Information

How does protein enter bloodstream?


If a hemophiliac patient injects his factor 8 through the veins directly into the bloodstream to provide the body with clotting factor… Why don't they just make the drug as a pill and have the liver do its job with extracting protein and dumping it into the bloodstream?


Proteins will be digested through a number of proteases in the stomach and intestines (pepsin, trypsin, etc) into their constituent amino acids. The amino acids are then absorbed in the small intestine. So any specific proteins you try to put into a pill will be digested into amino acids before being absorbed. If you somehow manage to defeat the digestive enzymes, the protein will simply pass through the digestive tract without being absorbed--the intestines don't have the capability to allow larger polypeptides through.

If you think about it, this is probably a good thing. We don't want random proteins from our food running around in our bodies. It would likely kill us in short order.


COVID-19 can affect the blood. Its spike protein may be the culprit.

Early on in the pandemic, Lee Makowski read an article about the condition of people’s bodies after dying of COVID-19, and he was shocked by what he learned—there was something very wrong with the patients’ blood.

The autopsy reports revealed COVID-19 patients were suffering from huge amounts of thick, coagulated blood, and dysfunctional blood vessels were tearing through body tissue instead of repairing it—highly uncommon side effects of respiratory diseases.

Lee Makowski, chair of the bioengineering department at Northeastern. Photo by Matthew Modoono/Northeastern University

The postmortem evidence plus his own experience with something called “COVID toes”—an odd side effect of the disease that causes heightened blood vessel formation in the toes, turning them bright red—led Makowski to speculate that something about the virus might be causing abnormal blood-related complications.

“One of the most perplexing and devastating effects of this disease is the scenario where three or four weeks after being hospitalized with pneumonia, people under the age of 50 are back home, they feel fine, and then all of a sudden they have a stroke and die,” says Makowski, professor and chair of the bioengineering department at Northeastern.

Makowski, who recently published his hypothesis in the journal Viruses, believes the spike protein found on the surface of the virus might mimic proteins that regulate blood vessels and control the formation of blood clots, which could explain many of the non-respiratory complications of COVID-19.

The spike protein is an arm-like apparatus that the virus uses to attach to and enter healthy cells. At the tip of the spike protein rests a string of three amino acids called RGD. This structure is known for connecting cells to each other in the body.

Researchers don’t know yet whether RGD is the culprit for COVID-19’s blood-related complications, but they do know that RGD can contribute to the formation of blood clots and the growth of new blood vessels when it interacts with cell receptors called integrins.

“Other proteins that have RGD are known to cause complications. Our theory is that RGD is making it easier for the virus to bind to things that could cause these blood complications,” says William Olson-Sidford, a third-year bioengineering student and co-author of the paper who worked on this project as a co-op last fall.

Right now, researchers know that the virus’s spike protein binds to cell receptors called ACE2. ACE2 is found in many cell types including in the lungs, heart, blood vessels, kidneys, liver, and gastrointestinal tract.

“But our theory is that because [the virus] has an RGD, it may also be more likely to bind to other cells in the body that people aren’t thinking about,” Olson-Sidford says.

Makowski hypothesizes that dysregulated blood vessel growth—which can disrupt lung tissue—is triggered by an increase of RGD during infection.

As for COVID-19-related kidney failure, “it’s hard to know whether it’s caused by direct damage to the tissue by viral invasion or indirect damage through coagulation and blocked arteries,” Makowski says. But either way, a faulty connection between RGD and integrin could be the culprit.

Recognizing that coagulation is a major problem has greatly improved the survival rate of people who are severely sick with COVID-19, Makowski says. “Now if you end up in the ICU, you almost always get an anticoagulant, and that saves a lot of lives.”

Uncovering the cause of that coagulation is the next step. Makowski hopes his hypothesis will spur other researchers to investigate further.


Protein binding: what does it mean?

Protein binding can enhance or detract from a drug's performance. As a general rule, agents that are minimally protein bound penetrate tissue better than those that are highly bound, but they are excreted much faster. Among drugs that are less than 80-85 percent protein bound, differences appear to be of slight clinical importance. Agents that are highly protein bound may, however, differ markedly from those that are minimally bound in terms of tissue penetration and half-life. Drugs may bind to a wide variety of plasma proteins, including albumin. If the percentage of protein-bound drug is greater when measured in human blood than in a simple albumin solution, the clinician should suspect that the agent may be bound in vivo to one of these "minority" plasma proteins. The concentration of several plasma proteins can be altered by many factors, including stress, surgery, liver or kidney dysfunction, and pregnancy. In such circumstances, free drug concentrations are a more accurate index of clinical effect than are total concentrations. Formulary committees must grasp the clinical significance of qualitative and quantitative differences in protein binding when evaluating competing agents.


