CELL ORGANELLES, MARKERS

AND DISORDERS

PRESENTED BY:- MODERATOR:-

DR ASWINI KUMAR SWAIN PROF(DR) SUBHASHREE RAY
1ST YEAR POSTGRADUATE STUDENT PROFESSOR AND HOD
DEPARTMENT OF BIOCHEMISTRY
DEPARTMENT OF BIOCHEMISTRY
IMS AND SUM HOSPITAL BHUBANESWAR
 INTRODUCTION
• Cell – structural and functional unit of all living organisms, including humans.

• Two types: Prokaryotic and Eukaryotic

• Cell organelles –Special structural components of the cell suspended in cytoplasm.

Classified into three categories based on the presence or absence of the membrane:-

o Organelles without membrane:- Ribosomes and Cytoskeleton [found both in Prokaryotic

cell and Eukaryotic cell]

o Single membrane-bound organelles:- Vacuole, Lysosome, Golgi apparatus, Endoplasmic

reticulum [present only in Eukaryotic cell]

o Double membrane-bound organelles:- Mitochondria and Nucleus [present only in

CRITERIA PROKARYOTIC CELL EUKARYOTIC CELL
SIZE 0.1-10 μm 10-100 μm
CELL TYPE Unicellular Multicellular
CELL WALL Tough cell wall Thin plasma membrane
CYTOPLASM No cytoskeleton Cytoskeleton exists
NUCLEUS AND HISTONES Does not have nucleus and histones Prominent membrane-bound nucleus in the
centre with histones
DNA DNA is circular DNA is linear (chromosomes)
ORGANELLES Absent Present
LYSOSOMES AND Absent Present
PEROXISOMES
MITOCHONDRIA Absent Present
RIBOSOMES 70S (30S + 50S) 80S (40S + 60S)
CELL DIVISION AND Quick, 20 min; Asexual; Binary fission Slow, hours; Sexual reproduction; Mitosis and
REPRODUCTION meiosis
GENOME Haploid genome Diploid genome
EXAMPLES Includes Bacteria, Blue-green algae and Includes animals, plants, Fungi and Protozoa
Archaea
PROKARYOTIC CELL EUKARYOTIC CELL
 CYTOPLASM
• Cytoplasm is the fluid known as cytosol, the jelly-like substance present inside the cell
extending from the cell membrane to the nucleus within the cell.

• Mainly composed of water along with proteins, carbohydrates, lipids, and electrolytes.

• Cell organelles are embedded in the cytoplasm.

• These cell organelles contain enzymes, mainly responsible for controlling all metabolic
activities and chemical reactions within a cell.

• Cytosol is the site of glycolysis, HMP pathway, and Denovo synthesis of fatty acids.

FUNCTION:- Site for glycolysis, HMP shunt pathway, fatty acid synthesis, few steps
of Gluconeogenesis, Urea cycle, and Haem synthesis.
 NUCLEUS
• Nucleus – the storehouse of the cell’s DNA is a
double-membraned organelle, spherical in shape,
located at the centre of the cell in all eukaryotic cells
[ except for mature RBCs in circulation]

• Comprises nuclear membranes, nucleolus, nuclear

matrix, nuclear lamina and chromatin.

• Surrounded by nuclear membrane enveloping

nucleoplasm.

• Nuclear membrane is double layer, an inner and an

outer membrane, arranged parallel to one another and
separated by 10-50 nm.
STRUCTURE OF NUCLEUS
CONTINUING
• Outer nuclear membrane is continuous with the membrane of endoplasmic reticulum, and the
inner membrane called as perinuclear membrane has numerous pores called nuclear pores
(made up of multiple proteins called nucleoporins).

• Nucleus contains nucleoplasm (karyoplasm), a gel-like ground substance that contains genetic
material DNA in combination with protein Histones.

• Comprises enzymes that are involved in the synthesis of DNA (DNA replication) and RNA
(Transcription).

• Within the nucleus, there are tiny spherical dense bodies called nucleolus which has role in the
modification of immature RNAs into mature RNAs.

• Nuclear lamina is a dense fibrillar network associated with inner face of inner nuclear
membrane.
CONTINUING

• It is composed of intermediate filaments called Lamins A, B, C and Lamin associated

membrane proteins.

