ALBUMIN

Group Members:
1. Kadija Andrews
2. Kimberly Daniels
3. Yonessa Fredricks
4. Jamal Joseph
5. Keisha Kellman
6. Bernard Mc David
7. Faila Ndjelekulu
8. Shekila Isaacs
9. Safiya Victorine
10. Shannon Wright

OBJECTIVES
Structure of albumin
Biochemical function of albumin
Disorders in relation to structure and function
Treatment of the disorder

WHAT IS
ALBUMIN?

Protein produced by the liver

Most abundant protein found in blood plasma

Involved in multiple function such as transport of small

molecules, binding to toxins, maintenance of osmotic or oncotic
pressure, etc.

PRIMARY STRUCTURE

Protein is a single polypeptide chain comprising of 585 amino

acids residues

Contains 17 pairs of disulphide bridges, one free thiol group

(cysteine 34) and a single tryptophan (tryptophan 214)

There are no prosthetic groups

SECONDARY STRUCTURE

67% of the proteins consists of consist of alpha helices

There are no beta pleated sheets

TERTIARY STRUCTURE
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The protein consist of 3 structurally similar globular domains

Each domain consists of 2 subdomains; there are six subdomains in all:
IA, IB, IIA, IIB, IIIA and IIIB.
There are two high binding sites for small heterocyclic or aromatic
compounds (on subdomains IIA and IIIA).
There are two to three dominant long-chained fatty acids binding site
(on subdomains IB and IIIB)
There are two distinct metal binding sites, involving cys 34 and the
other N terminus, making a total of six ligand binding sites on albumin.

PICTURE SHOWING THE THREE DOMAINS AND

SUBDOMAINS OF ALBUMIN

BIOCHEMICAL FUNCTIONS OF ALBUMIN

Human serum albumin (HSA), performs multiple
functions, including;
Ligand binding
Anti- oxidant
Maintenance of Oncotic pressure
Protectivecolloid- protein that stabilizes other
proteins
Anti- inflammatory

LIGAND BINDING
Binds

and transports many exogenous and endogenous molecules;

Includes transport of fatty acids, metal ions, pharmaceuticals, and
metabolites;
Implications for drug delivery and efficacy, detoxification, and
antioxidant protection.
Low and High affinity Ligand Binding Sites responsible for binding of
most pharmaceuticals
Site 1: large and flexible; tends to bind relatively large heterocyclic
compounds(drugs, pesticides, vitamins, antibiotics) or dicarboxylic
acids. It also binds to bulky endogenous substances like bilirubin and
porphyrins
Site2 (indole-benzodiazepine site) : smaller, less flexible; binding is
more stereospecific.

LIGAND BINDING

Metal Binding;
N- terminal binds with high affinity- Cu, Ni, and Co;
Au, Ag, and Hg ions bind to cysteine-34
Has relatively weak, nonspecific, latent iron-binding capacity

Antioxidant
An antioxidant is a substance which when present in low or high
concentrations prevents the oxidation of oxidizable substrates.
Pro- oxidants-heme; redox- active transition metals like iron and
copper(catalyze formation of Reactive Oxygen Substances( ROS),
that are toxic)
Primary Antioxidants prevents ROS formation e.g. iron binding
antioxidant transferrin
Secondary Antioxidant- scavenge pre- formed ROS.
Albumin reduces their pro- oxidant effect
Prevents damage that toxins may cause to cells by being sacrificed

Maintenance of "osmotic or oncotic pressure

Functions to maintain the distribution
ofextracellularfluidbetweenthevascularandextravas-cular
compartments.

Oncotic pressure becomes osmotic pressure as the negative charges

surrounding the protein molecules attract sodium, thus holding
water.

ANTI- INFLAMMATORY

Accessible thiol group communicates with inflammatory

cells depending on its redox state

25% albumin has been shown to modulate

neutrophil/endothelial cell interactions after shock and
resuscitation and to attenuate lung injury.

DISORDER IN RELATION TO
STRUCTURE
Main Cause of disorder:
Glycation- (sometimes called non-enzymatic glycosylation) is the result
of typically covalent bonding of a protein or lipid molecule with a sugar
molecule, such as fructose or glucose, without the controlling action of an
enzyme. This causes impairment of the function of biomolecules and
hence alters the structure of the molecules.
serum albumin may undergo a slow non-enzymatic glycation, mainly by
formation of a Schiff base between -amino groups of lysine (and
sometimes arginine) residues and glucose molecules in blood (Maillard
reaction).
Glycation can result in the formation of Advanced Glycation EndProducts (AGE). Accumulation of AGEs leads to tissue damage, stimulation
of cellular responses, through receptors specific for AGE-proteins, and
generation of reactive oxygen intermediates. AGEs also react with DNA,
thus causing mutations and DNA transposition.

DISORDER IN RELATION TO
STRUCTURE
Glycation gives rise to most functional impairment e.g. failure to
function as an antioxidant(becomes oxidative), Binding and
transportation of Tryptophan, mutation of genes etc.
The acute loss of albumin in the nephrotic syndrome leads to severe
generalized peripheral edema and difficulties in maintenance of normal
blood pressure as well as hypocalcemia.
Persons with impaired albumen may incur sleeping disorders.
N.B Persons with diabetes are more proned to having glycation of
proteins.

