Gastrointestinal | Digestion & Absorption of Proteins

I ninja nerds in this video we are going to talk about protein digestion and absorption we have a lot of things to talk about so let's go ahead and get started all right so what we're gonna do is we're gonna take a scenario just like if you guys haven't seen already please go see our video on carbohydrate digestion and absorption we do kind of the same diagram what we're gonna do the same diagram for lipids as well so what we're gonna do in this situation is we're going to start eating a nice chicken you know like drumstick alright there's tons of packed full of proteins in there right so we're gonna digest this drumstick but here's what I want to do before we start getting into all the details of protein digestion absorption what I want to do is I just want to get this quick little basic over because there's gonna be a lot of little stuff that we're going to talk about in this video so I want us to get just a basic understanding of what this protein digestion is gonna take like what kind of events are gonna take place and what kind of events are will take place in the absorption as well so when we talk about protein digestion what I want you to remember here is in the basic terminology when you talk about anatomy or biochemistry and stuff like as you hear the terms anabolism and catabolism well protein digestion is primarily going to be a catabolic pathway it's a catabolic pathway now what that means is is you're going to be breaking down large molecules into their small little individual units what I mean just like when we talked about an carbohydrate eyes that digestion we're taking polysaccharides like we took amylose and amylopectin and broke them down into monosaccharides in the same way what we're gonna do is we're gonna take these large proteins because all proteins are is they are going to be these special macro molecules that are consisting of amino acids so here I'm gonna put all these dots here you guys have watched your videos you've seen this probably once or twice before this is a protein this is what we're gonna have we're gonna consider this to be a protein now proteins we can say that they're like large polypeptides so we can say here this is going to be our protein molecule and in this case it's going to be a very very large poly peptide what we want to do throughout this process is we want to break down this protein into its constituent units and we're gonna do it through a mechanism which we call hydrolysis it's gonna be primarily through hydrolysis mechanisms what does that mean that means that you're going to be adding water into the reaction to break the different bonds in this case you're breaking peptide bonds so it's gonna be the hydrolysis of peptide bonds and we'll talk about what peptide bonds were actually breaking we get into this different specific enzymes but here's the basic thing we're gonna take this big protein with this large polypeptide and break it down into each individual individual monomer all right in this case that would be these little things here these little dots and these little dots that we're gonna break it down into is going to be your amino acids so now proteins are what we're going to refer to as a polymer a long chain of these different monomers are small little basic units and we're gonna break down this big polymer into these small little units called monomers the reason why is it's really really really hard and inefficient to digest and actually absorb these different types of proteins so because of that we want to break them down into small little components because it's going to be more efficient and easier to absorb the amino acids in that way so now that we got this basic concept that kept this protein digestion is a catabolic pathways which are large polypeptides with just components or constituents of amino acids we're gonna break them down by a hydrolytic mechanism meaning we're adding water into these bonds what kind of bonds peptide bonds and we're gonna break it into each individual or basic unit which is the amino acids so now that we understand that let's go ahead and get started and start digesting this chicken piece ok so now we're gonna start digesting this piece of chicken so let's say first we come to a special organ that is a part of the GI tract alright this guy we talked about this one in the gastric secretions phases specifically in the cephalic and in the gastric well there's special types of cells right there special types of cells here that are called chief cells and these chief cells they were the ones that were primarily responsible so we're put here chief cells all right these are our chief cells and what these chief cells are doing if you remember is they were see creating a protein digesting enzyme called pepsin ojen into the lumen here what we're gonna do is we're gonna say that this is the lumen this is going to be the GI tract or the alimentary canal here so we're gonna say here we're gonna see create this molecule this pepsinogen into this portion here of the GI tract so we're gonna say that we're at the level of the stomach because there is no protein digesting enzymes in the oral cavity the pharynx are in the esophagus so the first organ that we come into contact with this protein digesting enzyme is in the stomach there is another one called renin but we're not going to talk about that because it's really only functional and younger kids to digest milk protein so we won't talk too much about that so now first thing I want to do is we're gonna bring pepsinogen into the cell I mean into the lumen when the pepsinogen is brought into the lumen if you remember we talked about there was these parietal cells and the parietal cells were secreting a molecule called hydrochloric acid and what the hydrochloric acid was doing is is it was helping to be able to