FUNCTION:-
• Along with mechanical support, nuclear lamina regulates DNA replication, cell division, and
chromatin condensation to chromosomes during mitosis.

• Nucleus is responsible for cell division, growth and differentiation.

• Controls main cellular metabolism through controlling synthesis of particular enzymes.

• Allows levels of gene regulation and controls gene expression.

 MITOCHONDRIA
• Known as the Powerhouse of the cell because
they are the sites of aerobic respiration in the cell,
where energy released from the oxidation of
foodstuffs is trapped as chemical energy in the
form of ATP.

• Double membrane-bound, sausage-shaped

organelle found in all eukaryotic cells.

• A cell consists of around 2000 mitochondria,

occupying about 1/5th of the total cell volume.

• Usually vary in their size in their size having a

diameter between 0.5 and 1.0 μm and length up to STRUCTURE OF MITOCHONDRIA
7 μm.
CONTINUING

• RBCs do not contain mitochondria, whereas the tail of spermatozoa is fully packed with
mitochondria.

• The double membrane divides its lumen into two distinct aqueous compartments.

• The inner compartment is called the matrix, which is folded into cristae, whereas the outer
membrane forms a continuous boundary with the cytoplasm.

• Mitochondria have their own circular DNA, RNA molecules, ribosomes (the 70S) and few other
molecules that help in protein synthesis.

• Mitochondria DNA is double-stranded, highly coiled circular DNA; it has about 16,569
nucleotides.

• The mitochondrial proteins encoded by nuclear DNA are synthesized in the cytoplasm and
translocated into mitochondria by TOM ( Translocase of outer membrane) and TIM ( Translocase
CONTINUING
FUNCTION:-
• The most prominent role of mitochondria is to produce the energy currency of the cell- ATP
through electron transport chain and oxidative phosphorylation.

• TCA cycle, Oxidation of fatty acids, few steps of urea cycle and Haem synthesis takes place in
matrix of mitochondria.

• The mtDNA has information for synthesis of 2 rRNAs, 22 tRNAs and 13 proteins which are
components of electron transport chain(ETC).

• The inner mitochondrial membrane contains Cytochrome P-450, which is involved in

steroidogenesis.

• The antioxidant enzyme superoxide dismutase (SOD) is present in mitochondria.

 LYSOSOMES
• Lysosomes are single membrane-bound subcellular organelles.

• They are spherical vesicles that contain hydrolytic enzymes that

can break down many kinds of biomolecules.

• The lysosomal enzymes act only locally, but if the lysosomal

membrane is disrupted, the enzymes can cause autolysis of cell
constituent, hence known as suicide bags.

• The pH inside lysosomes is acidic (pH 5) and most enzymes are

acid hydrolases.
STRUCTURE OF LYSOSOME

• The lysosomes contain around 40 enzymes , which digest and

remove the unwanted metabolic waste substances.

• The hydrolysed products are utilized by the cell.

CONTINUING
• Enzymes of the lysosomes, synthesised in the rough endoplasmic reticulum, are transported to
Golgi apparatus in small vesicles and they are specifically tagged with mannose-6-phosphate, so
that they are properly sorted and transported to lysosomes.

• Synthesis of lysosomal enzymes is controlled by nuclear genes.

• Mutations in the genes for these enzymes are responsible for more than 30 different human
genetics disorders, which are collectively knowns as lysosomal storage diseases.

• Lysosomes act as the waste disposal system of the cell by digesting worn out organelles, food
particles through autophagy and engulfed viruses or bacteria by endocytosis.

• Endocytic vesicles and phagosomes fuse with the lysosome (primary) to form the secondary
lysosome or digestive vacuole.

