Plasma Proteins & Immunoglobulins

Question 1

functions of blood , 10

Answer 1

page 3 in sheet

Question 2

hydrostatic pressure vs oncotic pressure

Answer 2

Oncotic pressure is a form of osmotic pressure exerted by proteins either in the blood plasma or interstitial fluid. Hydrostatic pressure is a force generated by the pressure of fluid on the capillary walls either by the blood plasma or interstitial fluid.

Question 3

what’s edema

Answer 3

accumulation of fluid in the extravascular tissue spaces due to the concentration of plasma proteins being markedly diminished

Question 4

T/F Roughly 70 to 80% of all plasma proteins are synthesized in the liver. These include albumin, fibrinogen, transferrin

Answer 4

TRUE

Question 5

where are y-globulin synthesized

Answer 5

γ-globulins, which are synthesized in the lymphocytes

Question 6

what’s polymorphism

Answer 6

in biology, a discontinuous genetic variation resulting in the occurrence of several different forms or types of individuals among the members of a single species

Question 7

what’s half life of protein

Answer 7

he half-life of a plasma protein is the time required for 50% of the molecules present at any given moment to be degraded or otherwise cleared from the blood.

Question 8

what’s turnover process

Answer 8

when older protein molecules are cleared they are replaced by newly synthesized ones,During normal turnover, the total concentration of these proteins will remain constant as the countervailing processes of synthesis and clearance reach a steady state.

Question 9

protein-losing gastroenteropathy.

Answer 9

when considerable amounts of plasma proteins,, may be lost into the bowel through the inflamed intestinal mucosa. The half-life these subjects may be reduced to as little as 1 day, example Crohn disease

Question 10

T/F About 40% of the body’s albumin circulates in the plasma,The remainder resides in the extracellular space

Answer 10

T

Question 11

T/F albumin is initially synthesized as a preproprotein.

Answer 11

T

Question 12

structure of albumin

Answer 12

Mature human albumin consists of a single polypeptide chain, 585 amino acids in length, that is organized into three functional domains. Its ellipsoidal conformation is stabilized by a total of 17 intrachain disulfide bonds.

Question 13

A major role of albumin

Answer 13

bind to and transport numerous ligands. These include free fatty acids (FFA), calcium, certain steroid hormones, bilirubin, copper, and tryptophan. A variety of drugs, including sulfonamides, penicillin G, dicumarol, and aspirin, also bind to albumin; a finding with important pharmacologic implications. Preparations of human albumin have been widely used in the treatment of burns and of hemorrhagic shock.

Question 14

what’s analbuminemia.

Answer 14

Some humans suffer from genetic mutations that impair their ability to synthesize albumin. Individuals whose plasma is completely devoid of albumin are said to exhibit analbuminemia

Question 15

T/F The synthesis of albumin decreases relatively early in conditions of protein malnutrition, such as kwashiorkor.

Answer 15

T

Question 16

what are Acute phase proteins

Answer 16

Acute phase proteins (APPs) are defined as proteins that increase in concentration response to inflammatory cytokines,and 50% increase in patients with cancer

Question 17

what dose α1-antitrypsin do

Answer 17

α1-antitrypsin neutralizes certain proteases released during

acute inflammation.

Question 18

what are Hepatocytes

Answer 18

Hepatocytes are the chief functional cells of the liver and perform an astonishing number of metabolic, endocrine and secretory functions

Question 19

function of Interleukin 1 (IL-1)

Answer 19

a polypeptide released from mononuclear phagocytic cells, is the principal—but not the sole— stimulator of acute-phase reactant synthesis by hepatocytes

Question 20

-ve phsase acute proteins

Answer 20

are the proteins that get reduced in the body when it faces infection, burn and trauma

Question 21

what are the -ve phsase acute proteins

Answer 21

prealbumin, albumin, transferrin

Question 22

which proteins that increase after injury and are considered as acute phase injury

Answer 22

C-reactive protein

(CRP), α1 -antitrypsin, haptoglobin, & fibrinogen

Question 23

Nuclear factor kappa-B

Answer 23

a transcription factor that regulates the expression of the genes encoding many cytokines, chemokines, growth factors, and cell adhesion molecules. NFκB, a heterodimer comprised of a 50- and a 65-kDa polypeptide, normally resides in the cytosol as an inactive complex with a second protein, NFκB inhibitor-α, also known as IκBα. When stimulation by inflammation, injury, or radiation, IκBα becomes phosphorylated, which targets it for ubiquitination and degradation. Once freed from its inhibitory partner, active NFκB translocates to the nucleus where it stimulates transcription of its target genes.

Question 24

albumin structure detail

Answer 24

One polypeptide chain, 585 amino acids,

17 disulfide bonds

Question 25

methods of separating plasma proteins

Answer 25

salting out: based on solubility

Gel electrophoresis

Question 26

albumin binds to various ligands:state them.6

Answer 26

Free fatty acids (FFA)
Certain steroid hormones
Bilirubin
Plasma tryptophan
Metals: Calcium, copper and heavy metals
Drugs: sulfonamides, penicillin G, dicumarol,
aspirin (drug-drug interaction)

Question 27

what’s analbuminemia and it’s cause

Answer 27

characterized by the absence or dramatic reduction of circulating human serum albumina
mutation that affects
splicing
 Patients show moderate
edema!!!