decrease the peach in the pH in the lumen of the and what that does is is that this pepsinogen is an acidic type of enzyme it loves to be in acidic environments so in acidic environments around the pH of we can say anywhere 1.8 to 3.5 this is its optimal range here the hydrochloric acid concentration if it's nice and high will stimulate the conversion of pepsinogen into its active form which is called pepsin sweet deal now what does pepsin do perhaps it is really cool because it's kind of like a Auto activator because you know what else is really cool about pepsin is any other pepsinogen that is secreted this pepsin the active form so here's the active form of the enzyme this is the inactive or the precursor form of it this activated pepsin can come over and stimulate pepsinogen more pepsinogen 2 currently converted into pepsin so it's kind of like an auto activator once he's active he can go and activate more pepsinogen molecules and turn them into more pepsin so that's a pretty cool thing - it seems a very efficient mechanism all right cool but again as you know if the pH is getting really really high anywhere appoint 5 it can convert the pepsin back into pepsinogen because this enzyme does not like to be in alkaline situations it prefers acidic situations now here's our protein we're going to use that diagram here and again if you remember proteins have a amino end and they have a carboxy end they also have a alpha carbon with a specific R group but we're not going to talk about those in this video again this isn't a biochemistry video this is going to be specifically on the physiology of it but here's going to be our protein but we're going to refer to this as a very large polypeptide so here's our large polypeptide what we're gonna do is is we're gonna bring this pepsin over here pepsin is so cool because he actually loves to break down large polypeptides so what he does is he comes over here and he converts it's this large polypeptide into smaller polypeptides so now what I'm gonna do is I'm gonna break this large polypeptide up let's say we break it into like two units so now look I'm gonna have something like this here's an amino end here's a carboxy end and here's gonna be like a couple amino acids here right and I'm gonna have another piece here let's say I have another piece just like this and again here's the amino end and here is the carboxy in and we'll have some amino acids on this thing as well so now we have from this large polypeptide we have smaller polypeptides so now what we did is we had the pepsin pepsin came in cleave some peptide bonds and converted this large polypeptide into a small to multiple small poly peptides no it's so cool about this enzyme it digests our breaks specific bonds so pepsin is a pretty cool enzyme and what pepsin does is imagine here for a second I'm gonna take here a chain of pet like a peptide here right here's our polypeptide or a large polypeptide and let's say here I have a string of amino acids here but there's some particular amino acids here that he really likes to target you don't have to know their structure like completely I just want you guys to get an idea here of what they are they're aromatic amino acids so he targets aromatic amino acids one of them is called tyrosine so this is called tyrosine right here this is one type of amino acid that he likes to cleave like on the carboxyl side another one is called phenylalanine so another one is called phenyl alanine so this right here is called phenyl alanine and there's other ones I'm not going to keep going through these but here we'll have one more and this is called tryptophan so what he likes to do is he likes to break bonds on the carboxy side so here's the amino terminus here's the carboxy terminus he loves to break the actual bonds on the carboxy side or carboxy terminus of amino acids such as tryptophan phenylalanine and tyrosine by doing that we're going to break these large polypeptides into smaller polypeptides cool deal that covers this part now we come to the next segment so then what happens is the stomach will actually undergo its motility it'll undergo peristalsis where it'll contract and squeeze out some of the chyme into the first foot of the small intestine refer to as the duodenum in the duodenum we have special types of you know mucosal cells that pick up the different concentrations of the kind like if it's high in protons if it's high in different types of carbohydrates if it's high in protein digesting products or fats and what it does it signals the release of a bunch of different types of hormones some of these hormones are like cholecystokinin secretin GIP which is glucose insulin o tropic peptide there's a bunch of these different ones but the one that's really really significant in this is the cholecystokinin CCK what cholecystokinin does is is he comes to the pancreas and he stimulates a special area in the pancreas called the Ascend as' so what the Ascenta says is this just kind of like this little bulb doubt region here so imagine I kind of like zoom in like it's usually right here what happens is this a sinister Eanes it like imagine there's the duct and this is lying with like what's called a sin are cells and what happens is is CCK or cholecystokinin will act on these different cells here imagine there's a receptor for the cholecystokinin will do is is it'll trigger these cells to start releasing different types of digestive enzymes and the digestive enzymes that it releases are going to be protease is there's a bunch of other ones like amylase and lipase and nuclease but in this video we're only talking about the proteases what are some of these proteases that are released into the duodenum particularly through what's called the apparel pancreatic ampulla it's just where the common bile duct and the main pancreatic duct fuse they form is called the ampulla