• Lysosomes can help to self-destruct in a process called programmed cell death or apoptosis.
CONTINUING
LYSOSOMAL ENZYMES
SL. TYPES OF LYSOSOMAL ENZYMES EXAMPLES
NO.
1 Phosphatases Acid phosphatases
Acid phosphodiesterase
2 Glycosidases β-Glucosidase
β-Glucuronidase
β-Galactosidase
α-Glucosidase
α-Mannosidase
α-Fucosidase
β-N-Acetyl glucosaminidase
Hyaluronidase, Aryl
Sulphatse
Lysozyme

3 Proteases Cathepsin A, Cathepsin B,

Collagenase, Peptidase, Elastase
4 Lipases Acid lipase, Phospholipase A,
Fatty acyl esterase, Phosphatidic acid
phosphatase
5 Nucleases Acid ribonuclease, Acid deoxyribonuclease
LYSOSOMAL ENZYMES AND THE SUBSTRATE THEY DIGEST
ENZYME SUBSTANCE DIGESTED
α-Glucosidase Glycogen
Hyaluronidase Hyaluronic acid
Lysozyme Bacterial cell wall
Peptidases Peptides
Collagenase Collagen
Lipase Triacylglycerols
Phospholipase Phospholipids

 FUNCTION OF LYSOSOMES:-
• Contains hydrolytic enzymes

• Digests macromolecules

• Foreign substances and worn-out organelles.

 PEROXISOMES

• Peroxisomes are tiny spherical membrane-

bound organelles with granular matrix
occurring in the cytoplasm of eukaryotic
cells.

• Synthesized from rough endoplasmic

reticulum.

• Prominently present in leukocytes and

platelets.

• Peroxisomal disorders are a group of STRUCTURE OF PEROXISOMES

hereditary metabolic disorders that occur
when peroxisomes are missing or do not
function correctly in the body.
CONTINUING

FUNCTION:-
• Peroxisomes are involved in the catabolism of very long chain fatty acids, branched chain fatty
acids, and bile acid intermediates.

• They also contribute to the biosynthesis of membrane lipids known as plasmalogens.

• They transfer hydrogen from compounds to oxygen to create hydrogen peroxide (H2O2) and
then convert hydrogen peroxide into water.

• They contain peroxidase and catalase enzymes with an important role in detoxification.

• Catalase breaks down highly toxic hydrogen peroxide to water and oxygen.

• Peroxisomes of the liver detoxify alcohol and poisons by oxidation.

 CENTROSOME AND CENTRIOLE
• Centrosome is an organelle that serves as the main
microtubule organizing centre (MTOC) of the animal cell
and a regulator of cell-cycle progression.

• Found within the cytoplasm of cells, close to the nucleus,

and involved in cell division.

• Centrosomes are composed of two centrioles- a daughter

centriole and a mother centriole, linked together by
interconnecting fibres.

• They are arranged at right angles to each other and

surrounded by an amorphous mass of protein termed the
pericentriolar material (PCM). DIAGRAM OF THE ROLE OF
CENTROSOME DURING CELL
• Each centriole is a cylindrical array of nine microtubules. DIVISION
CONTINUING
• The cell cycle consists of G1, S, G2, Mitotic phase.

• Mitotic phase includes prophase, metaphase, anaphase and telophase.

• The centrosome replicates once during the S phase of the cell cycle.

• During the prophase of mitosis, the centrosomes migrate to opposite poles of the cell.

• During metaphase, the mitotic spindles are formed between the two centrosomes.

• These spindle fibres help to separate the chromosomes.

• Aberrant numbers of centrosomes in a cell have been associated with cancer.

FUNCTION:- Helps in formation of spindle fibres that separate the chromosomes during cell
 VACUOLES
• Vacuole – defined as a storage bubble in cells.

• Store food or any variety of nutrients a cell might need

to survive.

• Store waste products so that the rest of the cell is

protected from contamination.

• Eventually, those waste products are sent out of cell.

FUNCTION:- Storage of wastes and other

materials. STRUCTURE OF VACUOLES
 ENDOPLASMIC RETICULUM (ER)
• ER- a single-membrane bound organelle found in all
eukaryotic cells.

• Constitutes 30-60 % of the cell that extends through the

cytoplasm connecting cell membrane to the nuclear
membrane.

• It is an interconnected network of flattened, membrane-

enclosed sacs or tubular structures known as cisternae
filled with fluid that is different from the fluid in the
cytosol.

• During cell fractionation, the ER is disrupted and

automatically reassembles to form microsomes.
STRUCTURE OF
ENDOPLASMIC RETICULUM
• Types:- Rough Endoplasmic reticulum and Smooth
 ROUGH ENDOPLASMIC RETICULUM
• Rough endoplasmic reticulum (RER) has dense granular ribosomes lining its surface giving
the rough surface.

