DEPARTMENT OF BIOCHEMISTRY

MRDC

LECTURE TOPIC : MINERALS AND TRACE ELEMENTS

LEARNING OBJECTIVES

•TO STUDY IN DETAIL THE METABOLISM OF MINERALS SUCH AS Ca, K, P, Na,

Fe, I, F etc
• TO LEARN THEIR DIETARY SOURCES, NORMAL BLOOD LEVELS AND DAILY
REQUIREMENT
• TO LEARN THE FUNCTIONS OF EACH OF THEM

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AT THE CONCLUSION, THE STUDENT IS EXPECTED TO UNDERSTAND AND

ANSWER-

 Calcium- availability and functions

 Factors regulating blood calcium level
 Calcium, clinical applications
 Phosphorous sources, functions
 Magnesium sources, functions
 Iron absorption, transport, deficiency
 Copper,Sodium,Potassium, Zinc, Fluoride, Selenium, Cobalt, Iodine -
availability and functions

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CALCIUM
1.Source: milk and milk products, egg etc.
2.Daily requirement;
Adult;0.5 gm
Pregnancy;1.5 gm
Children;1.0 gm
2. Body Distribution:
• About 99% found in bones
• Normal plasma level= 9-11mg%
 Ionised Ca(diffusible)= 40% active form
 Protein bound Ca (major protein albumin)
 Complexed ca (complexed with organic acid)
.
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 Absorption
Absorption:
Absorbed mainly from duodenum and first half of
jejunum against concentration gradient.
Mechanism 2
I. simple diffusion
II. ‘active’ transport- involving energy and Ca pump
Both processes require 1, 2-5 DHCC which regulates
synthesis of Ca binding proteins and transport
of Ca
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FACTORS AFFECTING ABSORPTION

• Vitamin D- promotes Ca absorption
• PTH- directly can not increase the Ca absorption but PTH stimulates 1-
hydroxylase enzyme in the kidney and increases the synthesis of vit. D
• Acidity- favors Ca absorption; as calcium salts phosphates &carbonates are
quite soluble in acid medium.
• In aikaline medium insoluble tricalcium phosphate is formed.
• Phytic acid- present in cereals. Decreases absorption and forms insoluble
salts.
• Oxalates: present in leafy vegetables. Decreases absorption
• Phosphates: causes precipitation of Ca3(PO4)2 and decreases Ca absorption
• Fibres: presence of Excess fibres in diet interferes calcium absorption
• High Protein diet ; high protein diet favours absorption.& Out of 15% Ca of
dietry Ca absorbed.oniy 5%may be absorbed,if the protein content is low.

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FUNCTIONS
1. Activation of enzymes:
2. Calmodulin (Ca binding regulatory protein) can bind 4
Ca++ and is a part of various regulatory kinases.
3. Excitation and contraction of muscles: Increases
reactions of actin and myosin
4. It decreases neuromuscular irritability, its deficiency
causes tetany.
5. Transmission of nerve impulse
6. Mediates secretion of certain hormones- insulin, PTH
7. Required for coagulation known as factor IV
8. Acts as second messenger of hormones eg: glucagon
9. Used for formation of bones and teeth
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BLOOD Ca REGULATION
Normal level (9-11 mg) maintained by
Vit D PTH Calcitonin Phosphorus

Vit. D

Calcitonin
Ca PTH
9-11mg%

Phosohorus

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I.Vitamin D
Active form of vitamin D is DHCC
Increases Ca absorption from gut.
Increases number and activity of osteoblasts (which induces
mineralisation)
II. PTH
Secreted by parathyroid glands
In bones PTH causes decalcification or demineralisation
Induces osteoclasts cell activity
In kidney - causes decreased renal excretion of calcium
Causes increase in excretion of phosphate
III. CACITONIN
Secreted by thyroid parafollicular cell
Decreases serum calcium level
Decreases activity of osteoclasts and increases activity of osteoblasts.
Calcitonin
LRM 18and PTH
I BDS,U.G are antagonistic.
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When blood Ca tends to lower When blood Ca tends to increase

