Blood Metabolism (Heme synthesis and breakdown)

Introduction to Heme synthesis and Breakdown

Heme synthesis and breakdown

  • Structure of heme
  • Biosynthesis of heme
  • Porphyrias
  • Billirubin metabolism
  • Plasma billirubin
  • Jaundice

Porphyrin, Hemoglobin and Billirubin

  • Porphyrins are a group of compounds formed by the union of four pyrrole rings through methenyl Bridges
  • The porphyrins usually contain a metal ion linked to the nitrogen atoms of the pyrrole rings
  • The biologically important porphyrins are usually conjugated proteins consisting of a  metalloporphyrin linked to a protein
  • Some biologically important compounds containing porphyrins are the following:
    • Haemoglobin
    • Myoglobin
    • Cytochromes
    • Catalase
    • Peroxidase
    • Tryptophan pyrrolase

Haemoglobin

  • In haemoglobin, iron-porphyrin is linked with globin.
  • Haemoglobin is a tetramer made up of four subunits.
  • Each subunit contains a porphyrin nucleus, a ferrous ion and a polypeptide chain
  • Haemoglobin can reversibly combine with oxygen, and plays a vital role in the transport of oxygen in the body

Function of Heme

  • Hb =a conjugated protein
  • Heme = prosthetic group
  • Globin = protein
  • Tetrameric protein with 4 subunits
  • Each subunit a prosthetic heme group and the globin polypeptide 

Each polypeptide chains are usually 2-α and 2-β chains

  • MW Hb== 67,000 Daltons
  • Heme is present in:

   a. Hb

   b. Mb

   c. Cytochromes

   d. Perxidase

   f.  Catalase

   g. Trytophan pyrrolase

   h. Nitric oxide synthase

Haemoglobin structure

  • Normal level of Hb in blood in males is 14-16g/dl and in females ,13-15 g/dl.
  • Normal adult blood contains 97% HbA, about 2%HbA2 and about 1% HbF

Myoglobin

  • Structure similar to that of haemoglobin with the difference that it is a monomer
  • Present in muscles
  • Can reversibly combine with oxygen

Cytochromes

  • Contain iron-porphyrin conjugated to proteins
  • Iron-porphyrin portion is similar to that of haemoglobin.
  • Components of respiratory chain in mitochondria, and transport electrons.
  • Some cytochromes perform other functions as welle.g. microsomal hydroxylation.

Catalase

  • An iron-porphyrin containing enzyme that ispresent mainly in animals Acts on hydrogen peroxide.

Peroxidase

  • This is another iron-porphyrin containing enzyme that acts on hydrogen peroxide It occurs mainly in plants.

Tryptophan pyrrolase

  • Another iron-porphyrin containing enzyme
  • Acts on tryptophan

Chemistry

  • The structural units of porphyrins are pyrrole ring.
The structural units of porphyrins are pyrrole ring
  • Four pyrrole rings combine to form the parent  porphyrin, porphin.
Four pyrrole rings combine to form the parent  porphyrin, porphin.
  • A simple representation of the porphin structure
    has been proposed by Fischer.
Prophin according to Fischer representation
  • The carbon atom numbers 1 to 8 have different substituents attached to them e.g. acetate (A), propionate (P), methyl (M) and vinyl (V)
  • There are two types of porphyrins, porphyrin I and porphyrin III
  • In porphyrin I, the substituent groups are
    attached symmetrically to carbon atoms 1 to 8.
Porphyrin I
  • In porphyrin III, the order of substituent groups is reversed on ring IV.
Phorphyrin III
  • Type III porphyrins are found more commonly than type I
  • The important porphyrins in human beings are uroporphyrins, coproporphyrins and protoporphyrins
  • Uroporphyrins are mostly found in urine, coproporphyrins in faeces and protoporphyrins in blood and tissues
  • Haem is the most abundant protoporphyrin
Heam

Haemoglobin

  • In hemoglobin, iron-porphyrin is linked with globins.
  • Hemoglobin is a tetramer made up of four subunits.
  • Each subunit contains a porphyrin nucleus, a ferrous ion and a polypeptide chain.
  • Hemoglobin can reversibly combine with oxygen, and plays a vital role in the transport of oxygen in the body.