• It lies immediately adjacent to the cell nucleus, and its membrane is continuous with the outer
membrane of the nuclear envelope.

• The ribosomes on rough ER are the site of protein biosynthesis.

• The signal sequence on the protein synthesised directs them into the ER for processing.

• Proteins synthesised by the rough ER have specific final destinations.

• Some proteins, for example, remain within the ER, whereas others are sent to the Golgi
apparatus, which lies next to the ER.
CONTINUING

• From the Golgi apparatus, the proteins are directed to lysosomes or to the cell membrane and
secreted to the cell exterior.

FUNCTION:-
• Ribosomes attached to RER synthesis proteins go into the lumen of RER, where the proteins
are further modified.

• RER also helps in the folding of proteins, leading to their fully active form.

• RER acts as a channel to transport the proteins to the nucleus, to the cell, and outside the cell.
CONTINUING
SMOOTH ENDOPLASMIC RETICULUM

• Smooth endoplasmic reticulum (SER) is smooth in appearance without the ribosomes lining.
FUNCTION:-

• Acts as a storage organelle.

• Involved in the synthesis of lipids, including cholesterol and phospholipids, which are used

in the production of new cellular membrane.

• In certain cell types, smooth ER plays an important role in the synthesis of steroid hormones

from cholesterol.

• Supplies calcium for cellular functions.

• In cells of the liver, it contributes to the detoxification of drugs and harmful chemicals
 RIBOSOMES

• Small granular structures made up of 2/3 rd of RNA

and 1/3rd of protein.

• Non-membrane-bound and important cytoplasmic

organelles found in close association with the
endoplasmic reticulum (ER) to form rough ER,
where protein synthesis takes place.

• Free ribosomes are involved in the synthesis of

intracellular proteins.

• Named as the 70S (found in prokaryotes) or 80S

(found in eukaryotes).
STRUCTURE OF RIBOSOMAL
SUBUNIT
• “S” refers to the density and the size, known as
CONTINUING

• Composed of two subunits- small and large subunits (70S has 30S and 50S subunits; 80S has
40S and 60S subunits).

• The two subunits are joined to each other by interactions between the rRNAs in one subunit
and proteins in the other subunit.

• Small ribosomal subunits read the mRNA and the large ribosomal subunit form polypeptide
chains from amino acids.

FUNCTION:-
• Part of rough ER.

• Site of protein synthesis.

 GOLGI APPARATUS

• Coined by Italian cytologist Camillo Golgi in 1897.

• In most eukaryotic cells, Golgi body is present in all

cells except RBC.

• Located in the cytoplasm next to the endoplasmic

reticulum and near the cell nucleus.

• It is a single membrane-bound organelle has 8-10

broad flattened membranous stacked pouches called
cisternae.

• They are arranged in parallel, semi-circular array held STRUCTURE OF GOLGI APPARATUS
together by matrix proteins, and the whole of the Golgi
apparatus is supported by cytoplasmic microtubules.
CONTINUING
• It has three primary compartments, known as “cis” cisternae, nearest to the endoplasmic
reticulum, “medial” central layers of cisternae, and “trans” cisternae, farthest from the
endoplasmic reticulum.

FUNCTION:-
• Golgi apparatus is responsible for glycosylation i.e., addition of carbohydrate units to newly
synthesised proteins.

• It is responsible for the secretion of glycosylated proteins to lysosomes, secretory vesicles or

the the cell surface.

• It is also involved in the transport of lipids.

 CELL CYTOSKELETON

• All these cellular functions are carried out by a

meshwork of filamentous structures forming
cytoskeleton.

• Present in the cell cytoplasm, under the plasma

membrane, in cilia, axons, dendrites, etc.

• Consists of three types of filaments:-

o Actin filaments

o Microtubules

o Intermediate filaments DIAGRAM OF CYTOSKELETON

 F-ACTIN FILAMENTS

• Non-muscle cells contain F-actin filaments

consisting of a double-helical molecule made up of
two G-actin molecules.

• F-actin filaments assemble to form microfilaments

of 7-9.5 nm diameter.