of Vater or the pout of pancreatic ampulla and then whenever there's a muscle there that relaxes it opens up this substance the pancreatic juice and even bile to get released out here into the duodenum so where we're at right now is we're saying we're at the level of the duodenum now once we're at the duodenum there's a bunch of different enzymes released here let's do these in this purple color there's a bunch of them we're gonna talk about three of them okay the first one that we're going to talk about is what's called trip cinnamon now here's the thing when I told you that we released these proteases the proteases are technically inactive they get activated in the lumen of the duodenum so they're secreted in the in active form when they get into the duodenum this trypsinogen molecule is so cool there's a special enzyme that's present on the epithelial cells the simple columnar cells of our duodenum this enzyme right here is called inteiro kinase entero kinase and what entero kinase is it's kind of like around that's a comic a brush border enzymes actually and what it does is is whenever trypsinogen comes it can get activated by that inteiro kinase enzyme so the entero kinase can then stimulate trypsinogen what basically it just Cleaves off a specific like peptide sequence off of this enzyme and turns it into the active form the active form of this enzyme is called trypsin so the active form of this enzyme is called trypsin other chemicals that are released into this vicinity that follow this is going to be another one and this chemical is called kymo trip Sinnoh giin chymotrypsinogen and there's two other ones one is called pro carboxy peptidase and there's one more which is called pro elastase what happens is as trypsin is so cool that once he is activated by the entero kinase enzyme he can do four things alright ready he can take and see this trypsinogen that was activated by enteric ionics we're gonna have more of it right because we're releasing out tons of these enzyme thousands this trypsinogen can get activated by the already activated trypsin because trypsinogen got converted into an taro kinase there's going to be a ton more trypsinogen coming out here when more of the trypsinogen come out here this already activated trypsin can activate some of those trypsinogen molecules and convert those trypsinogen molecules into more trypsin that's cool then this trypsin we're going to take this one as example here he can come and activate every single one of these enzymes so what happens is chymotrypsinogen is going to be activated here let's do these in different let's do the arrows in different colors so we don't confuse it here alright so let's do this chymotrypsinogen and a red color let's do this one in this blue color and then let's do this pro elastase in this pink color what trypsin will do is he will come and stimulate each one of these steps if he stimulates each one of these enzymes he converts them into their active form because again under this this is the inactive form in active same thing here in active meaning they can't do anything they can't cleave any type of polypeptide yet so now what happens is trypsin is going to come down here and activate chymotrypsinogen he'll cleave off a specific sequence they're determined to turn them into the active form which is called kymo trypsin all right sweet so now we have chymotrypsin the next thing is will cleave a portion of pro carboxy peptidase annual cleave off a portion of pro elastase converting them into their active enzymes so get rid of the pro on both of these so you're gonna have carboxy peptidase and there is a type A and type B we're not gonna worry about that right now but just do you know that there is two types and it's gonna convert Pro E last days into elastase so now we have four pancreatic protease a--'s that we want to talk about now because we had pepsin and if you remember pepsin broke down large polypeptides into small polypeptides by cleaving peptide bonds where there was tryptophan phenylalanine and even tyrosine on the carboxy side of it these enzymes they kind of target around the same area particularly chymotrypsin he'll target the same thing so imagine here we have these small polypeptides we're gonna take it through here now what happens is we'll take each enzyme one at a time so let's take the first one which is going to be trypsin so let's take him first the first thing is going to be trypsin digestion if trypsin acts on this small polypeptide he specifically Cleaves bonds where there is a lot of lysine and arginine okay so he'll cleave a lot of peptide bonds specifically where there's a lot of lysine and there's a lot of arginine so that is what he is going to focus on so wherever there's a lot of these two guys he's going to cleave these guys here so to cleave the pep hyebin's particularly on the carboxy side so for example pretend that that amino acid right there is a lysine pretend that that amino acid right there is an arginine what he'll do is he'll come over here and he'll break these bonds right there okay so he'll break these bonds there is like an exception but again this isn't a biochemistry lesson here but just remember if you want to he can't do it if prolene is like right next to them okay but again not super specific here just know that trypsin can break down small polypeptides into even smaller polypeptides particularly we would like if it can break it down into maybe something like this this is called a tripeptide so we have three amino acids together this right here is called a tri peptide another one that we would like to see ideally is maybe even die peptides okay then there's the next one so this is going to be done by trypsin so trypsin is primarily going to be targeting the bonds which are going to be having lysine and arginine there all right then you go to the next guy chymotrypsin