ITM 2 | BIOCHEMISTRY

LESSON #07 - PLASMA PROTEINS

1st YEAR | A.Y. 2023-2024 | March 14, 2024
DR. Eduardo Domingo Jr., MD, FPCR, FPSVIR

● Serum
LESSON OUTLINE ○ the liquid part of blood AFTER coagulation,
● Components of Blood
therefore devoid of clotting factors as
● Functions of Blood
fibrinogen
● Starling Force
○ Values of Pressure
● Plasma Proteins Speaker’s note:
○ Half-life of Plasma Proteins ● Major component that is absent in serum is
○ Functions of Plasma Proteins
circulating fibrinogen.
○ Albumin
○ Haptoglobin
● If you centrifuge the blood, what you will get in the
○ Ferritin white part is the serum because it's devoid of
○ Transferrin fibrinogen, the clotting factors, and all other
○ Ceruloplasmin involved proteins.
● Total Iron Binding Protein ● In the laboratory, serum is usually preferred
○ Iron Deficiency Anemia because it yields real value or content of plasma
○ Iron Overload due to the fact that most of the proteins in the
● Intracellular Iron Homeostasis blood are albumin.
● Hepcidin
● Associated Diseases in Iron Regulation
○ IDA ● Total protein and albumin-globulin ratio
○ Hereditary hemochromatosis ○ Most abundant protein in the blood, either
○ Wilson’s Disease
in plasma or serum is albumin, other
○ Kayser-Fleischer Rings
proteins are globulins, including
● Deposition of Plasma Proteins into Tissue
○ Amyloidosis
immunoglobulins.

Speaker’s note:
COMPONENTS OF BLOOD
● When something is attached to albumin, it is
usable.

FUNCTIONS OF BLOOD

1. Respiration transport of oxygen from the lungs

Figure 1. Blood components
● Plasma
○ the liquid, cell-free part of the blood, that
has been treated with anticoagulants
○ white component of an anticoagulated
blood
Speaker’s note:
● Plasma is what’s inside our body.
● If it’s outside, you have to add anticoagulants,
meaning the fibrinogen, the clotting factors are still
there.
● Most plasma is protein-rich.
● 10. Coagulation
to the tissues and of CO, from the tissues to
the lungs
2. Nutrition - transport of absorbed food materials
3. Excretion - transport of metabolic waste to the
kidneys, lungs, skin, and intestines for removal
4. Maintenance of the normal acid-base balance
in the body
5. Regulation of water balance through the
effects of blood on the exchange of water
between the circulating fluid and the tissue
fluid
6. Regulation of body temperature by the
distribution of body heat
7. Defense against infection by the white blood
cells and circulating antibodies
8. Transport of hormones and regulation of
metabolism
9. Transport of metabolites