Question 28

what’s Hypoalbiminemia:

Answer 28

edema seen in
conditions where albumin level in
blood is less than 2 g/dl
Malnutrition (generalised edema)
Nephrotic syndrome(kidney disorder that causes your body to pass too much protein in your urine)
Cirrhosis (mainly ascites)
Gastrointestinal loss

Question 29

Prealbumin half life

Answer 29

It has short half-life (≈2 days):

Question 30

The normal albumin concentration is

Answer 30

3.5-5.5 g/dl

Question 31

why do New born babies have high concentration of bilirubin

Answer 31

enzymes are not mature enough=broken heme, bilirubin binds to
albumin till the body deals with it. and because the The blood brain barrier is not mature yet, this could be dangerous for the baby

Question 32

what’s kernicterus

Answer 32

• Aspirin binds on the same spot where bilirubin binds (competitive
ligand), so giving aspirin to a new-born will lead to high
concentration of bilirubin thus entering the brain and amassing
there. This is called kernicterus and it causes mental retardation.

Question 33

how can Phenytoin-dicoumarol cause drug interaction

Answer 33

When two drugs having high affinity to albumin are administered
together, there may be competition for the available sites, with
consequent displacement of one drug. such an effect may lead to
clinically significant drug interactions
• So, they both bind on the same spot, you shouldn’t take both of them at
the same time

Question 34

what’s Phenytoin and Dicoumarol

Answer 34

Phenytoin is an anti-epileptic drug

Dicoumarol is an anti-coagulant

Question 35

why is prealbumin named this way

Answer 35

because it
migrates a head of albumin (faster than albumin)
in gel electrophoresis.

Question 36

what’s Prealbumin or Transthyretin

Answer 36

a small glycoprotein (rich in tryptophan, 0.5%
carbohydrates)Prealbumin is a protein made in your liver. Prealbumin helps carry thyroid hormones (T4 (Thyroxine) and T3 carrier) and vitamin A through your bloodstream. It also helps regulate how your body uses energy. If your prealbumin levels are lower than normal, it may be a sign of malnutrition.

Question 37

what’s α1- fetoprotein

Answer 37

Synthesized primarily by the fetal yolk sac and then by liver parenchymal
cells.
• normally it is not produced in adults, abundant in very low levels.
• Level of α1-fetoprotein increases in: - -
- Fetus and pregnant women Normally
- Hepatoma & acute hepatitis (cancer in liver)

Question 38

Functions of α1-fetoprotein:,4

Answer 38

Functions of α1-fetoprotein:
• Protecting fetus from immunotypic attacks
• Modulating the growth of fetus
• Transporting compounds e.g. steroids
• Low level in pregnancy: increased risk of Down’ssyndrome.

Question 39

what’s α 1 – antitrypsin (52 kDa)

Answer 39

Also known as antiproteinase was first discovered as an antagonist (neutralizer) for
trypsin. Trypsin is a serine protease (hydrolase) that breaks down proteins. ,Antitrypsin breaks down elastase then the lung tissue is regenerated. So,
Antitrypsin prevents excessive damage of tissues

Question 40

problems associated with α 1 – antitrypsin, 2

Answer 40

1) A deficiency of Alpha-1 antitrypsin.
2) Mutated alpha-1 antitrypsin
if a person has any of the above-mentioned cases, during
inflammation, elastase will be released by macrophages and it will work
on digesting elastin of the microorganism and elastin of the lungs, but
since alpha-1 antitrypsin is not working well or not present in adequate
amounts, elastase will continue to digest elastin in the lung causing
problems.

Question 41

what’s Emphysema

Answer 41

Emphysema is characterized by having a barrel chest and difficulty in
breathing.

Question 42

how dose smoking cause emphysema

Answer 42

Smoking is a major cause of emphysema. It causes chronic
inflammation, so elastase is always produced by immune cells in the
lungs,so, Lung tissue will be broken down. If a person smokes and
has a ZZ phenotype, their case will be devastating.

Question 43

what’s Haptoglobin

Answer 43

Some hemoglobin molecules leave RBCs to plasma, the function of HP is to
bind to free hemoglobin (65 kDa) to prevent them from getting filtrated in
the kidneys and leaving with urine, because even though our body can
produce heme and globin, it can’t produce iron (trace metal).

Question 44

half life of Haptoglobin

Answer 44

Half-life of free HP is 5 days, when it is bound to hemoglobin the half-life of
the complex becomes 90 mins (MW=150 kDa), so the complex is transported
and broken in the liver quickly, and iron is extracted from the complex.

Question 45

what happens to the level of haptoglobin in hemolytic anemia

Answer 45

In cases of hemolytic anemia (damaged RBC→ more hemoglobin in plasma) the
level of HP decreases as it binds to the hemoglobin and gets broken in the liver.

Question 46

how many atoms of copper dose Ceruloplasmin contain

Answer 46

6

Question 47

what happens when Ceruloplasmin concentration decreases in the blood

Answer 47

Ceruloplasmin concentration is decreased, less affinity for binding to
the copper, this results in increment of Cu in plasma thus it enters
tissues, the person’s skin and eyes will become bronzy.

Question 48

what’s Wilson disease

Answer 48

copper is not put in ceruloplasmin. The disease also keeps your liver from sending extra copper to be eliminated in your bowel movements. Instead, copper builds up in your liver until it overflows into the bloodstream. From there, copper builds up in your brain, corneas, kidneys, liver, bones, and small glands near the thyroid. If not treated, the liver and brain damage due to copper poisoning from Wilson disease is fatal.

Question 49

enzymes that use copper

Answer 49

oxidative phosphorylation enzymes (complex IV) for ATP production
ferroxidase which oxidizes ferrous to ferric (transferrin) amine
oxidase, copper dependent superoxidase dismutase, cytochrome
oxidase, tyrosinase(catalyzes the production of melanin)

Question 50

T/F C Reactive Protein (CRP) is an acute phase protein

Answer 50

True, It is undetectable in healthy individuals.
But its levels increase in cases of inflammatory diseases (like acute
rheumatic fever, bacterial infection, gout), trauma, cancer and tissue
damage.