so let's take another small polypeptide here and let's treat this one with chymotrypsin so we'll have this one right here because this guy in this guy had the same attacking point so here's my small polypeptide here and i am going to use in this one chymotrypsin so now I'm going to use kymo trypsin and when chymotrypsin acts here he particularly targets the same thing as pepsin did so if you remember it targeted what amino acids it targeted things like tryptophan phenylalanine and tyrosine all right we already had all these here I might as well just for kicks let's just throw tryptophan in there all right a tryptophan is kind of like this here if you guys I know you guys are interested right we have a five carbon ring right here you have a nitrogen right here right and you have a benzene ring coming off here like this right and there's even one more bond like this right there okay so this right here is tryptophan but remember we said there was two different things here if we cleave this bond this bond sorry not this one here this one here and this one here this was done by what type of enzyme well it was done by pepsin so this could be done by pepsin well guess who else can come and do the same exact thing chymotrypsin so chymotrypsin can also target the same exact thing there okay so what type of things will he target here we're gonna denote them here he'll target peptide bonds with tryptophan TRP peptide bonds with tyrosine tyr and peptide bonds with phenylalanine and specifically on the carboxy terminus when he does that he's going to break down these small polypeptides into what same thing that trypsin did dipeptides and tripeptides so again this will be our try peptides and this will be our dipeptides okay cool so that's what we know so far one more thing is this pro carboxypeptidase and this pro elastic so now we're going to do is we're going to take these polypeptides they're these small ones and let's keep them going here for these guys okay so what carboxy peptidase and the last days to do is they target in the same exact fashion so pretend here what I'm gonna put carboxy peptidase and elastase and what they're going to do is they are going to specifically attack the carboxy end so they come at the carboxy end so imagine here I have this protein like this there's gonna be I'm gonna make it linear like this here's an imino end on this side and here's the carboxy end on this side let's say here's an amino acid amino acid amino acid amino acid these guys are like little pack hands and what they do is they come here on the carboxy side and they just start cutting these at the carboxy and one at a time so that's pretty cool and by doing that when they function like this they're gonna start releasing these amino acids out so preferably we'd like for them to spit out maybe some amino acids an individual one or they might even only be able to go to the point of two amino acids linked together or maybe even three amino acids linked together and again you know what should all of these be this should be a amino acid this one here should be a dipeptide and this one right here can be a tri peptide okay so cool we know how these enzymes are functioning whoa let's go to the next part the next part is we get to the actual intestinal cell this could be at different points of the small intestine primarily absorption of these different proteins is occurring in the small intestine duodenum jejunum ileum we're gonna just not be too specific and just say this is a part of the small intestine and this is going to be a inteiro site and intestinal cell so let's denote that here the top here this is a inteiro site now histologically and taro sites they do have like if you look at Anantara site here they do have these cytoplasmic extensions called micro villi these things right here called micro villi and these micro villi have a lot of these different types of brush border enzymes present on them I'm going to represent it here in blue here's a brush border enzyme and then I'm gonna have another one which is going to be purple this is going to be a nother brush border enzymes of the micro villi is to increase this surface area for chemical digestion and for absorption so what I have here on this surface is I have these things called brush border enzymes and there's of two types the purple ones we're just gonna say here let's make it the amino peptidases we're gonna make this the amino peptidase there's no preference here I'm just picking whatever color just makes sense here and then we're gonna make the blue one the dye peptidase is okay so we're gonna make the blue one the dye peptidases now these are the easy ones again they should be really easy just like the carboxy peptidase so here's the blue one okay this is our dye peptidase enzyme here this is one of our brush border enzymes dye pepti dace what do you think he's gonna break down dipeptides it's not that hard right that was one of the breakdown products there was three breakdown products dipeptides try peptides and maybe even a little bit of amino acids well what happens is this dipeptide here let's use a different color here for these peptides in this case i don't want to get it too confused here let's use this darker blue here these dipeptides let's put here this is one amino acid and then let's put this bond like this here is the other amino acid that's my dipeptide what the dye peptidase will do is he's on that microvilli he's gonna bind onto these die peptides and he's gonna break the peptide bond when he breaks the peptide bond he's gonna release these into two individual amino acids okay so these are going to be my amino acids it's that simple that one is a really easy one not too hard to digest on that one no pun intended all right next one is we're gonna come down to this bottom guy this guy is the amino peptidase again we've talked about this