• These exist as prominent bundles below the plasma

membrane.

• Often, they are referred to as stress fibres. DIAGRAM OF ACTIN FILAMENT

• During cancer stress fibres disappear.

 MICROTUBULES

• Microtubules are cylindrical structures consisting of

longitudinally arranged protofilaments.
• Each protofilament consists of α- and β- tubulin
proteins.
• They are present in mitotic spindles, cilia, axons,
dendrites, etc., and take part in their functions.
• These are also involved in the movement of vesicles
during endocytosis and exocytosis.
• Tubulin also tracks and guides the motor protein
kinesin and Dynein.
• Kinesin moves toward the positive side of
microtubules, and dynein moves toward the minus
end of microtubules. STRUCTURE OF DYNEIN AND
KINESIN WITH MICROTUBULE
 INTERMEDIATE FILAMENTS
• These are of intermediate size (8-10 nm) between microfilament (average 6 nm) and microtubule
(23 nm).

• More than 50 different intermediate filament proteins have been identified and classified into six
groups based on similarities between their amino acid sequences:-
 Types I and II: Acidic Keratin and Basic Keratin, respectively; found in epithelial cells, hair and
nails
 Type III
Vimentin found in Fibroblasts, white blood cells and other cell types
Desmin in muscle cells.
Glial fibrillary acidic protein in Glial cells that surround the neurons.
Peripherin in peripheral neurons (most prominently in the long axons of these cells).
 Type IV: Neurofilament H (heavy), M (medium) and L (Low) in neurons.
 Type V: Lamins found in nuclear lamina of all cell types.
 Type VI: Nestin found in stem cells of central nervous system.
DIFFERENT ORGANELLES AND THEIR SPECIFIC MARKER ENZYMES

SUBCELLULAR ORGANELLE MARKER ENZYMES

Plasma membrane 5’-Nucleotidase, Adenylcyclase, Na+-K+ ATPase
Cytoplasm Lactase dehydrogenase
Nucleus DNA polymerase, RNA polymerase, Lamin A & C
Microsome Glucose-6-phosphatase, Alpha glucosidase
(Endoplasmic reticulum)
Golgi complex Galactosyl transferase
Mitochondria ATP synthase, Succinate dehydrogenase, Cytochrome C
 Inner membrane Monoamino oxidase, Citrate synthase
 Outer membrane
 Matrix
Lysosomes Cathepsin, Acid phosphatase
Peroxisomes Catalase
 DISORDERS DUE TO MALFUNCTION OF THE
ENDOPLASMIC RETICULUM (ER)

• Proteins synthesized in the endoplasmic reticulum (ER) are properly folded with the assistance of
ER chaperones.

• Misfolded proteins are disposed of by ER-associated protein degradation (ERAD).

• When the amount of unfolded protein exceeds the folding capacity of the ER, human cells
activate a defence mechanism called the ER stress response, which induces expression of ER
chaperones and ERAD components and transiently decreases protein synthesis to decrease the
burden on the ER.

• A malfunction of the ER stress response caused by ageing, genetic mutations or environmental

factors can result in various diseases collectively known as conformational diseases’ such as
diabetes , inflammation and neurological disorders, including cerebral ischaemia, sleep apnoea,
Alzheimer’s disease, multiple sclerosis, amyotropic lateral sclerosis, the prion diseases and
 DISORDERS OF RIBOSOMES
• Mutations in some of the proteins that make ribosomes, cause “ribosomopathies”.

• These disorders are characterized by bone marrow failure and anaemia early in life, followed by
elevated cancer risk in middle age, e.g., Treacher-Collins Syndrome (TCS), Diamond-Blackfan
anaemia (DBA), Schwachman-Diamond syndrome (SDS), X-linked dyskeratosis congenita
(DKC), cartilage hair hypoplasia (CHH).

 TREACHER-COLLINS SYNDROME:
• Mutations in TCOF1 gene reduce the production of rRNA, which triggers apoptosis of certain
cells involved in the development of facial bones and tissues.

• It is characterized by deformities of the ears, eyes, cheekbones and chin.

• Patients with Diamond-Blackfan anaemia present with macrocytic anaemia and skeletal
 DISORDERS OF GOLGI APPARATUS
• Golgi disorders might result in a malfunction of the secretory pathways, which package and
secrete proteins synthesized in the rough endoplasmic reticulum.