From the Stomach to the Small Intestine

The stomach empties the chyme containing the broken down egg pieces into the small intestine, where the majority of protein digestion occurs. The pancreas secretes digestive juice that contains more enzymes that further break down the protein fragments. The two major pancreatic enzymes that digest proteins are chymotrypsin and trypsin. The cells that line the small intestine release additional enzymes that finally break apart the smaller protein fragments into the individual amino acids. The muscle contractions of the small intestine mix and propel the digested proteins to the absorption sites. In the lower parts of the small intestine, the amino acids are transported from the intestinal lumen through the intestinal cells to the blood. This movement of individual amino acids requires special transport proteins and the cellular energy molecule, adenosine triphosphate (ATP). Once the amino acids are in the blood, they are transported to the liver. As with other macronutrients, the liver is the checkpoint for amino acid distribution and any further breakdown of amino acids, which is very minimal. Recall that amino acids contain nitrogen, so further catabolism of amino acids releases nitrogen-containing ammonia. Because ammonia is toxic, the liver transforms it into urea, which is then transported to the kidney and excreted in the urine. Urea is a molecule that contains two nitrogens and is highly soluble in water. This makes it a good choice for transporting excess nitrogen out of the body. Because amino acids are building blocks that the body reserves in order to synthesize other proteins, more than 90 percent of the protein ingested does not get broken down further than the amino acid monomers.


Clinical Pathology

Serum Proteins

The total serum protein (TP) concentration includes the total of specific proteins in plasma with the exception of those that are consumed in clot formation, such as fibrinogen and the clotting factors. Plasma protein is about 3–5 g/L greater than serum protein. Hydration status of the animal should be considered when interpreting protein changes. Hypoproteinemia, as with anemia, can be masked by dehydration. It is important to remember that hematologic and serum chemistry values will be falsely elevated in dehydrated animals. Albumin and globulins are increased proportionately in simple dehydration.

Albumin accounts for 35–50% of total serum protein concentration in animals, and for about 75% of plasma colloidal activity. Synthesis occurs in the liver. There is a direct correlation between albumin turnover and body size. For example, plasma albumin half-life is two and eight days in the mouse and dog, respectively. Occurrence of hypoalbuminemia following seven days of administration of a test compound in the rat could reflect decreased assimilation of albumin, e.g., decreased food consumption, digestion or absorption, or hepatic pathology. However, other underlying causes, such as gastrointestinal, urinary, or vascular loss of albumin would be more likely causes of hypoalbuminemia in this time frame in the dog. Albumin is considered a negative acute phase protein, and may decrease during acute inflammatory conditions.

Globulins constitute a number of heterogeneous proteins, including coagulation factors, transport proteins, mediators of inflammation, and immunoglobulins. Electrophoretic separation will identify α, β, and γ fractions. Electrophoresis, sometimes used in the diagnostic setting, is not generally included in most non-clinical toxicology protocols, but may identify fractions affected in hyper- or hypoglobulinemia. The liver synthesizes most globulins. Immunoglobulins are synthesized by B-lymphocytes and plasma cells, and are generally found in the γ fraction of the electrophoretogram, although they may extend into the β region. The most frequent causes of hyperglobulinemia are dehydration or a polyclonal gammopathy secondary to antigenic stimulation. Increased acute phase proteins, such as alpha2-macroglobulin, haptoglobulin and ceruloplasmin, are frequently part of the increased total globulins in the general response to inflammation.

The albumin:globulin (A/G) ratio reflects whether changes in protein concentrations involve changes in either albumin or globulin, or both. Thus, if albumin is selectively lost through a protein losing nephropathy or is not produced, as in hepatic disease, then the A/G ratio will be low. However, if there is a concomitant loss or failure to synthesize globulins, as occurs in hemorrhage, enteropathy, exudation, and malassimilation, then panhypoproteinemia and a normal A/G ratio may occur.