• PTH secretion is stimulated • PTH secretion is inhibited
• Calcitonin is inhibited • Calcitonin is stimulated
• Bone demineralization leads to • Bone mineralization leads to
increase in serum calcium level decrease in serum calcium
level
IV. Phosphorus:
• Reciprocal relationship of calcium and phosphorus
HYPERCALCEMIA:
• Blood calcium is greater than 11 mg%
• Major cause is hyperparathyroidism
o Features- osteoporosis
o Bone resorption
o Fracture of bone
• Blood show high level of calcium and phosphorus
• Calcium maybe precipitated in urine leading to calculi
• Calcification maybe seen in urine renal tissue, pancreas, arterial
walls, muscle tissue
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HYPOCALCEMIA
• Serum calcium is less than 8.8mg%
• If lowered than 7.5%- tetany may result
• In tetany neuromuscular irritability is increased
• Main manifestations are spasm

Various causes of hypocalcemia

1. HYPERALBUMINAEMIA
Due to malnutrition, nephrotic syndrome, chronic liver disease and liver failure
2. HYPOPARATHYROIDISM
May be surgically induced, autoimmune
3. RENAL DISEASE
Renal tubular dysfunction, chronic renal failure etc.

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PHOSPHORUS
1. Sources: cheese, milk, egg meat etc.
2. Body Distribution:
• 85% in bones
• 15% in soft tissues
• 1% in E.C.F
3. Absorption
• 90% of daily dietary phosphate is absorbed
• Absorption is stimulated by both PTH and DHCC
4. Functions
• Constituent of bone and teeth
• For energy transfer as ATP, creatine phosphate
• For acid base balance, as phosphate buffer mixture
• Constituent of PL, nucleotides, LP and phosphoproteins
• As coenzyme NADP, TPP involved in enzymatic reactions
• Phosphorylation and dephosphorylation reactions
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• Clinical importance: Rickets and osteomalacia are important

deficiency disorders of calcium, phosphorus and vitamin D.

Increase calcium Decrease phosphate Primary hyperparathyroidism

Increase calcium increase phosphate Malignancy,post dialysis in

renal failure

decrease calcium increase phosphate hypoparathyroidism

decrease calcium Decrease phosphate Vitamin D deficiency

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SODIUM

1. Body distribution:
• 50% in bones
• 40% in ECF
• 10% in soft bones
2. Absorption:
• Absorbed by sodium pump situated in basal plasma
membrane which actively transports sodium into ECF.
• Sodium pump is operating in all the cells. Mechanism is ATP
dependent.

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3. Functions:
I. Fluid balance- maintains crystalloid OP of ICF and ECF
II. Along with other cations Na+ also involved in neuromuscular
irritability (α) which is given below
α = [K+][Na+]
[Ca2+][Mg2+][H+]
III. Acid base balance- by Na+ and H+ exchange in renal tubule to acidify
urine
IV. Maintenance of viscosity of blood- both Na+ and K+ regulate the
degree of hydration of plasma proteins
V. Role in action potential- local depolarization of nerve or muscle
fiber .

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4. Hypernatremia: means ECF Na is excessive relative to water
Causes-
• simple dehydration
• Diabetes incipidus (lack of ADH)
• Excessive Na intake (for treatment purpose)
• Steroid therapy (mineralocorticoids increase)
• Cushing syndrome, Conn’s syndrome (tumors of adrenal gland)

5. Hypotremia:
Causes
• Diuretic medications (act by promoting excretion of sodium by kidney).
Required for diseases eg- hypertension, congestive heart failure, chronic
kidney diseases
• Excessive sweating, Vomiting and diarrhoea
• Kidney diseases
• Addison’s disease
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Potassium
1. Distribution in body
• Whole blood = 200mg/dl
• Plasma = 20mg/dl
• Cells = 440mg/100gm
• Muscle tissue = 750-400mg/100gm
• Nerve tissue = 530mg/100gm
2. functions:
• Influence the muscular activity
• Involved in acid base balance
• Has an important role in cardiac functions
• Certain enzymes like pyruvate kinase requires K+ as cofactor
• Involved in neuromuscular irritability and nerve conduction
process.