Impaired structure

Normal Albumin structure

DISORDER IN RELATION TO STRUCTURE

Biological Impact of Glycation
Glycated Albumen has some clinical implications since:
It is involved in the damages associated with Diabetes mellitus,
such as Retinopathy, Nephropathy, Neuropathy and Coronary artery
disease.
Several in vitro studies have shown the implication of glycated
albumin in Platelet activation and aggregation
The lowering aggregation effects of glycated albumin have also
been demonstrated in Erythrocytes
Another pathogenic implication of glycated albumin can also be
observed in glucose metabolism of both skeletal muscle and
adipocyte cells

Disorders in relation to Structure

Contd
While for some studies glycated albumin is suggested as an
alternative marker for glycemic control in many diabetes
complications

such

as

Nephropathy,

Retinopathy,

and

Alzheimers disease and also in the case of Hemodialysis

patients or gestational diabetes.
NOTE: It should be noted that in some cases such as Thyroid
dysfunction, Nephrotic syndrome or liver cirrhosis in which the
amount of albumin is affected then glycerated albumen will no
longer be a suitable indicator.

DISORDERS IN RELATION TO FUNCTION

What causes the level of albumin to change
The normal level of albumin in adults is 3.5 to 5 g/dL and for
children, 4 to 5.9 g/dL.
Plasma levels of albumin may be increased or decreased depending
on the disease state. Elevations of serum albumin concentration occur
infrequently. Increases resulting from dehydration can be seen when
plasma water decreases. Upon rehydration, the albumin level usually
returns to normal.
An example of disruption of these pressures is edema. There are
several causes of extracellular edema, such as a decrease in plasma
proteins that includes albumin. The cause may be an increased loss of
proteins (ie, nephrosis, wounds, etc) or failure to produce proteins (ie,
liver disease or malnutrition).

DISORDER IN RELATION TO FUNCTION

CONTD
A decrease in the albumin level may be the result of decreased
synthesis, increased catabolism (use and loss), or combinations of
these. A deficiency known as analbuminemia is possible.
The most common cause of decreased plasma albumin levels is
related to inflammatory processes (i.e. acute-phase response and
chronic inflammatory disorders)
Urinary loss of albumin may lead to decreased levels.
What happens if there is a deficit?
Hypoalbuminemia
Hyperalbuminemia

DISORDERS IN RELATION TO FUNCTION

CONTD
Hyperalbuminemia

1.

An increased concentration of human serum albumin in the blood above the normal range of
3.5 and 5 g/dL.
Condition is a sign of severe dehydration.
Hyperalbuminemia is also linked to Vitamin A deficiency.
Also associated with high protein diets.
Contributing factors for hyperalbuminemia include:
1. Severe infections
2. Hepatitis
3. Kidney diseases
4. HIV/AIDS
5. Cancer
6. Chronic inflammatory diseases
7. Amyloidosis
High levels of albumin in the blood, is actually a symptom of dysfunction within the body.

DISORDERS IN RELATION TO FUNCTION CONTD

Hypoalbuminemia
What is hypoalbuminemia?
Hypoalbuminemia also known as low albumin is a medical condition where the levels of albumin in the
blood are extremely low.
Underlying causes of Hypoalbuminemia
Some causes of Low albumin levels in the body are:
Renal Dysfunction
Liver Diseases
Certain Heart Conditions
Problems with your stomach
Infections
Side effects of some medication
Signs and symptoms of hypoalbuminemia:
1. Swelling all over the body or swelling in a specific part of the body for e.g. in your legs
2. The patient may experience muscle fatigue , weakness or cramps
3. They may experience poor appetite.
4. Specifically patients that have liver problems may notice that the abdomen is swollen with fluids.

TREATMENT OF DISORDER
Hypoalbuminemia
In order to restore the normal levels of albumin in the body, it is important to treat the underlying cause of
the condition. Hypoalbuminemia may be caused by:

Inadequate nutrition- follow a diet plan that provides the required amount of proteins eg. Milk,
eggs,meat,beef,beans and peanut.

Renal dysfunction- medication, exercise and diet

Chronic Liver failure- the use of alcohol should be put to an end

Heart Condition-colchine is useful because it redues inflamination

Stomach Ailments- conditions such as lymphoma can be

treated by chemo radiation or surgery is done based on the stage of the
cancer

Lung Infection - people suffering from latent tuberculosis may need

one antibiotic, whereas people with active TB(particularly MDR-TB) will often require a
prescription of multiple drugs.
Hyperalbuminemia
In order to treat hyperalbuminemia, the following treatment procedures may be used:

Chronic dehydration- replacement of fluid orally by consuming water

Regulating diet.

Retinol (Vitamin A) deficiency use of artificial tear drops and ointments.

TREATMENT OF THE DISORDER

Albumin may be used for treating a variety of conditions,
including:
Shock due to blood loss in the body
Burns
Low protein level due to surgery or liver failure
Additional medicine for bypass surgery
Note: Albumin (human) is a concentrate of plasma proteins from
human blood. It works by increasing plasma volume or serum
albumin levels.

SUMMARY

REFERENCES

http://www.buzzle.com/articles/high-albumin-levels.html

http://medicinemosul.uomosul.edu.iq/files/pages/page_2072206.pdf

http://www.tandurust.com/health-faq-7/albumin-high-levels-causes.html