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ITM 2 | BIOCHEMISTRY
LESSON #07 - PLASMA PROTEINS
1st YEAR | A.Y. 2023-2024 | March 14, 2024
DR. Eduardo Domingo Jr., MD, FPCR, FPSVIR
PLASMA PROTEINS
● Plasma contains a complex mixture of proteins.
● Early scientists classified these proteins into three
groups, fibrinogen, albumin, and globulins, on
the basis of their relative solubility in the presence
of added organic solvents such as ethanol or
salting out agents such as ammonium sulfate.
● With the advent of electrophoresis, plasma proteins
were grouped into:
○ Albumin - densest, largest
○ Globulins
○ Alpha 1
○ Alpha 2
○ Beta
○ Gamma - lightest
● Synthesized in liver
● Mostly are glycosylated - proteins are attached to
the glycosides or carbohydrates (glycoproteins)
● Exhibits polymorphism
● Help determine the distribution of fluid between
blood and tissue
○ Most proteins maintain oncotic or osmotic
pressure in the blood.
Clinical notes: Edema is caused by decreased albumin.
● Plasma proteins are rich in disulfide bonds, which in
turn bonds into the carbohydrates and lipid
component of the blood, resulting in glycoprotein
and lipoprotein, respectively.
VALUES OF PRESSURE
● Plasma - 25mmHg
● Arterioles - 37mmHg
● Interstitial - 1mmHg
● Venules - 17mmHg
Speaker’s note:
● Homeostasis of fluid in the blood depends on the
oncotic and hydrostatic pressures.
● Major contributor of the oncotic pressure of the
plasma is albumin.
● The aggregate concentration of the proteins
present in human plasma falls in the range of 7 to
7.5 g/dL.
● The resulting osmotic pressure (oncotic pressure) is
approximately 25mmHg. Since the hydrostatic
pressure in the arterioles is approximately
37mmHg, with an interstitial (tissue) pressure of
1mmHg opposing it, a net outward force of about
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11mmHg drives fluid from the plasma into the
interstitial spaces.
● By contrast, the hydrostatic pressure in venules is
about 17mmHg; thus a net force of about 9mmHg
drives water from tissues back into the circulation.
Speaker’s note:
● This force is called the Starling Force.
STARLING FORCE
● Pressure mechanism of the blood, oncotic, and
hydrostatic which in turn, the exchange of water
into the interstitial and intracellular compartment of
the cell.
HALF-LIFE OF PLASMA PROTEIN
● The 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.
○ For example, the half-lives of albumin and
haptoglobin in healthy adults are
approximately 20 and 5 days, respectively.
● Under normal circumstances, as older protein
molecules are cleared they are replaced by newly
synthesized ones, a process called turnover.
● During normal turnover, the total concentration of
these proteins will remain constant as the
countervailing processes of synthesis and
clearance reach a steady state.
Speaker’s note:
● Remember the half-life, turnover, and steady state.
These are the main mechanisms which maintain
the homeostasis or the value of any proteins in the
blood.
● All proteins have their half-life, then, the body will
go to the turnover phase to replace what’s missing
to reach the steady state.
● The goal of the body is for the proteins or any
components of the blood to reach the steady state
phase.
● When most components of blood reach 50% or its
half-life, that is when the turnover phase is
activated.
○ Example: Half life of RBC is 30 days,
turnover phase will be activated, that is
why there will be an activation of the
erythropoietin to produce another RBC to
reach steady state (equilibrium).
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ITM 2 | BIOCHEMISTRY
LESSON #07 - PLASMA PROTEINS
1st YEAR | A.Y. 2023-2024 | March 14, 2024
DR. Eduardo Domingo Jr., MD, FPCR, FPSVIR
ALBUMIN
● most abundant protein in the human plasma;
60% by mass
● Major determinant of osmotic pressure
● Acts as acute phase proteins
Speaker’s note:
● Acute Phase Proteins A.K.A Acute Phase
Reactants
Table 1. Some Functions of Plasma Proteins
Function Plasma Proteins
Antiproteases Antichymotrypsin
a1 - Antitrypsin
a2 - Macroglobulin
Antithrombin
Blood Clotting Various coagulation
factors, fibrinogen
Enzymes Functions in blood, for
example, coagulation
factors, cholinesterase
leakage from cells or
tissues, eg,
aminotransferases
Hormones Erythropoietin
Immune Defense Immunoglobulins,
complement proteins,
and B2 -Macroglobulin
Involvement in Acute phase response
Inflammatory Response proteins (eg, C-reactive
protein, a1 -acid
glycoprotein
[orosomucoid])
Oncofetal a1 - Fetoprotein (AFP)