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3. Hyperkalemia:
• Due to kidney failure with decreased excretion of potassium
• Sudden release of potassium from the intracellular compartment
In hyperkalemia, there is increase membrane excitability and even minor
increase is life threatening.
4. Hypokalemia:
• Results from loss of potassium ions- prolonged vomiting and severe
diarrhoea and loss of potassium ions in urine
It is manifested as muscular weakness
5. Sources: Rich in potassium but deficient in sodium are banana, apple,
orange, pineapple, potato, beans etc.

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IRON
Total iron content of human body (70 kg)= 2.3gm- 3.8gm (75% in blood)

Hb
Heme
proteins
Myoglobin
Protein
Catalases
Other
essential Cytochromes
proteins
peroxidases
Iron requiring
enzymes

IRON
Ferritin
storage
Haemosiderin
Transport
form

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1. Hb and myoglobin:
• Protein with an iron porphyrin prosthetic group attached to protein
globin
• Most abundant essential iron compounds
2. catalases:
• Heme containing enzymes
• It destroys H2O2, formed in the tissues and molecular oxygen is
evolved in the reaction.
2H2O2 2H2O + O2
3. Peroxidases:
• Plant enzymes found in milk, erythrocytes, leukocytes and lens fibre.
• Its prosthetic group is protoheme loosely bound to apoprotein. eg-
glutathione peroxidase

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4. Cytochromes:
• Organoiron compounds of the body found in mitochondria
5. Iron requiring enzymes:
• Group of enzymes using riboflavin a coenzymes. Eg- xanthine
oxidase, cytochrome, reductase
• Other enzymes use iron as cofactors. Eg- succinate dehydrogenase,
aconitase
• Required for conversion of superoxide radical to free OH - radical
6. Ferritin:
• Storage protein of iron and found in blood, liver, spleen, bone
marrow and intestinal mucosal cells
• Free iron is toxic and catalyze the conversion of O2- radical to OH
free radical
• Iron bound to ferritin is non toxic.
• Bound form is more soluble and iron is present as ‘ferric
oxyhydroxy phosphate’ and is brown in color.
• Upto 4500 Fe3+ atoms are found stored in a ferritin complex.
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7. heamosiderine:
• Derived from ferritin
• Contains larger fraction of its mass as iron than does ferritin
• Seen in state of iron overload or when iron is in excess.
• Iron in haemosiderine is available for formation of Hb but
mobilization of iron is much slower than ferritin.
8. Transferrin:
• Non heme iron binding glycoprotein
• Iron is prothetic group
• Can bind with two atoms of Fe as Fe3+
• Fe2+ has to be oxidised to Fe3+ form, Ceruloplasmin and Ferroxidase
II are required for this conversion.
Functions of transferrin:
• Transport of iron to RE cells, bone marrow to reach the immature
RBCs.
• Within the target cells, iron is released and apotransferrin is
recycled to formLRMnew transferrin.
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 ABSORPTION:
• Around 10- 20 mg% is taken in the diet
• Only about 10% is absorbed
• The only mechanism by which total body stores of iron is regulated
is at the level of absorption
• Garnick proposed “Mucosal Block Theory” for Fe absorption
 MUCOSAL BLOCK THEORY:
• HCl present in gastric juice liberates free Fe3+ from non- heme
proteins.
• Absorption of Fe from lumen into mucosal cells is in Fe2+ form.
• Enterocytes (intestinal mucosal cells) are responsible for Fe
absorption
• Incoming Fe3+ is reduced to Fe2+ by ferrireductase present on the
surface of enterocytes and helped by vit C and glutathione present
in the diet.
• Transfer of Fe2+ from the apical surface of enterocytes into their
interior is performed by a DMT 1- Divalent metal transporter.
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• Once it is inside, it can either be stored as ferritin or it can be transferrred
across the basolateral membrane into the plasma where it is carried bound to
transferrin.
• Passage of Fe2+ across the basolateral membrane is carried out by another
protein IREG-1 (iron regulatory protein 1).
• Most of the Fe2+ required to be absorbed is transferred to plasma by Fe2+
transporter(FP) protein.
• Fe2+ can also come from heme by the action of hemioxidase.
• IREG-1 may interact with the Cu containing protein called hephaestin.
Hephaestin is thought to have a ferroxidase activity which is important in the
release of Fe from cells as Fe3+ . Iron is transported in the plasma as transferrin.
• Normally plasma/ serum transferrin is 33% saturated with iron.
• Iron is transported to bone marrow for heme-synthesis.
• Fe2+ is incorporated in protoporphyrin with the help of enzyme ferrochelatase
• A small amount of Fe released each day from RBC by phagocytosis.
• This released Fe2+ is recycled into new Hb.
• A small amount of Fe is also stored as ferritin.