Synthesis

  •  Synthesis of porphyrins begins with the condensation of succinyl CoA, an intermediate of citric acid cycle, with glycine
  •  This reaction is catalysed by δ-amino levulinic acid synthetase (ALA synthetase)

Biosynthesis of  heme

  • Pathway is partly cytoplasmic and partly mitochondria.

1. ALA Synthesis:

  • Synthesis of porphyrins begins with the condensation of succinyl CoA, an intermediate of citric acid cycle, with glycine.
  • This reaction is catalysed by δ-aminolevulinic acid synthetase (ALA synthetase)
ALA Synthesis
  • α-Amino-β-ketoadipic acid is decarboxylated to δ-aminolevulinic acid (ALA).
  • This reaction is catalysed by ALA synthetase in the presence of pyridoxal phosphate (PLP).
ALA Synthesis
  • Two molecules of ALA are condensed to form the first pyrrole compound, porphobilinogen.
  • This reaction is catalysed by ALA dehydrase
ALA Synthesis
  • Different porphyrins are formed from Porphobilinogen.
  • The exact reactions leading to the synthesis of porphyrins are not fully understood.
  • Four porphobilinogen molecules react in the presence of uroporphyrinogen I synthetase to form hydroxymethylbilane.
  • Hydroxymethylbilane spontaneously cyclises to form uroporphyrinogen I, or it can be enzymatically cyclised to uroporphyrinogen III by uroporphyrinogen I synthetase and uroporphyrinogen III cosynthetase.
  • Coproporphyrinogens can be formed from uroporphyrinogens, and protoporphyrinogens from coproporphyrinogens.
Protoporphyrin III
  • Protoporphyrin III is the most abundant and most  important porphyrin
  • Haem is synthesised from proto-porphyrin III in the presence of haem synthetase (ferrochelatase)

    Heme synthetase

  •  Protoporphyrin III + Ferrochelatase -› Heme
  • Haem can combine with different polypeptides to form haemoglobin and other haemoproteins

Regulation

  • The major purpose of porphyrin synthesis is to form haem.
  • The regulatory enzyme in the pathway is ALA synthetase.
  • The regulator is haem itself  Regulation occurs by repression-derepression.
  • When haem is not being utilised, its concentration increases and it combines with an aporepressor to form the repressor.
  • The repressor acts on the ALA synthetase gene and represses the synthesis of ALA synthetase.
  • This decreases the synthesis of porphyrins.

Disorders of Heme Synthesis

PORPHYRIAS

  • Porphyrias are a group of diseases in which large quantities of porphyrins or their precursors are excreted in urine.
  • The abnormal excretion is due to a defect in the synthetic pathway.
  • Absence or deficiency of an enzyme leads to accumulation of the intermediates proximal to the affected enzyme.
  • The urine of the patients is normal in colour when fresh but becomes pink on exposure to light due to oxidation of porphyrinogens
  • Skin photosensitivity is often present
  • Early intermediates bind to nervous tissue, and produce neuropsychiatric abnormalities
  • Thus, a defect early in the pathway is more harmful than a defect in the later steps.
  • Though the defective gene is present in all the tissues, the expression is usually confined to a particular tissue.
  • Depending upon the site of expression of the genetic defect, porphyrias may be divided into hepatic porphyrias and erythropoietic porphyrias.

Hepatic porphyrias include :

  • acute intermittent porphyria
    • porphyria cutanea tarda
    • hereditary coproporphyria
    • variegate porphyria
  • congenital erythropoetic porphyria
  • • protoporphyria

Congenital erythropoietic porphyria

  • Mode of inheritance : Autosomal recessive.
  • Affected enzyme : Uroporphyrinogen III cosynthetase.
  • Site of expression : Erythroid cells.