Transport or Binding Albumin (various
Proteins ligands, including
bilirubin, free fatty acids,
ions [Ca2+], Metals [eg.
Cu2+, Zn2+], metheme,
steroids, other
hormones, and a variety
of drugs)
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Corticosteroid-binding
globulin (transcortin)
(binds cortisol)
Haptoglobin (binds
extracorpuscular
hemoglobin)
Lipoproteins
(chylomicrons, VLDL,
LDL, HDL)
Hemopexin (binds
heme)
Retinol-Binding Protein
(binds retinol)
Sex-Hormone-Binding
Globulin (Binds T3, T4)
Transferrin (Transport
Iron)
Transthyretin (formerly
prealbumin; binds T4 and
forms a complex, with
retinol-binding protein)
Speaker’s note:
● Based on the table above, Albumin is the most
abundant protein.
● Usually, Albumin binds to Ligands. It binds to
another component of the blood for it to be usable
or transportable.
● Haptoglobin
○ Binds to extracorpuscular hemoglobin
to prevent the formation of damaging
precipitates in the tubules
Speaker’s note:
● Haptoglobins function similarly to transferrin but
in the extracorpuscular part or outside of the
RBCs.
● Ferritin
○ Binds to and stores ferric iron inside
cells
Speaker’s note:
● Ferritin is Activated and Degraded to release iron
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ITM 2 | BIOCHEMISTRY
LESSON #07 - PLASMA PROTEINS
1st YEAR | A.Y. 2023-2024 | March 14, 2024
DR. Eduardo Domingo Jr., MD, FPCR, FPSVIR
● Ferritin is inversely proportional to transferrin
(negative feedback mechanism)
● Transferrin
○ Transports iron to the sites where it is
required
Speaker’s note:
● Main transporter of Iron
● Transfers Iron from Tissue to a site where there is
an increase of demand for such
● Ceruloplasmin
○ The major copper containing protein in
plasma
Speaker’s note:
● Ceruloplasmin is responsible for Converting
Ferrous to Ferric Iron
● Ferrous (deduced form of Iron) is non-usable by
the body. It is absorbed by the intestine into the
intracellular compartment.
● Ferric is the Active Form of iron that is used by
the body
● The Senescent Red Blood Cells are processed
in the Reticulo-Endothelial System (Spleen): the
RBCs must be Discoid in shape and Absence of
a Nucleus.
● Any Change in the RBCs (eg. Hemosiderin
Bodies) triggers the RES Macrophages to activate
Splenic Culling or Splenic Pitting.
Splenic Culling: the ability of this organ to scrutinize the
passing red cells and to remove from circulation those
which do not meet certain minimum requirements.
Splenic Pitting: ability to remove a solid particle from the
cytoplasm of a red cell without destroying the cell itself
● Hemosiderin Granules: Triggered by Infections.
Addressed by the spleen in two ways. (1)
Destruction or (2) Splenic Pitting
● Bite Cell: An irregular RBC that is subjected to
Splenic Culling. Increases with Hemosiderin.
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● HIGH YIELD!!! ALWAYS REMEMBER THESE
FOUR PROTEINS: Haptoglobin, Ferritin,
Transferrin, and Ceruloplasmin. These are the
plasma proteins responsible for Iron Synthesis or
Iron Homeostasis in the blood.
● Imperfectly shaped RBCs are highly susceptible
to Splenic Culling which increases RBC
turnover.
Figure 2. Recycling of Iron in Macrophages. Senescent
erythrocytes are phagocytosed by macrophages. Hemoglobin is
degraded and iron is released from heme by the action of the
enzyme heme oxygenase. Ferrous iron is then transported out of
the macrophage via ferroportin (Fp). In the plasma, it is oxidized to
the ferric form by ceruloplasmin before binding to transferrin (Tf).
Iron circulates in blood tightly bound to Tf.
Speaker’s note:
● Heme Molecule contains the “Gold-Like”
substance iron
● Iron is a Precious Substance in the body. iron is
preserved through storage recycling.
● Exogenous Iron (intake of Iron Sulfate): is not
eliminated by the body unless it is subjected to
chelation.
Chelation: a type of bonding of ions and molecules to
metal ions. It involves the formation or presence of two or
more separate coordinate bonds between a polydentate
(multiple bonded) ligand and a single central metal atom.
● Ferroportin: serves as a gate that transfers iron
from the intracellular to extracellular component of
the cell
● Ceruloplasmin: converts Ferrous Iron to Ferric
Iron (non-function to functional form) then it will
bind to Transferrin to be used by other tissues. It
can also be stored in the liver in the form of
Ferritin.
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ITM 2 | BIOCHEMISTRY
LESSON #07 - PLASMA PROTEINS
1st YEAR | A.Y. 2023-2024 | March 14, 2024
DR. Eduardo Domingo Jr., MD, FPCR, FPSVIR