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FACTORS WHICH AFFECT Fe ABSORPTION:
A. Sources of Fe:
1. Heme iron- comes mainly from animal products and is efficiently
absorbed
2. Non- heme iron- present in plants, though ingested in larger amount
than heme iron. Are inefficiently absorbed.
Heme iron= 20- 30% absorbed
Non heme iron= 1- 5% absorbed
• Dietary factors which increase Fe absorption:
• Vitamin C, Glutathione
• Acidic pH
• Dietary factors which decrease Fe absorption:
• Tea by >60%
• Coffee by >35%
• phytates (found in soya, corn, grains)
• Dietary fibres

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Clinical
aspect

Iron
Iron overload
deficiency

Iron
Iron storage Iron Excessive Parental iron Repeated
deficiency
depletion deficiency absorption therapy transfusion
anaemia

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1. Iron storage depletion:
• S. Ferritin decreases
2. Iron deficiency:
• Iron stores are almost exhausted
• S. Ferritin is low.
• Transferrin saturation decreases
• Hb decreases
3. Iron deficiency anaemia:
• Hb continues to fall
• S. Ferritin shows decrease
• Transferrin saturation continues to fall
• Erythrocyte protoporphyrin increases
Iron overload: they are of two types:
1. Heamochromatosis: Fe overload is associated with injury to cells
2. Haemosiderosis: Fe overload without cell damage

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SELENIUM

• In mammals glutathione peroxidase is se containing enzyme.

• Rbc contain good quantity of glutathione peroxidase.
• Thyroxine is converted to T3 by enzyme containing Se.
• Se acts as antioxidant(complementary to vitamin E)
• Se concentration- In testis is highest ;required for development of
spermatozoa.
• Se toxicity is called selenosis.
• Toxicity symtoms include hair loss,falling of nails,diarrhoea and
weight loss.
• Se is present in metal polishes and anti rust compounds

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MAGNESIUM

• 70% of total Mg content is combined with Ca and P in bones.

• Acts as activator for many phosphate group transfer reactions.
• Also functions as cofactor for oxidative phosphorylation.
BLOOD LEVEL: 1-3mg%
ABSORPTION:
• Upto 50% daily ingested is not absorbed
• PTH increases its absorption.
DEFICIENCY DISEASE: Deficiency causes
• Depression
• Muscular weakness
• Convulsions
• Deficiency has also been observed in chronic alcoholics.
• In Kwashiorkar, S. Mg is low.
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ZINC
• Essential component of enzyme like carbonic anhydrase, ALP etc.
• Required for mobilisation of vitamin A from liver.
• Essential for normal growth and reproduction.
Deficiency:
• In men, its deficiency results in dwarfism and hypogonadism.
• Also causes anaemia.
COBALT
• Essential component of B12
• Certain enzymes which require B12 for their activity , indirectly require Co.