ACHONDROGENESIS:-

• Achondrogenesis is a type of disorder caused by a defect in the microtubules of the Golgi

apparatus.

• It includes congenital chondrodysplasia, malformation of bones and cartilage.

• These conditions are characterized by a small body, short limbs, with other skeletal
abnormalities.
CONTINUING

DUCHENNE MUSCULAR DYSTROPHY:-

• Duchenne muscular dystrophy (DMD) is caused by a mutation of the gene coding for
Dystropin, a protein that links dystrophin-associated protein complex in the sarcolemma to
the actin cytoskeleton.

• There is also a decreased number of Golgi and defective Golgi-mediated glycosylation.

• It is a progressive form of muscular dystrophy causing weakness and atrophy of skeletal and
heart muscles.
 DISORDERS OF LYSOSOMES
• Lysosomal enzymes synthesized in the endoplasmic reticulum (ER) are transported to the
Golgi apparatus, for processing.

• Enzymes are tagged for lysosomes by the addition of mannose-6-phosphate label, which
serves as a marker for proteins to be targeted to lysosomes.

• Without mannose-6-phosphate (target to the lysosomes), the enzymes are erroneously

transported from the Golgi to the extracellular space instead of to lysosomes, affecting its
normal function.

• Lysosomes cannot degrade complex carbohydrates and fats, leading to their accumulation.

• Accumulations of complex molecules are related to several neurodegenerative disorders,

cancers, cardiovascular diseases and ageing-related diseases.
CONTINUING
• Some of the most common lysosomal storage disorders include Tay-Sachs disease, Pompe
Disease, Inclusion-cell (I-cell) disease, Niemann-Pick disease type C, Gaucher disease, Fabry
disease.

I-CELL DISEASE:-
• Inclusion-cell (I-cell) disease is a lysosomal storage disease [also referred as mucolipidosis II
(ML II)].

• It is an autosomal recessive disorder caused due to deficiency of enzyme N-acetylglucosamine

Phosphotransferase.

• The enzyme not being labeled with mannose-6-phosphate is not targeted to lysosomes.

• Lysosomes cannot breakdown substances like oligosaccharides, lipids, and glycosaminoglycans

in various tissues throughout the body (i.e., fibroblasts).
CONTINUING

• As they are not degraded, they are accumulated in lysosomes, resulting in the characteristic I-
cells, or “inclusion cells,” seen microscopically.

• The defective lysosomal enzymes are normally found only within lysosomes are instead found
in high concentrations in blood.

• Children with ML II usually have hepatomegaly or splenomegaly, stiff claw-shaped hands and
fail to grow and develop in the first months of life.

• There is a recurrent respiratory tract infection, including pneumonia.

• They generally die before their seventh year of life, often as a result of congestive heart failure
or recurrent respiratory tract infection.
 CLINICAL APPLICATION OF LYSOSOMES
 CANCER METASTASIS:
• Cathepsins, the lysosomal proteases are implicated in cancer metastasis.
• As some cancer cells liberate cathepsins out of the cell, collagen and elastin are hydrolyzed,
degrading the basal lamina.
• In this way, cancer cells travel to distant organs, leading to metastasis.

 ARTHRITIS IN GOUT:
• The urate crystals deposited in knee joints are phagocytosed forming secondary lysosomes.
• This causes rupture of the lysosome, releasing the lysosomal enzymes causing inflammation
and arthritis.

 POST-MORTEM AUTOLYSIS:
• Post-mortem autolysis is also due to lysosomal rupture and release of enzymes following cell
CONTINUING

 SILICOSIS:
• Inhaled silica particles are phagocytosed and fuse with lysosomes, forming secondary
lysosomes.
• This causes a rupture of the lysosome, releasing the enzymes.
• This causes fibrosis of the lungs

DISORDERS OF PEROXISOMES

• Peroxisomes are oxidative organelles that have a role in detoxification.

• Disorders in Peroxisomes are Zellweger syndrome, Infantile Refsum’s disease, Neonatal

adrenoleukodystrophy, and Hyperoxaluria.
 ZELLWEGER SYNDROME
• Zellweger syndrome is a rare congenital autosomal recessive disorder caused by mutations in
genes that encode peroxins, proteins required for the normal assembly of peroxisomes.