Speaker’s note:
● In people with Iron Deficiency Anemia, women with
menses or post pregnancy, they are usually given
Vitamin C with Iron supplements to hasten the
conversion of Ferric to Ferrous state

● Once converted into the Ferrous state, it will

be transported into the intracellular
compartment of the enterocyte via the divalent
metal transporter1 (DMT1).

Speaker’s note:
● Divalent metal transporter1 (DMT1) transports any
metal with a 2+ charge hence the name “divalent”
● For example Ca2+, Cu2+, Fe2+ etc.

● Once inside the intracellular compartment of

the enterocyte, the Ferrous iron is reversibly
Figure 3. Nonheme (Exogenous) Iron Transport in Enterocytes. converted in the Ferric state as Ferritin or
Ferric iron is reduced to the ferrous form by a luminal
transported out of the cell by Ferroportin
ferrireductase, duodenal cytochrome b (Dcytb). Ferrous iron is
transported into the enterocyte via divalent metal transporter1 ● On the surface of the enterocyte is an
(DMT1). Within the enterocyte, iron is either stored as ferritin, or analogue of Ceruloplasmin known as
transported out of the cell by ferroportin (Fp). Ferrous iron is Hephaestin. This oxidizes the Ferrous iron
oxidized to its ferric form by hephaestin. The ferric iron is then back to its Usable Ferric state.
bound by transferrin for transport by the blood to various sites in
● The ferric iron is then bound by transferrin for
the body. (Based on Andrews NC: Forging a field: the golden age
of iron biology. Blood 2008;112;219.) transport by the blood to various sites in the
body.
Speaker’s note:
Table 2. Distribution of Iron in a 70kg Adult Male
● Exogenous absorption of Iron majorly occurs in the
Small Intestines (Duodenum and Proximal
Jejunum)
● Iron Malabsorption Symptoms: occurs when
there is a mass, parasite, or ulcers in the small
intestines which leads to decreased absorption of
iron (Iron Deficiency Anemia)

● Fe3+ (Ferric) is not absorbable in the body and

needs to be converted to Fe2+(Ferrous) state. Table 2 shows the normal values in a “Steady State”.
● 2 mechanisms: Notice how the Absorption is equal to the Losses.
○ By ingested oxidants or reducing
agents such as Vitamin C TOTAL IRON BINDING PROTEIN (TIBC)
○ Enzymatically by a brush border ● TIBC is a picture of your Transferrin.
membrane bound ferrireductase, ● Determines how much or how little iron there is
duodenal cytochrome b (Dcytb) in our body.
(Figure) ● The goal of transferrin is to transfer the
necessary amount of iron needed by the body
either to store as ferritin or used up by tissues.

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LESSON #07 - PLASMA PROTEINS
1st YEAR | A.Y. 2023-2024 | March 14, 2024
DR. Eduardo Domingo Jr., MD, FPCR, FPSVIR
● Transferrin is always active and always has
iron bound or occupied to it
● Of the 3-4mg of Transferrin, 30% of it is
occupied most of the time (normal).
Table 3. Examples of conditions affecting TIBC
Example % of Transferrin TIBC
occupied
Iron 16% Increased
Deficiency
Anemia
Iron 45% Decreased
Overload
● Iron Deficiency Anemia
○ Decreased iron means there are fewer
transferrin receptors bound to iron
thereby increasing its Capacity to bind
more.
● Iron Overload
○ Increased iron means there is
oversaturation of the transferrin
receptors with iron thereby decreasing
its Capacity to bind more.
Speaker’s note:
● TIBC depends on the number of occupied
receptors on your transferrin
Figure 4. Fenton Reaction
● The fenton reaction occurs when there is free
iron.
● Free iron is extremely toxic and can catalyze
the formation of hydroxyl radical (OH⋅) from
hydrogen peroxide.
● The hydroxyl radical is a transient but highly
reactive species that oxidize cellular
macromolecules resulting in tissue damage.
INTRACELLULAR IRON HOMEOSTASIS
● Regulated by a important Proteins
Receptors namely:
○ Iron Regulatory Protein (IRP)
○ Iron Response Element (IRE)
○ Transferrin Receptor 1 (TfR1)
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■ Most abundant and seen on the
surface of most cells
○ Transferrin Receptor 2 (TfR2)
■ Found primarily on the surface
of hepatocytes and the crypt
cells of the small intestine.
Figure 5. Schematic representation of the reciprocal relationship
between synthesis of ferritin and the transferrin receptor (TfR1).
● The mRNA for ferritin is represented on the
left, and that for TfR1 on the right of Figure.
● Ferritin mRNA:
○ (Ai) At high concentrations of iron, IRP
does not bind to IRE at the 5’ end of
the mRNA which translates to Ferritin
(storage form) → store.
○ (Aii) At low concentration of iron, IRP
binds to IRE at the 5’ end of the mRNA
which blocks the translation of Ferritin
→ no storage.
● TfR1 mRNA:
○ (Bi) At high concentration of iron, IRP
does not bind to IRE at the 3’ end of
the mRNA which degrades TfR1 → no
transferring of iron.
○ (Bii) At low concentration of iron, IRP
binds to IRE at the 3’ end of the mRNA
which translates to TfR1 → increase
transferring of iron.
Speaker’s note:
and
● Refer to Figure 4. Fenton Reaction
● Ceruloplasmin is necessary in converting ferrous
to ferric state.
● If it is not converted and it accumulates, some of
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ITM 2 | BIOCHEMISTRY
LESSON #07 - PLASMA PROTEINS
1st YEAR | A.Y. 2023-2024 | March 14, 2024
DR. Eduardo Domingo Jr., MD, FPCR, FPSVIR