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COPPER
• Has important role in Hb synthesis.
• Required for
• Melanin formation
• PL formation
• Collagen synthesis
• For maintenance and formation of myelin sheath
• Constituent of several enzymes
• Tyrosinase
• Cytochrome oxidase
• Ascorbic acid oxidase
• Uricase
• Ceruloplasmin
• Cu containing proteins are:
• Cerebrocuprein- brain
• Erythrocuprein- RBC
• Heptocuprein- liver
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Fluorine

1. FUNCTIONS:
• In trace quantity essential for development of bone, teeth.
• In combination with vitamin D required for treatment of osteoporosis.
• As NaF used for inhibition of enzyme enolase.
• As fluoroacetate inhibitor of aconitase.
• F ions inhibit metabolism of oral bacterial enzymes and diminish the local
production of acid which is important for formation of dental carries.
• Forms a protective layer of acid resistant fluoroapatite and hydroxyapatite
crytals of enamel.
2. DAILY REQUIREMENT:
• Drinking water contains 1-2 ppm

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3. ABNORMALITIES
• Intake of excessive amount of F (3-5ppm)causes dental fluorosis (molted
enamel)
• Enamel of the teeth looses its luster and becomes rough
• Chalky white patches with yellow or brown staining are found over the
surface of teeth
• Enamel becomes weak.
• Highly excessive amount of fluoride(>10ppm) results in hypercalcification
of the bones of spine, pelvis and limbs.
• In addition the ligaments of spine become calcified and collagen in the
bone is also calcified.
• Neurological disturbances are common.
• Such individuals can not exhibit simple daily task, such as bending.
• Drinking water containing <0.5ppm F causes dental carries in children.
4. PREVENTION OF FLUOROSIS:
• Fluorosis can be prevented by removing fluoride from water by treatment
with activated charcoal or by some other suitable absorbents.
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IODINE

• Required for synthesis of thyroxine and tri-iodothyroxine of thyroid gland.

• SOURCES: Sea water, sea foods
• BLOOD IODINE: normal conc. In plasma=4-10ug/dl
• ABSORPTION: easily absorbed
• STORAGE: 90%stored as thyroglobulin
• DEFICIENCY:
 In adults -thyroid gland is enlarged (goitre)
 in children severe deficiency results in the extreme retardation of growth
known as cretinism.
• GOITROGENIC SUBSTANCES: food such as cabbage, cauliflower etc.
contain 1-5 vinyl 2-iodo oxazolidone which reacts with the iodine present
in the food and make it unavailable to the body.

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THANK YOU

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ASSESSMENT OF STUDENTS FOR LECTURE TOPIC- MINERALS

1. What is normal blood calcium level ? What are the mechanisms by which
Calcium homeostatis is maintained?
2. Write short notes on
a) Ferritin
b) Transferrin
c) Regulation of calcium level
d) Mucosal block theory
e) Iron overload
3. MCQs (Give one correct answer)
I. Normal level of calcium in blood is:
a) 3-4 mg/dL
b) 9-11 mg/dL
c) 4-5 mEq/L
d) 96-106 mEq/L
II. Calcium is required for the following except:
a) Coagulation
b) Absorption of Iron
c) Neuromuscular transmission
d) Enzyme activity LRM 18 I BDS,U.G CURRICULUM-DEPT. OF B
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III. Zinc is present in all enzymes except:
a) ALP
b) Amylase
c) Carbonic anhydrase
d) Carboxypeptidase
IV. Which trace element has antioxidant role?
a) Zn
b) Ca
c) Se
d) Fe
V. Deficiency of which element causes goiter?
e) Zn
f) I
g) Se
h) Fe
VI. Which trace element maintains water and electrolyte balance in body?
i) Na
j) Se
k) Cu
l) Zn
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