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The Cell

Prokaryotes and
eukaryotes
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Cells
Cells :structural and functional units of all living
organisms
unicellular, consisting of a single cell and
multicellular, (an estimated 1013 cells in humans!)
Each cell can take in nutrients, convert these
nutrients into energy, carry out specialized
functions, and reproduce as necessary.
Each cell stores its own set of instructions for
carrying out each of these activities.
There are two general categories of cells:
prokaryotes and eukaryotes
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Life on Earth
.

Cellular components
.

Eukaryote and prokaryotes


.

The cell
.

The cell
.

Where do viruses fit?


.

The Nucleus and Nucleolus


.

The Nucleus
.

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Nucleoproteins
.

11

Nucleosome and beads on a string


conformation

12

Chromosomes
.

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The Nucleus and Nucleolus


The nucleus is the most obvious organelle in any eukaryotic
cell.
It is a membrane-bound organelle and is surrounded by a
double membrane. It communicates with the surrounding
cytosol via numerous nuclear pores.
Within the nucleus is the DNA responsible for providing
the cell with its unique characteristics.
The DNA is similar in every cell of the body, but depending
on the specific cell type, some genes may be turned on or
off - that's why a hepatocyte is different from a epithelial
cell .
When a cell is dividing, the DNA and surrounding protein
condense into chromosomes that are visible by microscopy.
The prominent structure in the nucleus is the nucleolus.
The nucleolus produces ribosomes, which move out of the
nucleus to positions on the rough endoplasmic reticulum
where they are critical in protein synthesis.

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Endoplasmic reticulum(ER)
.

15

RE
.

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Endoplasmic reticulum(ER)
Is a vast membrane structure.
The ER membrane is a continuation of the outer nuclear
membrane
When viewed by electron microscopy, some areas of the
endoplasmic reticulum look "smooth" (smooth ER) and some
appear "rough" (rough ER). The rough ER appears rough due
to the presence of ribosomes on the membrane surface.
Smooth ER is important in the synthesis of lipids and
membrane proteins. Rough ER is important in the synthesis of
other proteins.
Information coded in DNA sequences in the nucleus is
transcribed as messenger RNA. Messenger RNA exits the
nucleus through small pores to enter the cytoplasm. At the
ribosomes on the rough ER, the messenger RNA is translated
into proteins.
These proteins are then transferred to the Golgi in "transport
vesicles" where they are further processed and packaged into
lysosomes, peroxisomes, or secretory vesicles.

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The Golgi

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Golgi complex regulates the insertion of plasma membrane proteins

19

Golgi Apparatus
The Golgi apparatus is a membrane-bound
structure with a single membrane.
It is actually a stack of membrane-bound
vesicles that are important in packaging
macromolecules for transport elsewhere in the
cell.
The stack of larger vesicles is surrounded by
numerous smaller vesicles containing those
packaged macromolecules.
The enzymatic or hormonal contents of
lysosomes, peroxisomes and secretory vesicles
are packaged in membrane-bound vesicles at
the periphery of the Golgi apparatus.
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Mitochondria
An eukaryotic cell contains many mitochondria,
occupying up to a quarter of the cytoplasmic volume.
The size of a mitochondrion is about 1.5-2 mm in
length, 0.5-1 mm in diameter.
It has two membranes: outer membrane and inner
membrane. Mitochondria also have their own DNA
( mtDNA), which encodes some of the proteins and
RNAs in mitochondria.
However, most proteins operating in mitochondria still
originate from nuclear DNA.
The major role of mitochondria is to produce ATP
In animal cells, the major sources for the synthesis of
ATP are fatty acids and glucose.
The generation of ATP involves a series of electron
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transport in the mitochondria

Mitochondrion

22

Mitochondrial compartments

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ATP synthesis in the cristae


.

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Electron Transport on the inner mitochondrial membrane

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The respiratory chain is located on the inner mitochondrial


membrane

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Protein import by mitochondria through protein


"porin".

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Mitochondria ( apoptosis and aging)