a lot already so if we kind of have an idea of the chemical structure of these protein we know that a protein has to have a terminus in terminus and on one end a C terminus that's one of the important things that you can see in proteins carboxypeptidase is cleave at they C terminus the carboxy end amino peptidase is cleave at the amine and so now bring one of these let's keep it consistent here since we chose this collar here we'll put here some amino acids here and let's put it like this I'm gonna put a tripeptide in this case I could do a dipeptide but I kind of want to do a tripeptide and let's imagine here that on this end here is going to be the amino end and on this in here it's going to be the carboxy end of this tripeptide it'll cleave the bonds starting here at the amino end so it'll go in order watch this it'll go one and two so two cleave this bond first and then cleave that bond second and again the bond that it's cleaving is the peptide bonds as a result what is it going to release it's going to release three amino acids oh my goodness such a beautiful thing here but here's the thing it's not just amino acid sometimes it doesn't always not all the tripeptides not all the dipeptides get broken down unfortunately here in the actual lumen of the small intestine sometimes you might even have a little bit of some dipeptides here remaining so here is going to be our dipeptide and you might even have some tripeptides remaining still here in the lumen so this is our tri peptide okay here's the cool thing we have transporters for all of them we have transporters for the amino acids we have transporters for the tripeptide and we have transporters for the dipeptides such a beautiful thing guess what that one's going to be gonna keep them going in here in order dipeptide is gonna go here there's gonna be a special transporter that will put this dipeptide into this inteiro site and hey let's make a room so let's bring him up in the cell okay so he's gonna go up in this part of the cell so here's the dipeptide same thing tripeptide this is gonna be his little part and the amino acids they're going to funnel into this one and we have one more mechanism that I'll talk about at the end very very briefly because they're still trying to figure this mechanism out what the significance of it is now here's the thing dipeptides and tripeptides when they get absorbed across the entire site it's through a different mechanism than the amino acids what's happening is on this apical surface there is a transporter let's do this one in pink we haven't used this one a little bit there's these special transporters on the apical surface here and what they're doing is is they're pumping out into this area a lot of protons and they're bringing into the cell some sodium ions so this is a sodium hi hydrogen ion antiporter these proton ions that we're pushing out here are going to get specifically used for the dipeptides and it's also going to get specifically used for the tripeptides so in order for the the dipeptides and the tripeptides to get into the cell they have to go undergo a co transport mechanism pace import mechanism with the protons so this is going to bring in the dipeptide this is going to bring in the tripeptide the last one is different if you remember we talked about this before let's do another pink here there's gonna be another one it's just a nice color alright and then what we're gonna do here is this is on every cell in the entire body every cell and what it's doing is it's constantly pushing three sodium ions out of the cell and two potassium ions into the cell what is that doing that's if you look at it we're pushing sodium out so what do you think is gonna happen to the concentration of the sodium inside of the cell the concentration of the sodium inside of the cell is going to decrease but we're having a lot of sodium out here so the sodium concentration based upon whatever nutrients reading my diet I probably got in high sodium all the time but if you look here the sodium concentration is probably gonna be pretty high right here so now if you look we can go from areas of high concentration to areas of low concentration that's passive diffusion but the amino acids they have to go from areas of low concentration to high concentration in the cell so because of that they're going against their concentration gradient but if we bring sodium with the amino acid it's going to help it's the same mechanism for the protons so now what I'm gonna do is I'm gonna bring these sodium ions into the cell by bringing the sodium ions into the cell it helps to be able to by secondary active transport bring the amino acids into this cell as well okay now here's the cool thing amino acids I'm gonna put a a here my tripeptides TP and my dipeptides DP unfortunately when we put this into the actual blood of the apat 'ok portal vein eventually it'll go into we don't want them to be in tripeptides and dipeptides so what we do here is we have special enzymes located inside of the cell let's do this in this orange color we haven't used this one in a bit at all actually so dipeptides tripeptides they're going to have these different enzymes we have different enzymes inside of the cell and these enzymes are just peptidases so this is going to be a peptidase and this is going to be an intracellular peptidase when these intracellular peptidase act on the dipeptide and the tripeptide what do you think it's going to do it's going to cleave those peptide bonds giving us free amino acids in this case we'll have three here in this case we'll get to here so now we have three amino acids and then over here amino acids oh man this is so cool then we're gonna make one big transporter let's use red here one just gargantuous transporter and this transporter what it's going to do is it's going to bring the actual amino acids out of the cell