Protein: metabolism and effect on blood glucose levels

Insulin is required for carbohydrate, fat, and protein to be metabolized. With respect to carbohydrate from a clinical standpoint, the major determinate of the glycemic response is the total amount of carbohydrate ingested rather than the source of the carbohydrate. This fact is the basic principle of carbohydrate counting for meal planning. Fat has little, if any, effect on blood glucose levels, although a high fat intake does appear to contribute to insulin resistance. Protein has a minimal effect on blood glucose levels with adequate insulin. However, with insulin deficiency, gluconeogenesis proceeds rapidly and contributes to an elevated blood glucose level. With adequate insulin, the blood glucose response in persons with diabetes would be expected to be similar to the blood glucose response in persons without diabetes. The reason why protein does not increase blood glucose levels is unclear. Several possibilities might explain the response: a slow conversion of protein to glucose, less protein being converted to glucose and released than previously thought, glucose from protein being incorporated into hepatic glycogen stores but not increasing the rate of hepatic glucose release, or because the process of gluconeogenesis from protein occurs over a period of hours and glucose can be disposed of if presented for utilization slowly and evenly over a long time period.


The Killer in the Bloodstream: the “Spike Protein”

“From the beginning Covid has been a conspiracy against health and life. Covid is a profit-making agenda and an agenda for increasing arbitrary government power over people. There should be massive law suits and massive arrests of those who block effective Covid cures and impose a deadly vaccine.” – Paul Craig Roberts, Former Assistant Secretary of the Treasury under President Ronald Reagan

The Spike Protein is a “uniquely dangerous” transmembrane fusion protein that is an integral part of the SARS-CoV-2 virus. “The S protein plays a crucial role in penetrating host cells and initiating infection.” It also damages the cells in the lining of the blood vessel walls which leads to blood clots, bleeding, massive inflammation and death.

To say that the spike protein is merely “dangerous”, is a vast understatement. It is a potentially-lethal pathogen that has already killed tens of thousands of people.

So, why did the vaccine manufacturers settle on the spike protein as an antigen that would induce an immune response in the body?

That’s the million-dollar question, after all, for all practical purposes, the spike protein is a poison. We know that now due to research that was conducted at the Salk Institute. Here’s a summary of what they found:

“Salk researchers and collaborators show how the protein damages cells, confirming COVID-19 as a primarily vascular disease…. SARS-CoV-2 virus damages and attacks the vascular system (aka–The circulatory system) on a cellular level… scientists studying other coronaviruses have long suspected that the spike protein contributed to damaging vascular endothelial cells, but this is the first time the process has been documented….

the spike protein alone was enough to cause disease. Tissue samples showed inflammation in endothelial cells lining the pulmonary artery walls.

Author: Centre for Research on Globalization

The Centre for Research on Globalization (CRG) is an independent research and media organization based in Montreal. The CRG is a registered non-profit organization in the province of Quebec, Canada.

© 2021, Z3 News. The first 200 words of Z3 News articles may be shared online in exchange for a clickable link to our site. Please include the author name and do not make any changes to text or titles. No image files from our site may be shared because we don’t own them. For permission to use our content in other formats, please contact us.

If you found this post helpful, please consider sharing it with others by emailing the link or posting it on social media sites like Facebook, Instagram, Tumblr, and Twitter.


Clotting process of blood

Thromboplastin is a lipoprotein secreted from Blood platelets when injured blood vessels comes in exposure to collagen fiber which help in blood clot formation. Clotting process of blood or clot formation consists of mainly three phases

1) formation of prothrombin Activator :- thromboplastin helps in the formation of an enzyme prothrombinase. this enzyme inactivates heparin that is natural anticoagulant material present in our body which secreted from mast cell of liver and also convert the inactive plasma protein prothrombin into its active form thrombin being both the changes require calcium iron and blood coagulating factors

2) formation of thrombin and fibrin monomer:- the prothrombin activator in presence of calcium ion Ca+2 change the inactive prothrombin into to activate thrombin. And thrombin act as proteolytic enzyme to separate two peptides from the soluble plasma protein fibrinogen molecules to form insoluble fibrin monomer.

3) polymerization of fibrin monomer :- the fibrin monomer polymerized to form long sticky fibres, the fibrin threads form of fine network over the wound and trap blood corpuscles like red blood cells, white blood cells blood,blood platelets to form a crust known as blood clot.

Describe the clotting process of blood and its mechanism

What is blood clotting process ?

What is blood clotting process ? Solve by studying the mechanism of blood clotting and their process consists of multi step process and blood clotting process consist of formation of prothrombin activators have two Pathways extrinsic pathways and intrinsic pathways, change of inactive prothrombin into to active thrombin, change of soluble fibrinogen molecules into insoluble fibrin monomer and change of insoluble fibrin monomer into insoluble fibrin polymer or clot.

1) formation of prothrombin Activator :- formation of prothrombin activator is multi step process and there is two types of protein help in formation of prothrombin Activator. first is thromboplastin lipoprotein molecules released from injured tissues and blood platelets and second prothrombin activator is group of coagulation factor protein like vii, X, V, xi, xii, ix and iv.