them turn into highly ROS which is cytotoxic to the → ↓ Hepcidin

cells.
● This is the reason why some people take
antioxidants to reduce ROS.
HEPCIDIN
● Regulates iron homeostasis by blocking
internalization of the cellular iron export
protein, ferrocidin
● Stimulated when binding of transferrin iron
complexes to types 1 transferrin receptors
displaces HFE protein, which then binds to
and activates type 2 transferrin receptors
Speaker’s note:
1. IDA (Iron Deficiency Anemia): If the level of
● In short, Hepcidin is the major iron-regulating
protein in our bodies, primarily produced by the
liver
● It does not respond in the feedback mechanism, it
only conserves the iron intracellularly
Speaker’s note:
Figure 6. Role of hepcidin in systemic iron regulation. Hepcidin
binds to and triggers the internalization and degradation of
ferroportin expressed on the surface of enterocytes and
macrophages. This decreases iron absorption from the intestine
and inhibits iron release from macrophages, leading to
hypoferremia.
● High turnover rate (e.g., rapid red blood cell
production) → Suppresses hepcidin → Increases
iron absorption and release from stores to meet
demand.
● Steady state reflects balance between iron intake
and loss → Hepcidin helps maintain this balance
by regulating iron absorption and recycling.
● Overall, the biochemical process of iron
conservation involving hepcidin helps maintain
iron balance in the body by regulating iron
absorption, recycling, and storage in response
to varying physiological conditions.
ASSOCIATED DISEASE IN IRON REGULATION
transferrin saturation falls to 20% or below,
hemoglobin synthesis will be impaired,
resulting in iron-deficient erythropoiesis
● Diet and blood loss (e.g., menstruation - common
in women) affect iron levels.
● In Africa, nutritional deficiencies and high rates
of iron deficiency anemia (IDA) are common due
to factors such as inadequate dietary iron intake
and limited access to iron-rich foods or
supplements.
○ Traditional iron cooking utensils, such
as iron pots, pans, and cooking stoves,
are commonly used.
○ IRON FISH can contribute to the dietary
intake of iron, as some iron leaches into
the food during cooking, especially when
cooking acidic foods like tomatoes.

Speaker’s note:
● ↑ Iron levels/inflammation/erythropoiesis → ↑
Hepcidin production
● Hepcidin binds to ferroportin (found on the surface
of cells involved in iron export: e.g. enterocytes in
the intestine and macrophage in the
reticuloendothelila system) → ↓ Iron export from
enterocytes and macrophages
● ↓ Iron absorption from diet → Iron conservation
● Feedback regulation: ↑ Iron → ↑ Hepcidin; ↓ Iron

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LESSON #07 - PLASMA PROTEINS
1st YEAR | A.Y. 2023-2024 | March 14, 2024
DR. Eduardo Domingo Jr., MD, FPCR, FPSVIR

