CELL STRUCTURE CHARACTERISTICS FUNCTIONS Abnormalities/

Transport
Cellular membrane Trilamar compartmentalization
Lipid and protein organise enzyme for
Carbs effective biochemical
Dynamic (Fluid mosaic interaction
model) selectively permeable
barrier
Transporting solutes
Responding to external
signal
Interaction for adjacent
cells
Energy transduction
Mitochondria Can fuse with one Contain DNA, ribosome Disorder
another or split into and enzyme. RNA and mutation in
two protein are synthesised mitochondrial
Two membranes in matrix, not DNA/mtDNA
Outer – 50% lipid intermembrane space Inherited
Inner bacterial like – Cristae – ATP machinery maternally
75% protein, locate Proliferation
cardiolipin, porin Carbohydrate mitochondria
metabolism – TCA cycle Premature
aging

Peroxisome Membrane bound Oxidative metabolism Zellweger

vesicles with oxidative Oxidise long chain fatty syndrome
enzymes acids Lack enzyme
Form by splitting from Synthesise
preexisting organelle plasmalogens in neuron Adrenoleukodyds-
Glyoxysome(plant) cells trophy
Export preformed Fatty acid
proteins accumulate in
H2O2 formed, is broken brain,
down by catalase destruct
myelin sheath
SER In endocrine cell synthesis of steroid
In liver detoxification
In muscle cell sequestration of calcium ion
into cytoplasm
RER On ribosomes Polypeptide synthesis Messenger RNA
(secreted, integral binds to free
membrane, soluble ribosome
proteins) Nascent protein
On “free” ribosomes Human genome, cytosolic, synthesised on
peripheral membrane, ribosome have
nuclear protein their signal
sequence
recognised by SRP
SRP interact with
Processing nascent/newly a SRP receptor
synthesised protein Ribosome interact
-carbo added by with translocon
oligosaccharltransferase SRP-RIBOSOME-
- RER is packed with NASCENT PEPTIDE
 chaperones to assist in CHAIN COMPLEX
folding and contain protein binds to ER
disulfide isomerase to add GTP-binding
disulfide bonds protein helps the
release of SRP
Upon entering
RER lumen, the
signal sequence is
cleaved by signal
peptidase
Transport vesicles Donor compartment Biosynthetic – modify & Fuse to form the
budding transport ER G intermediate
Receptor Secretory- constitutive & compartment
Recipient regulated COP II-coated
compartment fusion vesicles move
materials from ER
forward to ERGIC
to Golgi
COP I-coated
vesicles move
materials
backwards
Golgi Apparatus Stack of flattened Cis Golgi network sorts Vesicular
cisternae protein for the ER od transport model
Functional next Golgi station Cargo is shuttled
compartments Trans Golgi network fr CGN to CGMGN
Cis- sort protein proteins to to MGN to
Trans- membrane/ MGTGN to TGN in
intracellular destination vesicles
Glycoslyation, assembly Clathrins-coated
of carbo in glycolipid, vesicles move
glycoprotein, sequence materials from
them into TGN to
Lysosomal protein is oligosaccharides with endosomes,
phosphorylated/tagged enzyme lysosomes and
with mannose residue so glycosyltransferases(α-
they are recognised by mannosidase I, GlcNac-
(MPRs) mannose-6- transferase I, α-m iI,
phosphate receptors GlcNac-t Ii, fucosyl &
galactosyl- t, Sialyl- t

Lysosome Organelle turnover Lysosomal

Autophagy when fuse storage disorder –
with autophagosome absence of
To digest damaged lysosomal enzyme
organelle thus accumulated
material cause
Tay-Sachs disease