it's gonna bring the amino acids out of the cell and into this little area here where it can go into the capillaries the in intestinal capillaries primarily like of the superior mesenteric veins but then again the superior mesenteric veins will combine with the inferior mesenteric veins combined with the pancreatic veins comply with the splenic the gastric veins and make this big sucker here called the a patek portal vein again we'll talk about that that like that scheme that circulatory scheme when we do the liver lobby again we do have another video on this where we talk about the thoracoabdominal circulation the veins or a flowchart kind of gives an idea a little bit more about the a patek portal vein so go check that out if you want to know more about it but what happens here is these amino acids through this like facilitate diffusion mechanism we can bring them out of these antara sites and then from here guess where these amino acids can go they can go into and again I'm denoting an AAA here these can go into the apat portal vein from the apat ik portal vein this will eventually take the blood to the liver and then from this amino acids we can use them for many things you'll notice that the liver does a lot of protein synthesis so he's going to convert these most likely into proteins and there's also going to be a decent release of insulin during this feeding period during the fed state we say so that's going to also help to be able to increase the protein synthesis and amino acid uptake into our cells one last thing I want to talk about and the only reason I want to talk about is because they're believing that it's being related to certain types of diseases one of those is they think related to celiac disease we're not going to talk super super on detail about this so now in different parts of the small intestine primarily at the ileum you have special types of cells called M cells and you have antara sites what they have found is that we can actually absorb member I told you that we generally don't want to absorb intact proteins it's really hard and the reason why is our immune system doesn't like to do that we can do that in the postnatal period up to about six six months for the passive immunity to be passed from our mother from the mother to the baby but generally as an adult we don't normally do that very much but into cells and Terra sites in the ilium and the ilium and these other ones called M cells they can do what's called an endocytosis mechanism okay they believe the M cells do through it's called clathrin-coated mediated endocytosis but let's say here i endocytosed a whole intact protein so here's my whole intact protein they believe that whenever we do this the entero sites can break them down by combining them with lysosomes and degrading that and releasing the free amino acids or free peptides afterwards into the blood which can go to the hepatic portal system but the M cells do something else that's really interesting they found that the M cells I can take and actually not brig this protein down they don't actually break it down because they don't have a lot of lysosomes so they keep the protein actually intact and when they keep the protein intact they actually can release this protein out on the basolateral surface so imagine here I released this protein out into the basolateral membrane so now here I'm going to have this protein released onto the basolateral membrane when it does this there's a connective tissue right underneath the epithelial cells and this connective tissue is usually areolar connective tissue they call it the lamina propria well what happens is we have special types of cells immune system cells out here these immune system cells are called macrophages there's a lot of those and what these macrophages do is is they naturally are tasting and controlling what's leaving the coming from the GI tract into the blood what this macrophage will do is is they believe that the macrophage can respond to this chemical it can phagocytose it and present that actual peptide on the cell membrane on what's called an MHC 2 complex in this peptide after it's expressed here it can take it to different types of immune system cells they believe it can take it to what's called t-cells and trigger an immune response by the release of different types of cytokines now why is that important they believe they believe that this plays a role the M cells play a role within what's called mucosal immunity but at the same time they believe it could relieve certain diseases because there is a protein in gluten called gliadin and whenever gliding gets released over here in certain people their macrophages will attack the glide and express it as MHC two complexes take it to the T cell and the T cell will start releasing tons of different types of chemicals that trigger a massive inflammatory response so if it did that and it brought it to a t-cell and it did this reaction here where it presented it to the t-cell through what's called cd4 proteins and a TCR it could trigger this T cell to start releasing chemicals like tumor necrotic factor alpha and gamma interferon which trigger a massive inflammatory response and can lead to a lot of problems and people with celiac disease I initiative so I hope you guys enjoyed this video on protein digestion absorption I hope it made sense if it did please hit that like button comment down in the comment section and please subscribe also if you guys get a chance go check out our Facebook or Instagram even our patreon account alright engineers as always until next time [Music] you [Music]

Channel: Ninja Nerd

Views: 108,134

Rating: 4.9789171 out of 5

Keywords: gastrointestinal, digestion & absorption of proteins, proteins, digestion of proteins, absorption of proteins

Id: FsKf1WOIs48

Length: 42min 26sec (2546 seconds)

Published: Mon Jun 25 2018