• It is characterized by the reduction or absence of functional peroxisomes in the cells of an

individual.

• This results in the accumulation of very long-chain fatty acids (VLCFA) and branched-chain
fatty acids (BCFA) in the cells that are normally degraded in peroxisomes.

INFANTILE REFSUM’S DISEASE(IRD):

• Zellweger spectrum of peroxisome biogenesis disorders (PBD-ZSD) include Infantile
Refsum’s Disease, Zellweger syndrome (ZS), and neonatal adrenoleukodystrophy (NALD).

• Although they share a similar molecular basis for disease, Infantile Refsum’s disease is less
severe than Zellweger syndrome.
HYPEROXALURIA:
• Hyperoxaluria is an inherited genetic disorder due to the mislocalization of
the peroxisomal enzyme Alanine-glyoxylate aminotransferase (AGT) to
the mitochondria.

• Primary hyperoxaluria is a rare condition characterized by excessive urinary

excretion of oxalate.

• It manifests as recurrent kidney and bladder stones.

MITOCHONDRIAL DISORDERS

• Mutation in mtDNA may result in multisystem syndromes known as mitochondrial diseases,

affecting predominantly tissues that require high levels of ATP, such as skeletal muscle
(mitochondrial myopathies), resulting in muscular and neurological problems.
CONTINUING
LEIGH’S DISEASE:

• Leigh’s disease can be caused by mutations in mitochondrial DNA affecting the production of
cytochrome oxidase.

• It is a severe neurological disorder that usually becomes apparent in the first year of life and
typically results in death within 2-3 years, usually due to respiratory failure.

PEARSON SYNDROME:

• Pearson syndrome is due to deletion of part of mitochondrial DNA, characterized by

sideroblastic anaemia, failure to thrive, pancreatic fibrosis with insulin-dependent diabetes and
 FANCONI SYNDROME:

• Fanconi syndrome is a rare disorder of the kidney tubule, which affects the
reabsorption of glucose and electrolytes, leading to electrolyte imbalance.

• This disorder results in the excretion of excess amounts of glucose, bicarbonate,

phosphates, uric acid, potassium, and certain amino acids in the urine.
 SUMMARY
• Marker enzymes are present only in particular organelles and identify them during cell fractionation.
• Nucleus is the storehouse of genetic information containing DNA organized into 23 pairs of
chromosomes.
• All cells in the body contain a nucleus except mature erythrocytes.
• Endoplasmic reticulum, a network of interconnecting membranes is the site of protein synthesis
(rough endoplasmic reticulum).
• Smooth endoplasmic reticulum is the site for complex lipid and carbohydrate synthesis and
detoxification of drugs.
• Nascent proteins synthesized in ER are modified in Golgi bodies and then exported to specific
destinations in the cell.
• Golgi apparatus is primarily involved in glycosylation, protein sorting, packaging and secretion.
• Lysosomes are bags of hydrolytic enzymes responsible for autophagy, postmortem autolysis, and
phagocytosis.
• Mitochondria, the powerhouse of the cell has its own DNA encoding mitochondrial proteins and a
role in triggering apoptosis.
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 DR.SK GUPTA M.D AND DR. BINITA GOSWAMI MBBS, M.D, DNB, MNAMS,
FIMSA, TEXTBOOK OF MEDICAL BIOCHEMISTRY 3RD EDITION OF ARYA
PUBLISHING COMPANY.

 DR.INDUMATI V, DR.SOWBHAGYA LAKSHMI, INTEGRATED TEXTBOOK OF

BIOCHEMISTRY 2ND EDITION PARAS MEDICAL PUBLICATION.

DR.DM VASUDEVAN, DR. SREEKUMARI S, DR. KANNAN VAIDYANATHAN,

TEXTBOOK OF BIOCHEMISTRY FOR MEDICAL STUDENTS 10TH EDITION OF
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DR. PRASAD R MANJESHWAR, TEXTBOOK OF BIOCHEMISTRY FOR

MEDICAL STUDENTS REVISED 6TH EDITION, RM PUBLICATION