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Plasma Protein Synthesis - Reference Module in …

Behavior in the Solid State and Aqueous Solution and Biotransformation in the Presence of Blood Plasma Proteins

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Hepatic plasma-protein synthesis is regulated by many factors

Normal methionine metabolism is absolutely critical for folate-dependent transmethylation and transsulfuration. Abnormal metabolism of methionine can be found in both genders at any age. It is usually associated with genetic or nutritional deficiencies, aging and exposures to environmental toxins. For example, lead can impair methylation via inhibition of the enzyme methylene-tetrahydrofolate reductase (MTHFR).

Conditions associated with untreated, aberrant methionine metabolism include, but are not limited to:

Methylation
Methionine is first enzymatically converted to S-adenosylmethionine (SAM), the principal methyl donor for methylation of DNA, RNA, protein, phospholipids, creatinine and neurotransmitters. S-adenosylhomocysteine (SAH) is generated as a product of transmethylation and is hydrolyzed to homocysteine (Hcy) and adenosine through a reversible reaction. SAH is a potent inhibitor of methylation reactions. Efficient removal of adenosine and Hcy is imperative to prevent accumulation of SAH. Hcy is normally removed or recycled by remethylation to methionine through a series of reactions that require 5-methyltetrahydrofolate, B12 and betaine to complete the normal methylation cycle. A low ratio of SAM to SAH is a sensitive indicator of under-methylation. Elevated plasma Hcy is an independent risk factor for cardiovascular disease (CVD). Recent research suggests that elevated SAH may be an even better predictor of risk for CVD.

Transsulfuration: Methionine > Homocysteine > Cysteine

The methionine transsulfuration pathway occurs primarily in the liver and diverts Hcy away from remethylation to methionine toward synthesis of the conditionally essential amino acid cysteine. Homocysteine in the presence of serine and B6 is enzymatically converted to cystathionine and ultimately cysteine. Cysteine is the rate-limiting amino acid in the biosynthesis of quintessential glutathione (GSH). GSH is pivotal in the regulation of intracellular redox homeostasis, oxidative stress, immune function, DNA synthesis and repair, apoptosis and detoxification of metals and chemicals.

The DDI Methylation profile evaluates the plasma levels of methionine, cysteine, SAM, SAH, Hcy and cystathionine, and provides the important "methylation index," a ratio of SAM to SAH. The test results can appropriately guide nutritional support to improve or normalize methionine metabolism and meliorate or prevent the potential adverse consequences associated with inadequate methylation and transsulfuration capacity.

Blood Plasma - Ascension Glossary

N2 - Monolayers of chicken embryo hepatocytes, cultured in chemically defined medium, retain the ability to synthesize a wide spectrum of plasma proteins for several days in the absence of added hormones. Addition of insulin to the medium elicited a biphasic stimulation of plasma protein synthesis: a rapid response of the synthesis of a limited number of plasma proteins (e.g., albumin and α1-globulin 'M'), then, after prolonged exposure to the hormone, the involvement of additional plasma proteins (e.g., fibrinogen and lipoproteins). Synthesis of transferrin and a few other plasma proteins was not affected by the presence of insulin. The degree of stimulation for the most responsive plasma proteins ranged between 2- to 4-fold during the early phase and 10- and even 30-fold during the late phase of the cells' response to insulin. Stimulated synthesis in the early phase was detected within 1 hr and was rapidly reversible. Plasma protein synthesis in culture was sensitive to concentrations of insulin below 0.35 nM, well within the physiological range. The delayed response was elicited only at higher hormone levels. Parallels between the control of synthesis of plasma proteins in this system and that observed in diabetic animals suggest that the embryonic chicken hepatocytes may be a useful model for studying liver function in diabetes as well as insulin action in general.

