Lean how calcium ion concentration dictates whether a muscle contracts or not. Explore how myosin II, using ATP, interacts with actin filaments to enable muscle contraction. Learn about the regulatory roles of proteins tropomyosin and troponin, and the crucial part calcium ions play in muscle contraction and relaxation. This is a deep look into muscle cell anatomy and function. Created by Sal Khan.
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- What exactly happens during rigor mortis?(6 votes)
- In order to "block" myosin from actin (relax muscles) we need ATP. When you're dead, there's no ATP to make the muscle relax and all the Calcium ions diffuse out of the Sarcoplasmic reticulum causing the muscles to enter their resting state which is contracted.
Another more visual video about the muscular system you might find helpful https://www.khanacademy.org/partner-content/crash-course1/crash-course-biology/v/crash-course-biology-130(15 votes)
- Would any type of involuntary muscle contraction such as a seizure or the positions taken by cerebral palsy sufferers be caused by unregulated Ca ion influx or malfunctioning of troponin?(7 votes)
- It is caused by unregulated Ca ion influx as a consequence of uncontrolled activation of neurons and generation of action potential. This allows the release of ACh into neuromuscular junction that leads to opening of Na and Ca channels and Ca influx.(6 votes)
- If the tropomyosin is in place and blocks the myocin from doing its job, what prevents the myocin from twitching in place and burning atp?(4 votes)
- At least one of the conformational changes in the cycle that's required for ATP hydrolysis is dependent on binding to actin. Without being bound to actin, the myosin cannot take up the active form to hydrolyze ATP.(7 votes)
- Why Ca ion is a very important factor to makes the muscle contract?(4 votes)
- Ca+ is used as an ion on the terminal button of a neuron. It is used to stimulate the release of neural transmitters used in muscle contractions.(5 votes)
- Are the long pieces of actin and tropomyosin composed of one huge protein? Or are they repeating patterns of polypeptides?
Also, if all the tropomyosin does in the absence of calcium ions is prevent the myosin from climbing up the actin but allows it to stay bound where it already is, how come when we relax a muscle everything moves back to the way it was prior to the contraction? Shouldn't everything stay the same unless we actively move it back?(5 votes)
- Those are long fibers of proteins.
2. Sounds reasonable but you are incorrect.
For muscle contraction to happen, myosin actin has to be in that 'tense' state. That's why everything moves back to the original state after muscle contraction. Imagine, if everything just stayed like there is hydrolized ATP, it is called rigor mortis and happens right after the death. Muscles are contracted for a long period.(3 votes)
- why is it that when a doctor suspects a myocardial infarction he will check the troponin levels how does that tell him anything (why would there be an increase of troponin in the blood when there is an myocardial infarction) it seems to me that there is a bigger need for more calcium in the blood to control the troponin(4 votes)
- If you have an infarction some heart cells die and burst, they release troponin into the blood. Normally there is less then 0,1 ng/ml troponin in the blood but after some time this value goes up significantly if you had an infarction. The amount of troponin correlates with the amount of damaged cells.
I do not understand your point about Ca .What means "control the troponin"?(2 votes)
- How can you relate this concept when, for example, a person has low levels of calcium in the blood (hypocalcemia) and experiences tetany / muscle spasms?(3 votes)
- When there is a low calcium level, the sodium channels on the muscle cells become more excitable. As a result, they open and generate an action potential with much less perturbation than is typical. This leads to some spontaneous action potentials which lead to contraction and tetany. It is likely that the calcium interacts with the external component of the sodium channels to depress their activity.(4 votes)
- Why is it that clinical presentation of high serum Ca conc. causes muscles to be relaxed or "calm" and low serum Ca conc. causes muscles to twitch/spasm. However here in the video, high Ca conc causes the unbinding of troponin on tropomyosin which allows myosin to proceed further with the continuation of muscle contraction? I would think it would be the other way around and this is causing a bit of confusion for me...UNLESS high SERUM conc would most likely mean a low Ca conc in the CELL so then -->Ca unbound to troponin-->tropomyosin maintains its shape-->myosin unable to proceed further down the actin filament ?(3 votes)
- For muscles to contract, Ca from sarcoplasmic reticulum is required. Not serum Ca necessarily.