Release of cytochrome c from mitochondria into the cytoplasm,


in concert with Apaf1, can activate caspase 9, which then
activate caspase 3 to execute the death program.
Cytochrome c and other small molecules may pass through the
mitochondrial permeability transition pore in the outer
membrane, the adenine nucleotide translocator (ANT) in the
inner membrane, and several auxiliary proteins that include the
Bcl-2 family involved in apoptosis.
The Bcl-2 family of proteins may be divided into three groups:
Anti-apoptotic. They share sequence homology at BH1, BH2,
BH3, and BH4 domains (BH = Bcl-2 homology). Examples: Bcl2 itself and Bcl-xL.
Pro-apoptotic. They share sequence homology at BH1, BH2 and
BH3 domains. Examples: Bax and Bak
BH3-only proteins. They are pro-apoptotic, but share homology
only at the BH3 domain. Examples: Bid, Bik, and Bim.
Electrons may leak from the electron transport chain, producing
free radicals. This has been suggested to be the major
mechanism involved in the aging process.
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Mitochondria
Mitochondria provides energy to the cell. They
are the power centers of the cell.
They are about the size of bacteria but may have
different shapes depending on the cell type.
Mitochondria are membrane-bound organelles,
and like the nucleus have a double membrane.
The outer membrane is fairly smooth. But the
inner membrane is highly convoluted, forming
folds called cristae.
The cristae greatly increase the inner
membrane's surface area.
It is on these cristae that NADH and FADH2 from
food oxidation is combined with oxygen to
produce ATP
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Prokaryotic Ribosome(70S)

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80S and 70S Ribosomes


.

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Composition of Ribosomes
.

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Lysosomes, Peroxisomes, Secretory Vesicles

Lysosomes:
i. Lysosomes (common in animal cells but rare in plant cells)
contain hydrolytic enzymes necessary for intracellular digestion.
ii. In white blood cells that engulf bacteria, lysosome contents are
carefully released into the vacuole around the bacteria and serve
to kill and digest those bacteria.
iii. Uncontrolled release of lysosome contents into the cytoplasm can
also cause cell death .
Peroxisomes:
i. This organelle is responsible for protecting the cell from its own
production of toxic hydrogen peroxide.
ii. As an example, white blood cells produce hydrogen peroxide to
kill bacteria. The oxidative enzymes in peroxisomes break down
the hydrogen peroxide into water and oxygen.
Secretory Vesicles:
i. Cell secretions - e.g. hormones, neurotransmitters - are packaged
in secretory vesicles at the Golgi apparatus.
ii. The secretory vesicles are then transported to the cell surface for
release.

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Membrane and Cytosol


Cell Membrane:
i. Every cell is enclosed in a membrane. The membrane
is a double layer of lipids (lipid bilayer) but is made
quite complex by the presence of numerous proteins
that are important to cell activity.
ii. These proteins include receptors, pores, and
enzymes. The membrane is responsible for the
controlled entry and exit of ions like sodium (Na)
potassium (K), calcium (Ca++).
Cytosol:
i. The cytosol also called cytoplasm is an ammorphous
viscous fluid within which all the other cell
organelles reside and where most of the cellular
metabolism occurs.
ii. It is full of proteins that control cell metabolism
including signal transduction pathways, glycolysis,
intracellular receptors, and transcription factors etc.
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FUNCTIONS OF BIOLOGICAL MEMBRANES

Compartmentation

Cells use plasma membrane as an envelope.

Subcellular organelles nuclei, mitochondria, chloroplasts,


endoplasmic reticulum, Golgi apparatus, etc.
Control of the passage of materials

Control the flow of nutrients, waste products, ions, etc.

Contain pumps and gates.


Biochemical processes

Oxidative phosphorylation
.
electron transport

Processing of information

Sensory stimuli

Intercellular communication(gap junctions

Nerve impulses

Hormonal actions
Cell-cell recognition
. immunological

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The chemical components of


membranes

General composition.
The components

Lipid -- cholesterol, phospholipid and sphingolipid


Proteins
Carbohydrate -- as glycoprotein

Differences in composition among membranes (e.g.


myelin vs. inner mitochondrial membrane)

Illustrate the variability of membrane structure.


This is due to the differences in function. Example:
Mitochondrial inner membrane has high amounts of
functional electron transport system proteins.
Plasma membrane, with fewer functions (mainly ion
transport), has less protein.
Membranes with similar function (i.e. from the same
organelle) are similar across species lines, but membranes
with different function (i.e. from different organelles) may
differ strikingly within a species.

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Common membrane phospholipids

37

Phosphatidyl choline

38

Phosphatidylcholine
.

39

Cholesterol is another common membrane


lipid

40

Amphipathic molecules.

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Structure-based classification of membrane


lipids

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Lipid Bilayer
Amphipathic lipids in association with
water form complexes in which their polar
regions are in contact with water and their
hydrophobic regions are away from water.
Various micelle structures. E.g., the
spherical micelle is a stable configuration
for amphipathic lipids that have a conical
shape, such as fatty acids.
A bilayer. This is the most stable
configuration for amphipathic lipids with a
cylindrical shape, such as phospholipids.
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Phosphatidylcholine
.