Coagulation factor generaly indicates by Roman numbers the coagulation factors are generally serine protease enzyme which act by leaving down-stream proteins and the coagulation factor circulate as inactive enzymes known as zymogens.

The coagulation cascade or injury therefore classical divided into two Pathways the tissues factor Pathways known as extrinsic Pathways and contact activation Pathways known as intrinsic Pathways.

extrinsic Pathways :- extrinsic pathway is also known as tissue factor pathway. The main role of tissue factor pathway is to generate thrombin and formation of prothrombin activators molecules.

this extrinsic Pathways clotting process of blood starts from release of thromboplastin lipoprotein molecules from Blood platelets of injured tissues.

Coagulation factor VII circulate in higher amount in blood plasma then any other activated coagulation factors, following damage to the blood vessels coagulation factor vii leaves the circulation and comes into the contact with thromboplastin molecules. Combination of thromboplastin and coagulation factor VII, it activate the inactive coagulation factor x into active x.

And active coagulation factor x bind to active calculation factor v to form prothrombin activators molecules.

◆you should also visits our website https://biologysir.com and other website for civil engineer calculation at https://www.civilsir.com

intrinsic Pathways:- intrinsic pathway also known as contact activation Pathways. And this Pathways of clotting process of blood starts from exposure of injured blood vessels to collagen fibres. The contact activation of Pathways begins with formation of primary complex on collagen of blood vessels.

Collagen of blood vessels help in changes of inactive coagulation factor xii to active coagulation factor xii.

And active coagulation factor xii act on inactive coagulation factor xi and change into to active factor xi.

And active coagulation factor xi act on inactive coagulation factor ix and change into to active factor ix.

And active coagulation factor ix act on inactive coagulation factor x and change into to active factor x.

And active coagulation factor V bind with active coagulation factor x change to form prothrombin activator molecules.

2) formation of active prothrombin :- prothrombin is known as coagulation factor ii, it is vitamin K dependent plasma protein synthesise and secreted from liver. The prothrombin activator molecules help in formation of enzyme prothrombinase.

The enzyme prothrombinase helps to inactivate anticoagulant material heparin and also activate inactive protein prothrombin into its active form. So main function of thromboplastin prothrombin activators molecules to change inactive prothrombin to active prothrombin molecule.

heparin ( active) + prothrombinase ( prothrombin activators) —- inactive heparin

● inactive prothrombin + prothrombinase ( prothrombin activators) —- active prothrombin

3) formation of thrombin molecule:- in the presence of coagulation factor iv that is calcium ion and prothrombin Activator act on Active prothrombin molecule and changes into active thrombin

4) formation of fibrin monomer :- active thrombin molecules act as proteolytic enzyme to separates two peptides from the soluble plasma protein known as fibrinogen molecules to form insoluble fibrin monomer.

5) polymerization of fibrin monomer:- the fibrin monomers polymerized in the presence of active coagulation factor xiii to form long stick fibres. The fibrin threads form a fine network over the wound and trap blood cells like red blood cells, white blood cells, blood platelets to form a crust that is known as blood clot.

The blood platelets also polymerize actin and myosin into contractile apartus. the latter contracts and the clot become relatively firm and solid. The part of blood plasma in the clotted area is squeezed out as clear fluid material known as blood serum, serum is Plasma axcept that it lacks fibrinogen and blood cells it is therefore unavailable for clot.

Clotting factors present in the blood

● v — Proaccelerin, Ac globulin

● vi — factor is hypothetical

● vii — SPCA ( serum prothrombin conversion accelerator)

● viii — AHF ( anti haemophilic factor)

● ix— PTC ( plasma thromboplastin component or Christmas factor)

● xi — PTA ( plasma thromboplastin antecedent)

● xiii — fibrin stabilizing factor

Role of vitamin K in blood clotting

Vitamin K is necessary for the synthesis of prothrombin in the liver, if vitamin K is inadequate in the diet or is not observed in the intestine, blood clotting becomes inefficient. this produce symptoms similar to those of haemophilia and which is described as lack of haemophilic globulin or to lack of thromboplastin molecules.

Natural anticoagulants

A substance that checks the clotting of blood in blood vessels is known as anticoagulant material. blood does not clot in uninjured vessels due to the presence in it of a strong natural anticoagulant such like heparin produce in the mast cell of liver. its check the change of prothrombin into thrombin.

And another natural anticoagulant material name is hirudin occurs in The Saliva of leech it prevents clotting of victims blood in the leech crops, another Sodium and potassium oxalate are the also anticoagulant and they participate calcium iron which prevent clotting.