Blood - Plasma: The liquid portion of the blood, the plasma, ..

plasma proteins into amino acids for tissue protein synthesis 2

Monolayers of chicken embryo hepatocytes, cultured in chemically defined medium, retain the ability to synthesize a wide spectrum of plasma proteins for several days in the absence of added hormones. Addition of insulin to the medium elicited a biphasic stimulation of plasma protein synthesis: a rapid response of the synthesis of a limited number of plasma proteins (e.g., albumin and α1-globulin 'M'), then, after prolonged exposure to the hormone, the involvement of additional plasma proteins (e.g., fibrinogen and lipoproteins). Synthesis of transferrin and a few other plasma proteins was not affected by the presence of insulin. The degree of stimulation for the most responsive plasma proteins ranged between 2- to 4-fold during the early phase and 10- and even 30-fold during the late phase of the cells' response to insulin. Stimulated synthesis in the early phase was detected within 1 hr and was rapidly reversible. Plasma protein synthesis in culture was sensitive to concentrations of insulin below 0.35 nM, well within the physiological range. The delayed response was elicited only at higher hormone levels. Parallels between the control of synthesis of plasma proteins in this system and that observed in diabetic animals suggest that the embryonic chicken hepatocytes may be a useful model for studying liver function in diabetes as well as insulin action in general.

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the per cent utilized in liver and plasma protein synthesis.

In diabetes mellitus, hyperglycemia is often associated with elevated levels of glucagon in the blood. This suggests that glucagon (1) is a contributing factor in the metabolic abnormalities of diabetes mellitus. A glucagon-receptor antagonist would provide direct evidence for glucagon's role in diabetes mellitus. On the basis of careful consideration of conformational, amphiphilic, and structural factors, we have synthesized two new glucagon analogues with antagonist biological activities by using solid-phase methodology. These two new analogues, [Asp3 D-Phe4,Ser5,Lys17,18,Glu21]glucagon (2) and [D-Phe4,Tyr5,3,5-I2-Tyr10,Arg 12,Lys17,18,Glu21]glucagon (3), had IC50 values 5.4% and 50% those of glucagon, respectively, and showed no measurable adenylate cyclase activity. When tested in normal rats, 2 lowered plasma glucose levels and suppressed glucagon-mediated hyperglycemia 105 ± 8%, back to basal levels. Analogue 3, which lowered the basal adenylate cyclase activity in rat liver plasma membranes, increased plasma glucose levels at very high concentration in vivo and inhibited glucagon-mediated hyperglycemia in normal rats by 50%. However, neither of the new glucagon antagonists lowered the plasma glucose levels of diabetic animals. The data would suggest these new glucagon-receptor antagonists may have two actions: (a) in normal rats they can act as standard glucagon-receptor inhibitors of glucagon-mediated glycogenolysis; (b) in diabetic rats, however, because of the low levels of glycogen in the liver, the antagonists apparently have little or no antagonist effect or enhancement on glucagon-mediated glucose production.

AB - Monolayers of chicken embryo hepatocytes, cultured in chemically defined medium, retain the ability to synthesize a wide spectrum of plasma proteins for several days in the absence of added hormones. Addition of insulin to the medium elicited a biphasic stimulation of plasma protein synthesis: a rapid response of the synthesis of a limited number of plasma proteins (e.g., albumin and α1-globulin 'M'), then, after prolonged exposure to the hormone, the involvement of additional plasma proteins (e.g., fibrinogen and lipoproteins). Synthesis of transferrin and a few other plasma proteins was not affected by the presence of insulin. The degree of stimulation for the most responsive plasma proteins ranged between 2- to 4-fold during the early phase and 10- and even 30-fold during the late phase of the cells' response to insulin. Stimulated synthesis in the early phase was detected within 1 hr and was rapidly reversible. Plasma protein synthesis in culture was sensitive to concentrations of insulin below 0.35 nM, well within the physiological range. The delayed response was elicited only at higher hormone levels. Parallels between the control of synthesis of plasma proteins in this system and that observed in diabetic animals suggest that the embryonic chicken hepatocytes may be a useful model for studying liver function in diabetes as well as insulin action in general.

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  • What is the function of plasma in blood? - Quora

    The quality of our blood and Blood Plasma is what gives instruction to the entire set of proteins that are ..

  • What is the function of plasma in blood

    are carried by blood plasma

  • Several trends continue to shape the landscape in blood/plasma ..