44

Membrane fluidity

The interior of a lipid bilayer is highly fluid


In the liquid crystal state, hydrocarbon
chains of phospholipids are disordered and
in constant motion.
At lower temperature, a membrane
containing a single phospholipid type
undergoes transition to a crystalline state
in which fatty acid tails are fully extended,
packing is highly ordered, and van der
Waals interactions between adjacent
chains are maximal.
Kinks, due to cis double bonds in fatty
acids, interfere with packing of lipids in the
crystalline state, and lower the phase
transition temperature.
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Membrane fluidity

Presence of cholesterol in a phospholipid membrane


inhibits transition to the crystalline state. However
interaction with the relatively rigid cholesterol
decreases the mobility of hydrocarbon tails of
phospholipids. Phospholipid membranes that include
cholesterol have a fluidity intermediate between the
liquid crystal and crystal states.
Two strategies by which phase changes of membrane
lipids are avoided:
Cholesterol is abundant in membranes, such as
plasma membranes, that include many lipids with
long-chain saturated fatty acids. In the absence of
cholesterol, such membranes would crystallize at
physiological temperatures.
The inner mitochondrial membrane lacks cholesterol,
but includes many phospholipids whose fatty acids
have one or more double bonds, which lower the
melting point to below physiological temperature.
46

Membrane Fluidity
Cholesterol is abundant in membranes,
such as plasma membranes, that include
many lipids with long-chain saturated
fatty acids. In the absence of cholesterol,
such membranes would crystallize at
physiological temperatures.
The inner mitochondrial membrane lacks
cholesterol, but includes many
phospholipids whose fatty acids have one
or more double bonds, which lower the
melting point to below physiological
temperature.
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Bilayer and micelle


.

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Lipid bilayer
.

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Lipid Bilayer
.

50

Lateral mobility and Flip Flop


.

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Lipid bilayer
.

Color scheme: PO4 = green, N(CH3)3 = violet, water = blue, terminal CH3
= yellow,
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O = red, glycol C = brown, chain C = grey

Schematic diagram of membrane structure

53

Schematic diagram of membrane proteins

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Membrane-spanning -helix

A membrane-spanning a-helix is the most common


structural motif found in integral proteins

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Membrane structure
.

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Plasma membrane
.

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A cartoon of EM view of membranes via freeze


fracture/freeze technique

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Blood-group antigens
The antigens which determine blood types belong to
glycoproteins and glycolipids.
There are three types of ABO blood-group antigens: O,
A, and B. They differ only slightly in the composition of
carbohydrates.
All humans contain enzymes which catalyze the
synthesis of the O antigen.
Humans with A-type blood also contain an additional
enzyme (called A-type enzyme here) which adds NAcetylgalactosamine to the O antigen.
Humans with B-type blood contain another enzyme
(called B-type enzyme ) which adds Galactose to the O
antigen.
Humans with AB-type blood contain both A-type and
B-type enzymes while humans with O-type blood lack
both types of enzymes.
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Blood group antigens


.

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Distribution of lipids in membranes


There can be large membrane to membrane
differences in lipids (compare
phosphoglycerides and cholesterol in plasma
membrane vs. inner mitochondrial
membrane).
There can be large differences within
classes of lipids (compare the cardiolipin of
the inner mitochondrial membrane to other
membranes).
There are also patterns of differences
among the fatty acyl groups of the lipids of
various membranes
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The proteins of membranes


Classification

Peripheral: Are loosely associated with the


membrane surface.
In integral: Are deeply imbedded in the
membrane. Roles of membrane proteins.
Catalytic: enzymes
Receptors
Transport
Structural Carbohydrates of membranes are present
attached to protein or lipid as glycoprotein or
glycolipid.

Typical sugars in glycoproteins and glycolipids


include glucose, galactose, mannose, fucose and
the N-acetylated sugars like N-acetylglucosamine,
N-acetylgalactosamine and N-acetylneuraminic
acid (sialic acid).
Membrane sugars seem to be involved in
identification and recognition.
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Transmembrane proteins
(1) single-pass
(2) multiple-pass
Trans-membrane proteins have membrane
spanning portions containing alpha
helically arranged sequences of 20-25
hydrophobic amino acids.
Short strings of hydrophilic amino acids
separate the hydrophobic sequences from
each other:
These hydrophilic stretches tend to be
found exposed to the more aqueous
environments associated with the
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cytoplasm or the extra cellular space.

Aliphatic side-chains
.

Residues with aliphatic side-chains (leucine, isoleucine, alanine,


valine)
predominate in the middle of the bilayer.
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Polar amino acids in membranes

Tyrosine and tryptophan are common near the membrane


surface. Lysine and arginine are often at the lipid/water
interface, with the positively charged groups at the ends of
their aliphatic side chains extending toward the polar
membrane surface.

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Lipid anchor
Lipid anchor: Some proteins bind to membranes via a
covalently attached lipid anchor, that inserts into the
bilayer
The attached lipid may be a fatty acid such as
palmitate or myristate.
Palmitate is usually attached via an ester linkage to
the thiol of a cysteine residue. A protein may be
released from the plasma membrane to the cytosol via
depalmitoylation, hydrolysis of the ester linkage.
An isoprenoid, such as a farnesyl residue, is attached
to some proteins via a thioether linkage to a cysteine
thiol.
Fatty acid or isoprenoid chains link proteins to the
cytosolic surface of the plasma membrane
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Lipid anchors
.