Types of Protein Testing

There are various types of protein testing. A kind of protein, known as the C Reactive Protein, is also present in the blood. This protein increases in quantity as a response to inflammation in the body. The C Reactive Protein test is conducted to find out the progress of various diseases.

Some of the common CRP protein tests are ELISA, immunodiffusion, immunoturbidimetry and visual agglutination. A recent study has found that with the help of a newly identified Decoy receptor 3 (DcR3) protein, rheumatoid arthritis can be cured.

The blood serum protein is checked for the progression of all these diseases. Due to the deficiency of protein, heart attack can also be caused. Therefore, doctors may suggest a regular monitoring of protein in the blood.


Reference Range for Blood Proteins

Before we look into the causes of high or low levels of blood proteins, let’s take a look at the normal range for blood proteins.

Serum Protein Normal Range
Total Protein 6.0-8.3 gm/dL
Albumin 3.8-5.0 gm/dL
Globulin 2.3-3.5 gm/dL
Alpha-1 globulin 0.1-0.3 gm/dL
Alpha-2 globulin 0.6-1.0 gm/dL
Beta globulin 0.7-1.1 gm/dL
Gamma globulin 0.7-1.6 gm/dL
Albumin/globulin ratio 1.1-1.4

High Levels of Proteins in Blood

High levels of protein in the blood could be indicative of a weakened immune system. When people have an abnormally high blood protein count, doctors may recommend them to get themselves tested for Hepatitis or HIV. Total blood protein levels may become elevated if one is suffering from a chronic infection. Liver dysfunction could also cause the levels of protein to increase. Since chronic inflammation could also be a contributory factor, people suffering from rheumatoid arthritis can have a high blood protein count. Sometimes abnormal levels of protein in blood could be caused due to certain bone marrow diseases such as multiple myeloma, amyloidosis or monoclonal gammopathy of undetermined significance.

Waldenstrom’s disease could also elevate the levels of protein in the blood. This is a type of cancer which can make the blood very viscous which in turn could impair the functioning of the brain. A person suffering from this disease could also experience symptoms such as fatigue, swollen lymph glands, nosebleeds or gum bleeding. Elevated levels of albumin could occur due to excess of glucocorticoids due to prolonged use of certain drugs. Albumin levels could also increase if adrenal glands produce larger amounts of cortisol. Albumin levels could also get elevated in people suffering from congestive heart failure or dehydration. Since most of the antibodies are gamma globulins, very high levels of globulins in blood could be indicative of an autoimmune condition, infection or an inflammatory disorder.

Low Levels of Proteins in Blood

The levels of total protein could become lower than the reference range due to malnutrition. A diet lacking in proteins and certain amino acids could be one of the contributory factors. Malabsorption of proteins could also be responsible for lowering the levels of protein. Such people must take the recommended daily protein intake. People suffering from nephrotic syndrome could also have a low blood protein count. Certain conditions that affect the kidneys can also cause a dip in the levels of protein. Sometimes the level of proteins present in the urine could be high. If the kidneys are not working properly proteins might leak into urine. Besides kidney diseases, medical conditions such as Crohn’s disease, celiac disease and Whipple’s disease can also damage the intestines and affect their ability to absorb protein from food.

Since albumin and globulin are made in the liver, any damage to the liver can also be responsible for lowering the levels of proteins. At times, there could be a dip in the levels due to retention of extra fluids within the vascular system. This could cause dilution of proteins and cause a dip in the levels of proteins. While low albumin levels may be seen in people suffering from malnutrition, albuminuria, loss of protein through gastrointestinal tract in diarrhea, liver dysfunction or hormonal imbalance, low levels of globulin may be seen in people who are suffering from liver dysfunction, nephrotic syndrome or acute hemolytic anemia.

While abnormal blood protein levels don’t pinpoint any particular illness, these do indicate health problems. When the total serum protein test reveals low or high levels of protein, doctors usually order other tests to ascertain the underlying cause. The affected individuals must follow the dietary guidelines and make the right lifestyle choices to bring the levels of blood proteins within the normal range.

Disclaimer: This HealthHearty article is for informative purposes only, and should not be used as a replacement for expert medical advice.


White Blood Cells And Protein

All white blood cells require amino acids in order to sustain normal function. Some of the uses of amino acids by white blood cells are very apparent in immune function. For instance, antibodies are proteins, and are therefore made up of amino acids. You have to eat proteins to get the amino acids that your B-lymphocytes use to make antibodies. Even white blood cells that don't make antibodies, however, need protein all cells require protein for energy and to make major structural and functional molecules that operate within the cells.