Acute intermittent porphyria

  • Mode of inheritance : Autosomal dominant
  • Affected enzyme : Uroporphyrinogen I synthetase
  • Site of expression : Liver cells

Porphyria cutanea tarda

  • Mode of inheritance : Autosomal dominant
  • Affected enzyme : Uroporphyrinogen decarboxylase
  • Site of expression : Liver cells

Hereditary coproporphyria

  • Mode of inheritance : Autosomal dominant
  • Affected enzyme : Coproporphyrinogen oxidase
  • Site of expression : Liver cells

Variegate porphyria

  • Mode of inheritance : Autosomal dominant
  • Affected enzyme : Protoporphyrinogen oxidase
  • Site of expression : Liver cells

Protoporphyria

  • Mode of inheritance : Autosomal dominant
  • Affected enzyme : Ferrochelatase (haem synthetase)
  • Site of expression : Liver cells
  • The clinical abnormalities are mainly neurovisceral in hepatic porphyrias and cutaneous in erythropoietic porphyrias
  • However, some overlapping of signs and symptoms is not uncommon

Hepatic Porphyrias

  • Acute attacks of abdominal pain, nausea and   vomiting occur in hepatic porphyrias
  • Overactivity of the sympathetic nervous system produces tachycardia, tremors and hypertension
  • Psychiatric symptoms, e.g. anxiety, insomnia, disorientation and depression, are common
  • Motor neuropathy may cause progressive muscular weakness
  • Seizures can also occur
  • The biochemical basis of neurovisceral

    abnormalities is not known

  • In addition to the neurovisceral signs and symptoms, cutaneous photo-sensitivity of varying degrees is also present in hereditary coproporphyria, variegate porphyria and porphyria cutanea tarda

Erythropoietic Porphyrias

  • Severe cutaneous photosensitivity from a very early age is the hallmark of erythropoietic porphyrias
  • Porphyrin precursors are present in skin, and damage the skin on exposure to sunlight
  • Multiple vesicles erupt on the skin
  • The skin is pigmented and fragile
  • Denuded areas on skin are prone to infections
  • Bones and teeth may be pigmented due to deposition of porphyrin precursors
  • Haemolysis may occur due to binding of porphyrin precursors to haemoglobin
  • In protoporphyria, liver damage also occurs in some patients
  • Cutaneous manifestations are produced by exposure to sunlight
  • The neuro-visceral manifestations are precipitated by :

• Steroids

• Alcohol

• A number of drugs e.g. barbiturates, meprobamate, carbamazepine, mephenytoin,

. sulphonamides, griseofulvin etc

Catabolism

  • When the life-span of erythrocytes is over, they are broken down in the reticuloendothelial cells
  • Haem is removed from globin
  • The end product of heme catabolism are bile pigments

Catabolic pathway of hemoglobin

Catabolic pathway of hemoglobin
  • Bile pigments-Bilirubin and biliverdin
    •   They the breakdown product of heme.
    • They are useless excretory products.
  • Bile salts-are sodium salts of bile acids ( glycocholate and taurocholate) 
    • Products of cholesterol
    • Helps in absorption of fat

Both bile pigments and bile salts are present in the bile.   

1. Generation of Bilirubin

  • The methenyl bridge between ring I and ring II is broken, releasing iron and converting haeminto a green pigment, biliverdin
  • Biliverdin is reduced to yellow-coloured

   bilirubin, which is the major bile pigment in

   human beings

  • Biliverdin is formed from haem by microsomal haem oxygenase system, and bilirubin is formed from biliverdin by biliverdin reductase

2.Transport to liver

  • Bilirubin is released from reticuloendothelial cells into circulation
  •  Since it is insoluble in water, it transported in association with albumin
  • Albumin has two bilirubin-binding sites, a high affinity site and a low-affinity site
  • is first bound to the high-affinity site If the high-affinity sites on all the albumin molecules are saturated, excess billirubin is bound to the low-affinity site
  • At a normal plasma albumin concentration, 20 to 25 mg of billirubin can be bound to the high-affinity sites of the albumin molecules per 100 ml of plasma.
  • Water-insoluble bilirubin released from reticuloendothelial cells is known as unconjugated bilirubin
  • It is taken up by liver cells from the circulating albumin with the help of a carrier-mediated active transport system.

