have a tendency to jump headfirst into whatever hobby, interest or pursuit has grabbed my attention.  From triathlons to trail running, kettlebells to knitting, economics to geophysics; if I learn about something new or try something new – and I like it – I want to learn more about it, or do more of it, or get better at it.  Currently I have a small family of kettlebells which have taken up residence in our living room, a drawer full of yarn, looms and knitting needles, and a stack of owned, library-borrowed, or downloaded books about human nutrition and metabolism.   And the current podcast count on our iTunes is 733, thanks to such prolific podcasters as Robb Wolf and Our Natural Life.

I’m a bit of a health/nutrition nerd, and I’ll frequently read textbook snippets off of Google Books for fun.  But I really love books thatare scientific in nature, but still read a bit like a novel.   My favorite on-the-go book at the moment is Queen of Fats: Why Omega-3s Were Removed from the Western Diet and What We Can Do to Replace Them.   (I think book preferences must run in the family a bit, because I sent this book to my mom’s kindle and she’s finished it before I have! )  I’ve had this book on the computer for some time now, but wasn’t enthusiastic to start reading it because of the title, which makes it seem like one of those ubiquitous single-nutrient popular health books about how deficiency in this one nutritional element is the source of all our health woes.   Fortunately I was wrong – although I haven’t yet got to the “What We Can Do to Replace Them” part of the book, what I have read is really good.

The author (Susan Allport) writes about the history of omega-3 fatty acids: how they were discovered and how scientists learned about their role in human health.  It’s an interesting story, and you get to learn all sorts of fun facts about fats along the way.  It’s fairly general knowledge these days that omega-3 fats are healthy and that we should probably all eat a whole lot more of them.  But beyond that, I didn’t know much about them.  Why are they good for us?  How are they different from other fats?  Here’s a little primer:

Fats come in two general flavours: saturated and unsaturated, which refers to the number of double bonds in the molecule.

We all know that there are certain things that we need to eat in order to survive (or thrive); essential vitamins or minerals that our bodies can’t themselves make, but luckily other creatures or plants can.  So we eat them, get what we need, and we’re healthy.  And of course we function best on a certain balance of macronutrients – fat, protein and carbohydrates – that our body uses for fuel and to build and repair tissues.   Just like there are essential vitamins and minerals, so too are there essential macronutrients.  In the case of protein, there are essential amino acids, the building blocks of proteins.   In the case of fat, there are essential fatty acids, the building blocks of triglycerides.  (There aren’t any “essential” carbohydrates – in fact, our body can function pretty well without them altogether if it’s forced too. )

The essential fatty acids are called omega-6 and omega-3, because of the location of their double bonds.   The omega designation comes from a quotation from the Book of Revelations, in which God is described as the “alpha and omega, the beginning and the end, the first and the last”.  The omega end of the fatty acid is the one with the red, which has a methyl group attached to it.  The omega-3 fatty acid has its first double bond 3 carbons from this end, while the omega-6 fatty acid has its first one 6 carbons from this end.  There’s also an omega-9

fatty acid, but our body is able to manufacture it, so it’s not essential in the diet.  These essential fatty acids play a unique role in the body.  When we ingest, digest and absorb fat into our body, it can be used as fuel, and it can be used to build tissues.   Every cell is surrounded by a phospholipid bilayer, two layers of molecules that have a phosphate head and two fatty acid tails.  Proteins and fats can be embedded in this membrane to make it more or less fluid, and to transport substances in and out of the cell.

These phospholipids bilayers need to be relatively fluid; to achieve this, they need to have at least one unsaturated fatty acid in their tail.  Saturated fatty acids are more solid at a given temperature than unsaturated ones, because unsaturated fatty acids have double bonds which give the molecule a kink, and they can’t stack together nicely the way solids like to exist.  So there’s an enzyme that assembles these fatty acids, and it has a really strong preference for fatty acids with 20 carbons, just like the omega-6s and the omega-3s.  But apart from that, the enzyme is, as Allport puts it, “promiscuous”.  It will take whatever it can get, and if there’s tons of omega-6′s around, that’s what it’s going to use to make your cell membranes.   This is a literal case of “you are what you eat”: if you eat food containing a high omega-6: omega-3 ratio, then your cell membranes will be made out of primarily omega-6 fatty acids.

But that’s not the end of the road for these EFAs.  They don’t just sit idly by in our cell membranes, but rather they play an active role in our bodies’ signalling processes.  Prostaglandins or eicosanoids are produced from the EFAs; they are called autocoids, and they act like local, ephemeral hormones in the body.   If a part of the body is injured, eicosanoids will be produced from local EFAs, and they in turn produce different effects in the body.  If the eicosanoid is one that was produced from an omega-6 EFA, it will tend to have an inflammatory effects, while the omega-3 derived eicosanoids tend to be anti-inflammatory and more mild in nature.   So where do these “local” EFAs come from when eicosanoids are needed?  They’re snipped straight from the phospholipid bilayer.  And once again, the enzyme that does the snipping isn’t discriminating: either omega-6 or omega-3, it doesn’t matter.  So if you’re eating a lot of omega-6 relative to omega-3, your cell membranes are going to be composed primarily of omega-6 EFAs, and the eicosanoids produced by your body will tend to be the pro-inflammatory omega-6 derived variety.  Many pain and anti-inflammatory medications like aspirin, ibuprofen, and acetaminophen work by inhibiting the enzyme that turns omega-6 into eicosanoids; but you can do the same thing just by changing the relative amounts of omega-6 and omega-3 EFAs you’re eating.   The take-home message:  cut down on omega-6s (found in many industrial seed oils and nearly all processed food) and up your intake of omega-3 (eat fish, take fish-oil supplements).  Then maybe you can forgo that ibuprofen after a long run, along with all the concomitant side effects.