Figure 7. Lucky Iron Fish Ⓡ A Natural Source of Iron

2. Hereditary hemochromatosis:
Hemisoderosis, the accumulation of
stainable concentrations of iron in tissues.
Hereditary hyperabsorption of iron by the
intestines can be caused by mutations in the
gene encoding homeostatic iron regulator
protein (HFE), or, less frequently, hepcidin,
TfR2, HJV, or ferroportin. Figure 9. Wilson’s Disease (Hepato-Lenticular Degeneration)

Speaker’s note:
● Iron is to hemoglobin
● Copper is to ceruloplasmin
● Ceruloplasmin is a protein produced in the liver.
● It binds to copper in the blood, forming
holo-ceruloplasmin.
● Holo-ceruloplasmin delivers copper to tissues and
cells.
○ Ceruloplasmin is needed for the
conversion of ferrous iron (Fe2+) to
ferric iron (Fe3+) in the blood.

Figure 8. Hereditary hemochromatosis Pathogenesis

3. Wilson’s Disease: A mutation in the gene for

a copper-binding P-type ATPase (ATP7B
protein) blocks the excretion of excess
copper in the bile.

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LESSON #07 - PLASMA PROTEINS
1st YEAR | A.Y. 2023-2024 | March 14, 2024
DR. Eduardo Domingo Jr., MD, FPCR, FPSVIR

Table 4. Changes in Various Laboratory Tests Used to Assess Iron-Deficiency Anemia

Table 5. Iron Overload Conditions

Speaker’s note:
● Most cases of secondary hemochromatosis are disease-related or pathologically related.
● Thalassemia major is a severe form of thalassemia that requires regular blood transfusions to manage the
anemia.
○ One of the major complications of thalassemia major is iron overload, which can lead to
hemochromatosis.
● Oxidative stress in red blood cells (RBCs) can lead to the formation of hemosiderin, a complex of ferritin
and denatured ferritin, which is a form of iron storage.
○ Hemosiderin is formed when there is an excess of iron that exceeds the binding capacity of ferritin,
leading to the deposition of iron in the form of hemosiderin granules in various tissues, including
the liver, spleen, and bone marrow.
○ Regular transfusion of packed red blood cells (PRBCs) can increase the deposition of hemosiderin
in tissues over time.

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LESSON #07 - PLASMA PROTEINS
1st YEAR | A.Y. 2023-2024 | March 14, 2024
DR. Eduardo Domingo Jr., MD, FPCR, FPSVIR

Speaker’s note:
KAYSER-FLEISCHER RINGS
● In amyloidosis, proteins misfold into a
beta-pleated sheet configuration (see figure
below).
● These misfolded proteins aggregate into insoluble
fibrils.
● The fibrils deposit in various tissues throughout
the body and the deposition of amyloid fibrils
can lead to organ dysfunction and damage.
● Amyloidosis can affect organs such as the
Figure 10. A Kayser-Fleischer ring (Copper accumulation from kidneys, heart, liver, and nervous system.
Wilson’s Disease) in a 32-year-old patient who had long standing
speech difficulties and tremor

● Pathognomonic of Wilson’s Disease

Figure 12. Physical Structure of Amyloid Material

Figure 11. Descemet’s membrane

● Caused by direct copper deposition in the

Descemet membrane of the cornea and are
thought to be from epithelial cells absorbing
Figure 13. Major pathological hallmarks of AD are amyloid plaques
copper from the aqueous humor and neurofibrillary tangles

DEPOSITION OF PLASMA PROTEINS INTO TISSUE

Speaker’s note:
● Amyloidosis
○ Impairment of tissue function that
results from the accumulation of
insoluble protein
○ Deposition of insoluble proteins into the
tissue
Table 6. A Classification of Amyloidosis
● Alzheimer's disease, beta-amyloid protein
aggregates into insoluble plaques in the brain.
These plaques are primarily composed of
beta-pleated sheets, similar to the fibrils found
in amyloidosis.
● The aggregation contributes to neuronal damage
and cognitive decline.
● The accumulation of beta-amyloid plaques,
along with tau tangles (neurofibrillary tangles),
is a hallmark of Alzheimer's disease pathology.

REFERENCES
● Kennelly. (2022). Harper's Illustrated Biochemistry
32e (i: E) Ional Experien:ce.
● Doc’s PPT: https://shorturl.at/etGQ8

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