Meaning that high blood Ca is low cell Ca and vice versa.(3 votes)
- there is a binding myosin in my biceps then if i extend my arm passively what will happen? does that myosin rupture?(3 votes)
The crash course video will give you a better overview. In summary, the majority of our muscles work in pairs. The bicep brachia muscle is on the anterior arm while the triceps brachia muscle is on the posterior arm and each crosses the elbow joint to the forearm. When extending your elbow, the biceps brachii m. Relaxes and the triceps brachii m. Contracts, it gets bigger as the Myosin slides the actin toward the middle of the designers. When flexing the elbow, the biceps brachii m. Contracts, gets bigger, pulls the forearm toward the arm and the triceps brachii m. Relaxes. No, nothing ruptures in normal movement, the binding is released as the calcium returns to the sarcoplasmic reticulum. muscles on the anterior body tend to flex the body, muscles on the posterior body tend to extend the body when they both do the same thing, contract.(3 votes)
- What does ATP and ADP stand for?(2 votes)
In the last video, we learned how myosin-- and myosin II in particular-- when we say myosin II it actually has two of these myosin heads and their tails are inter-wound with each other-- how myosin II can use ATP to essentially-- you can almost imagine either pulling an actin filament or walking up an actin filament. It starts attached. ATP comes and bonds onto it. That causes it to be released. Then the ATP hydrolyzes into ADP and a phosphate group. And when that happens, that energy's released. It puts this into a higher energy state. It kind of spring-loads the protein and then it attaches up another notch on the actual actin filament and then the phosphate group leaves and that's where the confirmation change in this protein is enough. It generates the power stroke to actually push on the actin filament-- and you could imagine, either move the myosin-- whatever the myosin is connected to-- to the left or whatever the actin is connected to to the right. We're going to talk a lot more about what they're connected to in future videos. Now, a couple of questions might have been raising in your head. This guy had so much effort to pull on this thing, right? There's some tension pulling in the other direction, right? I said this is what happens in muscles, so there must be some weight or some other resistance. So what happens when this releases? At the first step when ATP joined and this released, wouldn't the actin filament just go back to where it was before? Especially if there's some tension on it going in that direction. And the simple answer to that is, this isn't the only myosin protein that's acting on this actin. You have others all along the chain. Maybe you have one right there. Maybe you have one right there. They're all working at their own pace at different times. So you have so many of these that when one of them is disengaged, another one of them might be in their power stroke or another one might be engaged. So it's not like you have this notion of, if all of a sudden one lets go, that the actin filament will recoil back to where it was. Now the next question that you might be thinking is, how do I turn on and off this situation? We have command over our muscles. What can turn on or off this system of the myosin essentially crawling up the actin? And to understand that, there's two other proteins that come into effect. That's tropomyosin and troponin. And so I'm going to redraw the actin-- I'll do a very rough drawing of the actin filament. Let's say that that's my actin filament right there with its little grooves. It's actually a helical structure. And actually, these grooves-- it's kind of a helical-- but we won't worry too much about that. What we drew so far, at least in the last video, you had these little myosin. You can view them as feet or head or whatever that keep attaching to it and then based on where they are in that ATP cycle, they can keep getting cranked back up or spring-loaded and go to the next one and push back. Now, on top of this actin, you actually have this tropomyosin protein. And this tropomyosin protein, it coils around the actin. So this is our actin right here. This is one of the two heads of the myosin II. And then we have our tropomyosin. Tropomyosin is coiled around. It's a very rough sketch, but you can imagine it's coiled around and it goes back behind it, then it goes like that, and then it goes back behind it, then it goes like that. So it's coiled around it and the important thing about it is, if there's-- let me take a step back. It's coiled around and it's attached to the actin by another protein called troponin. Let's say it's attached there and-- this isn't exact, but let's say it's attached there, and there, and there, and there, and there by the troponin. So let me write this down. So you can imagine, the troponin is kind of like the nails into the actin. So it dictates where the tropomyosin is. So when a muscle is not contracting, it turns out that the tropomyosin is blocking the myosin from being able to-- and I've read a bunch of accounts on this and I think this is still an area of research. It's not 100% clear one way or the other. Tropomyosin is-- or maybe both-- blocking the myosin from being able to attach to the actin where it normally attaches so it won't be able to crawl up the actin-- or sometimes the myosin is attached to the actin, but it keeps it from releasing and sliding up the actin to keep that walking procedure. So the bottom line is that this tropomyosin kind of blocks the myosin head-- this is the myosin head right there-- from crawling up the actin, either by physically blocking its actual binding site or if it's already bound, keeping it from being able to keep sliding up the actin. Either way, it's blocking it and the only way to make it unblocked is for the troponins to actually change their confirmation, for them to change their shape. And the only way for them to change their shape is if we have a high calcium ion concentration. So if you have a bunch of calcium ions, if you have a high enough concentration, these calcium ions are going to bond to the troponin and then that changes the confirmation of the troponin enough to move the configuration of the tropomyosin. So let me write this down. So normally, tropomyosin blocks, but then when you have a high calcium ion concentration, they bind to troponin and then the troponin, they change their confirmation so it moves the tropomyosin out of the way. So when it moves out of the way, you have a high calcium concentration, bonds troponin, moves tropomyosin out of the way, then all of a sudden what we talked about in the last video-- these guys can start walking up the actin or pushing the actin to the right, however you want to view it. But then if the calcium concentration goes low, then the calciums get released from the troponin. You need to have enough to always hang around here. If the concentration becomes really low here, these guys will start to leave. So then the troponin goes back to, I guess, standard confirmation. That makes the tropomyosin block the myosin again. So it's actually-- I mean, I can't say anything here is simple. This was only discovered maybe 50 or 60 years ago and you can imagine to actually observe these things or to create experiments to definitively know what's happening-- nothing is simple, but the idea is simple. Without calcium, the tropomyosin is blocking the ability of the myosin to attach where it needs to attach or slide up the actin so it can keep pushing on it. But if the calcium concentration is high enough, they will bond to the troponin-- which essentially nails down the tropomyosin that's wound around the actin and when they change their confirmation with the calcium ions, it moves the tropomyosin out of the way so that the myosin can do what it does. So you can imagine already, we're building up a way for-- one, for muscles to contract, but even better, for us to control muscles to contract. So if we have a high calcium concentration within the cell, the muscle will contract. If we have a low calcium concentration again, then all of a sudden, these will release. They'll be blocked, and then the muscle will relax again.