GE foods, continued

After reading up a bit on GE foods, I realized there was a substantial gap in my knowledge about one of the most contentious issues on the subject: Monsanto and its Roundup-Ready line of plant seeds.  I learned a little bit about it in one of my high school classes, and a few things I’ve picked up here and there, but I’ve never done any real research into the matter.   So it’s about time I did, especially given the recent deregulation of GE alfalfa and the subsequent protestations; before I become exasperated with anti-GMO sentiments, I should at least examine some of their main points.

First, some fundamentals about herbicides in general and RoundUp™ in particular:

Chemical structure of glyphosate

  1. Most herbicides work by interfering with a plant’s enzymes.   Enzymes are catalysts in reactions, breaking down inputs (substrates) into end products that can be used in other reactions.  If you mess around with an enzyme that is essential in one of the plant’s metabolic pathways, it can’t survive.
  2. The active ingredient in Roundup  is glyphosate, which acts as a competitive inhibitor of the enzyme 5-enolpyruvylshikimic acid-3-phosphate synthase (EPSPS). ( I love crazy long chemical names.)  This means that it binds to the enzyme, preventing the substrate from doing so.  If the substrate can’t bind to the enzyme, the necessary end products for that stage of the pathway can’t be produced. In this case, the plant cannot produce the amino acids tyrosine, tryptophan, and phenylalanine that are necessary in protein synthesis.  EPSPS is found in the chloroplasts of plant cells, so animals don’t have them.  Instead, we get these amino acids from eating other plants or animals.
  3. Glyphosate is broad-spectrum, and can’t be used to target specific plants.  That’s why up until Monsanto stepped in with its GE plants, it could be used only for weed control prior to planting; otherwise it would kill the entire crop along with the weeds.  Throwing the baby out with the bathwater as it were.
  4. To get around this unfortunate side-effect, you can engineer glyphosate-tolerance into the plants you want to keep.  Like all of the other GE foods I’ve learned about, this is such a simple, elegant solution for weed control.  There are two ways to do this: one is to allow the plant to produce EPSPS that is not affected by glyphosate, and the other is to give it the ability to produce an enzyme that inactivates glyphosate.  Both modifications have been developed, separately and combined, using GE (after failed attempts using “traditional” techniques of mutagenesis and selection. )  The gene that codes for glyphosate-resistant EPSPS comes from Agrobacterium, which is often used in recombinant DNA, while a gene coding for a glyphosate-degrading enzyme derives from another common soil bacterium.
  5. The new proteins produced by the transgenic plants degrade rapidly in even mildly hot or acidic conditions, not holding up even a few minutes in the highly acidic environment of our stomachs.   They are not allergenic, and they don’t interfere with plant growth or make the plant dangerous to its environment.
  6. Glyphosate is readily adsorbed by soil particles, making it immobile in the environment.  Basically it just sticks to soil particles until it is degraded by soil microbes, which means it’s not going to travel through the environment killing plants indiscriminately.  And it’s not going to enter our water supply or pollute rivers and lakes.
  7. One big downside I’ve read about: it’s moderately toxic to fish.  But because it binds so strongly and easily to soil particles, this is less of a concern than it otherwise would be (given that glyphosate is also highly water soluble).
  8. It’s not something you want  to rub on your skin and eyes, but there’s no evidence of carcinogenicity, and little evidence of toxicity to humans.   Some people  have died from ingesting about 200ml of Roundup, while others have had no side effects from as much as 500ml.  Incredibly, there were 80 cases of intentional ingestion!

I don’t know, Roundup and Roundup-ready seeds seem like a good idea – they allow us to use a herbicide of relatively low toxicity compared to others in use.  Ideally we wouldn’t use any herbicides, but that’s unrealistic.  So in theory, I find nothing objectionable about Roundup.  Now, the corporate practices of Monsanto are another matter; they’ve done some truly evil things, but one can’t fault the science for that.

As for the whole idea of patenting an organism and trying to render it infertile… well, I see this as being similar to the issue of drug patenting.  Drug companies provide life-saving products, but they are also profit-seeking entities.  Necessity is the mother of invention, but so is money.  Pardon the very rudimentary economics, but if there’s less incentive for these companies to research quality-of-life-improving drugs, then there will be fewer such products available.   So it would be nice if we could save a lot of lives by giving  drugs at cost to people who can’t afford them, we have to be concerned about black-market dealings and maintaining incentive-worthy prices for affluent consumers.

So for GE organisms, it’s the same thing.  Why would Monsanto research and develop glyphosate-resistant plants if it can’t patent them and prevent farmers from reseeding from their first generation of Roundup-ready plants?  From what I’ve read, glyphosate-based herbicides are much better for human and environmental health than their alternatives, so Roundup is producing positive externalities for a lot of people.  If we destroy incentives for companies to develop better pest control strategies through genetic engineering, we’re going to lose those potential benefits.

I’ll have to read on about Monsanto and glyphosate-based herbicides; clearly this is not the whole story   In the meantime, I’m going to watch “The World According to Monsanto” while I’m on my trainer tonight.