3. Conjugation in liver

  • In hepatic parenchymal cells, bilirubin is

  conjugated with glucuronic acid to make it water soluble

  • The conjugation reaction occurs in two steps
Conjugation in liver
  • The conversion of bilirubin mono-glucuronide into bilirubin diglucuronide may also occur by a trans-esterification reaction between two bilirubin mono-glucuronide molecules
  • This reaction is catalysed by bilirubin-glucuronide glucuronosyl transferase (dismutase)
Conjugation in liver
  • Bilirubin diglucuronide (conjugated bilirubin) is excreted into the intestine through bile
  • Excretion of conjugated bilirubin by hepatic cells into biliary canaliculi takes place by an active transport mechanism
  • In the large intestine, bilirubin is free from glucuronic acid, and is reduced to uro-Bilinogen by the enzymes of intestinal bacteria

4. Excretion of bilirubin to bile

– A small portion is reabsorbed into portal circulation, and is taken to liver which re-excretes

  • Most of it into the intestine (enterohepatic circulation of urobilinogen)
  • A very small amount of urobilinogen enters the systemic circulation, and is excreted by the kidneys in urine. Most of the urobilinogen is excreted in the faeces

JAUNDICE

  • erum bilirubin concentration (total) ranges from 0.2 – 1.0 mg/dl
  • This includes :

  • Conjugated bilirubin

  • Unconjugated bilirubin

  • This enters the circulation from the reticuloendothelial cells
  • The concentration of conjugated bilirubin in serum ranges from 0.1 – 0.4 mg/dl
  • This enters the circulation from liver after it has been conjugated
  • The concentration of un-conjugated bilirubin in serum is 0.1- 0.6 mg/dl
  • Conjugated bilirubin is also known as direct reacting bilirubin because, being water-soluble,
  • it can directly react with Ehrlich’s diazo reagent without the addition of an organic solvent
  • Un-conjugated bilirubin is known as indirect
  • reacting bilirubin because, being water insoluble,
  • it reacts with Ehrlich’s diazo reagent only after addition of methanol or ethanol
  • When serum bilirubin concentration rises above normal (hyperbilirubinaemia), bilirubin gets deposited in tissues which are stained yellow.
  • This is known as jaundice.
  • The yellow staining can be seen in skin and mucous membranes but is most clearly visible in the sclera.
  • Jaundice can occur in a number of diseases
  • Depending upon the site of the disease, jaundice can be divided into three types:
  • 1. Pre-hepatic jaundice
  • 2. Hepatic jaundice
  • 3. Post-hepatic jaundice

Pre-hepatic Jaundice

  • This is also known as hemolytic jaundice
  • It is due to an increased rate of haemolysis
  • As the rate of breakdown of haemoglobin increases, bilirubin is formed in such large
  • quantities that the capacity of the liver cells to take up, conjugate and excrete it is exceeded.
  • The concentration of unconjugated bilirubin in serum rises and jaundice results
  • Since unconjugated bilirubin can not be excreted by the kidneys, urine does not contain bilirubin
  • As the rate of formation of bilirubin is increased, the rate of formation of urobilinogen is also increased, and urinary excretion of urobilinogen is raised.
  • A common cause of haemolytic jaundice is the
  • “physiological jaundice of neonates”
  • This occurs in some neonates between the third
  • and tenth days of life
  • Erythrocytes formed during foetal life containing
  • foetal haemoglobin are rapidly destroyed after
  • birth
  • The rate of formation of bilirubin is increased
  • As the hepatic conjugating system is not fully
  • developed in the first two weeks of life,
  • unconjugated bilirubin accumulates in blood
  • causing jaundice
  • This, however, is a transient and benign condition
  • Haemolytic jaundice can occur in several other
  • haemolytic diseases, the most serious of which is erythroblastosis foetalis or “haemolytic disease of the newborns”
  • This occurs when an Rh-negative mother conceives an Rh-positive baby
  • The Rh-antigen can be transferred across the placenta from the foetus to the mother
  • The maternal system starts forming Rh-antibodies which can be transferred across the placenta to the foetus
  • The resulting Rh-incompatibility in the foetus causes severe haemolysis and unconjugated hyperbilirubinaemia
  • The baby is born with jaundice
  • If serum bilirubin (unconjugated) exceeds 20-25
  • mg/dl, the excess bilirubin is attached to the lowaffinity
  • site of albumin which is off- loaded in the
  • central nervous system as the lipids of the
  • nervous tissue can easily take up nonpolar
  • bilirubin from the low-affinity site of albumin
  • In the central nervous system, bilirubin is attached to basal ganglia, hippocampus, cerebellum, medulla etc
  • These tissues are stained yellow (kernicterus)
  • Kernicterus is often fatal, and leaves behind permanent neurological damage if the patient survives