    Plasma proteins are proteins found in blood plasma, including albumin, fibrinogen, and globulin

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Blood Plasma Fractionation | MilliporeSigma

An adult at rest consumes the equivalent of 250ml of pure oxygen per minute. This oxygen is used to provideenergy for all the tissues and organs of the body, even when thebody is at rest. The body's oxygen needs increase dramaticallyduring exercise or other strenuous activities. The oxygen iscarried in the blood from the lungs to the tissues where it isconsumed. However, only about 1.5% of the oxygen transported inthe blood is dissolved directly in the blood plasma. Transportingthe large amount of oxygen required by the body, and allowing itto leave the blood when it reaches the tissues that demand themost oxygen, require a more sophisticated mechanism than simplydissolving the gas in the blood. To meet this challenge, the bodyis equipped with a finely-tuned transport system that centers onthe metal complex heme.

Learn more about Blood Plasma Fractionation at MilliporeSigma

N2 - In diabetes mellitus, hyperglycemia is often associated with elevated levels of glucagon in the blood. This suggests that glucagon (1) is a contributing factor in the metabolic abnormalities of diabetes mellitus. A glucagon-receptor antagonist would provide direct evidence for glucagon's role in diabetes mellitus. On the basis of careful consideration of conformational, amphiphilic, and structural factors, we have synthesized two new glucagon analogues with antagonist biological activities by using solid-phase methodology. These two new analogues, [Asp3 D-Phe4,Ser5,Lys17,18,Glu21]glucagon (2) and [D-Phe4,Tyr5,3,5-I2-Tyr10,Arg 12,Lys17,18,Glu21]glucagon (3), had IC50 values 5.4% and 50% those of glucagon, respectively, and showed no measurable adenylate cyclase activity. When tested in normal rats, 2 lowered plasma glucose levels and suppressed glucagon-mediated hyperglycemia 105 ± 8%, back to basal levels. Analogue 3, which lowered the basal adenylate cyclase activity in rat liver plasma membranes, increased plasma glucose levels at very high concentration in vivo and inhibited glucagon-mediated hyperglycemia in normal rats by 50%. However, neither of the new glucagon antagonists lowered the plasma glucose levels of diabetic animals. The data would suggest these new glucagon-receptor antagonists may have two actions: (a) in normal rats they can act as standard glucagon-receptor inhibitors of glucagon-mediated glycogenolysis; (b) in diabetic rats, however, because of the low levels of glycogen in the liver, the antagonists apparently have little or no antagonist effect or enhancement on glucagon-mediated glucose production.

detection of hydrogen sulfide in blood plasma ..

AB - In diabetes mellitus, hyperglycemia is often associated with elevated levels of glucagon in the blood. This suggests that glucagon (1) is a contributing factor in the metabolic abnormalities of diabetes mellitus. A glucagon-receptor antagonist would provide direct evidence for glucagon's role in diabetes mellitus. On the basis of careful consideration of conformational, amphiphilic, and structural factors, we have synthesized two new glucagon analogues with antagonist biological activities by using solid-phase methodology. These two new analogues, [Asp3 D-Phe4,Ser5,Lys17,18,Glu21]glucagon (2) and [D-Phe4,Tyr5,3,5-I2-Tyr10,Arg 12,Lys17,18,Glu21]glucagon (3), had IC50 values 5.4% and 50% those of glucagon, respectively, and showed no measurable adenylate cyclase activity. When tested in normal rats, 2 lowered plasma glucose levels and suppressed glucagon-mediated hyperglycemia 105 ± 8%, back to basal levels. Analogue 3, which lowered the basal adenylate cyclase activity in rat liver plasma membranes, increased plasma glucose levels at very high concentration in vivo and inhibited glucagon-mediated hyperglycemia in normal rats by 50%. However, neither of the new glucagon antagonists lowered the plasma glucose levels of diabetic animals. The data would suggest these new glucagon-receptor antagonists may have two actions: (a) in normal rats they can act as standard glucagon-receptor inhibitors of glucagon-mediated glycogenolysis; (b) in diabetic rats, however, because of the low levels of glycogen in the liver, the antagonists apparently have little or no antagonist effect or enhancement on glucagon-mediated glucose production.

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