Hepatic Jaundice

  • This is due to rapid destruction of liver cells as in viral hepatitis and on exposure to hepatotoxic drugs and chemicals
  • It is also known as hepatocellular jaundice
  • As the liver cells are destroyed, the capacity of the liver to take up, conjugate and excrete bilirubin is decreased
  • The concentration of unconjugated bilirubin in
  • serum rises even though the rate of formation of
  • bilirubin is normal
  • In viral hepatitis, the surviving liver cells are
  • inflammed and swollen, and compress the biliary
  • canaliculi
  • This intraheptatic obstruction leads to
  • regurgitation of conjugated bilirubin into systemic
  • circulation
  • The concentration of conjugated bilirubin in serum
  • is raised, and as it is water-soluble, it is excreted
  • in urine
  • Thus, both unconjugated and conjugated bilirubin
  • are raised in serum, and bilirubin is present in
  • urine in viral hepatitis
  • Urinary urobilinogen is usually normal

Post-hepatic Jaundice

  • This is also known as obstructive jaundice as it is caused by an obstruction to the flow of bile
  • The obstruction may be intrahepatic or extrahepatic
  • The commonest cause of biliary obstruction is the presence of gall stones in the biliary passage
  • The obstruction may also be due to compression
  • of biliary channels by tumours e.g. cancer of the
  • head of pancreas
  • Rarely, atresia or stricture of biliary channels may
  • cause obstruction
  • As the flow of bile is obstructed, bilirubin which
  • has been conjugated in the liver cells cannot be
  • excreted into the intestine
  • Conjugated bilirubin is regurgitated into
  • circulation
  • As it is water-soluble, it is excreted in urine
  • Since bilirubin can not reach the intestine,
  • formation of urobilinogen is stopped and
  • urobilinogen is absent from urine
  • Therefore, the characteristic biochemical features
  • of obstructive jaundice are a rise in the
  • concentration of conjugated bilirubin in serum,
  • presence of bilirubin in urine and absence of
  • urobilinogen from urine
  • Jaundice also occurs in the following inherited
  • disorders of bilirubin metabolism:
    • 1. Gilbert’s syndrome
    • 2. Crigler-Najjar syndrome
    • 3. Lucey-Driscoll syndrome
    • 4. Rotor’s syndrome
    • 5. Dubin-Johnson syndrome

Gilbert’s syndrome

  • This is a group of disorders in which the active transport system for hepatic uptake of circulating bilirubin is defective
  • The bilirubin UDP-glucuronyl transferase activity  in liver cells is also sub-normal
  • The concentration of unconjugated biliburin is raised in serum
  • The inheritance is autosomal dominant

Crigler-Najjar syndrome

  • This is an autosomal recessive disorder
  • Two types have been recognised
  • In type I, hepatic bilirubin UDP-glucuronyl transferase activity is absent
  • Unconjugated bilirubin is greatly elevated in serum, kernicterus is common and the disease is often fatal.
  • In type II, hepatic bilirubin UDP-glucuronyl transferase activity is decreased
  • There is unconjugated hyperbilirubinaemia but it is not as severe as in Crigler-Najjar syndrome, type I

Lucey-Driscoll syndrome

  • An inhibitor of bilirubin UDP-glucuronyl transferase, believed to be a progestational steroid, is present in the plasma of patients withLucey-Driscoll syndrome
  • This causes unconjugated hyperbilirubinaemia

Rotor’s syndrome

  • The active transport system, responsible for excretion of conjugated bilirubin in bile, is defective in Rotor’s syndrome
  • This leads to conjugated hyperbilirubinaemia
  • The inheritance is autosomal recessive

Dubin-Johnson syndrome

  • The nature of the defect is similar to that in Rotor’s syndrome
  • In addition, a black pigment, probably melanin, is deposited in liver
  • The concentration of conjugated bilirubin in plasma is raised
  • The inheritance is autosomal recessive

Other Biochemistry Notes :-

Carbohydrate Metabolism

VITAMIN PYRIDOXINE AND BIOTIN

Vitamin A

VITAMIN D

Pyrimidine metabolism

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