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Membrane structure

The amphipathic properties of the phosphoglycerides


and sphingolipids These charges are responsible for
the hydrophilicity.
The long hydrocarbon chains of the acyl groups are
hydrophobic
Phospholipids in an aqueous medium spontaneously
aggregate into orderly arrays.
Micelles
Lipid bilayers
Liposomes are structures related to micelles, but
they are bilayers,.
The properties of phospholipids determine the kinds
of movement they can undergo in a bilayer.
Rotation ,Lateral diffusion ,flexing of the acyl
chains,Transverse movement from side to side of
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the bilayer (flip-flop).

The fluid mosaic model


.

A lipid bilayer composed of phospholipid and


cholesterol
Proteins. Integral proteinss.Peripheral proteins are
loosely attached to the surface.
Membrane surfaces have asymmetry
There are differences in lipid/protein composition
between the sides of a membrane.
Different catalytic proteins (enzymes) appear on
the two sides of membranes.
Carbohydrate is mostly on the outer
surface.egRBCs
Some proteins (ankyrin, spectrin) are associated
with the inner surface of the membrane.
Other proteins transfix the membrane
(glycophorin), or loop back and forth from side to
side
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Passive (simple) diffusion

- Water and small lipophilic organic compounds can


cross. Large molecules (e.g. proteins) and charged
compounds do not cross.
Movement is DOWN the concentration gradient ONLY
Rate of diffusion depends on
charge on the molecule -- electric charge prevents
movement.
size -- smaller molecules move faster than larger
molecules.
lipid solubility -- more highly lipid-soluble molecules
move faster.
the concentration gradient -- the greater the
concentration difference across the membrane, the
faster the diffusion.
Molecules may cross the membrane in either direction,
depending only on the direction of the gradient.

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Passive (simple) diffusion

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Protein channels

Protein channels transport specific ions.


Ion channels exist for Na+, K+ and Ca+
+ movement. These channels are specific
for a given ionic species.
Channels consist of protein, which forms
a gate that opens and closes under the
control of ligand or membrane potential.
Ion movement is always down the
concentration gradient.

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transport).
A carrier must be able to :

Recognition its ligand


Translocation
Release -- on the other side of the membrane
Recovery -- return of the carrier to its original
condition. Carriers resemble enzymes in some
of their properties.
They are NOT enzymes, They are enzyme-like in
the following ways:
They are specific.
Their dissociation constants are analogous to
Km of enzymes.
Inhibited by specific inhibitors.
They exhibit saturation.
Nomenclature:
Uniport:,Symport,: Antiport.
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Passive mediated transport( facilitated diffusion).

The characteristics:.
Faster than simple diffusion
Movement is down the concentration gradient only
No energy input is required.
The carrier exhibits specificity, saturation kinetics ,specific
inhibitability
Examples :
Glucose transport in many cells.
A uniport system
Adding a substance analogous to glucose can inhibit glucose
transport specifically.
It is specific for glucose. The Km for glucose is 6.2 mM
Involves attachment of glucose outside the cell.
Conformational change of the carrier protein. Release of the
glucose inside the cell.
Chloride-bicarbonate transport in the erythrocyte membrane.
An antiport system: both ions must move in opposite
directions simultaneously.
The system is reversible, and can work in either direction.
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Movement is driven by the concentration gradient

Passive mediated transport(facilitated diffusion).

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Active mediated transport

i.
ii.

Is against a concentration gradient, and requires energy.


There are two sources of energy .
ATP hydrolysis may be used directly.
The energy of the Na+ gradient may be used in a symport
mechanism. The energy of the Na+ going down its gradient
drives the movement of the other substance. But since the Na+
gradient is maintained by ATP hydrolysis, ATP is the indirect
source of energy for this process.
A carrier operating by active transport.
Can move substances against a concentration gradient.
Requires energy.
Is unidirectional
Exhibits :specificity, saturation kinetics and specific
inhibitability.
Release from the carrier into a higher concentration is explained
by:
The affinity of the translocase for the substance must
decrease. (conformational change?).
Require energy in the form of ATP.
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Active mediated transport.


Ca++ transport is a uniport system, using ATP.
There are two Ca++ translocases of importance.
In the sarcoplasmic reticulum, important in
muscle contraction.
A different enzyme with similar activity in the
plasma membrane.
The Na+-K+ pump (or Na+-K+ ATPase).
An antiport system.
Importance: To maintain the Na+ and K+
gradients.
Stoichiometry: 3 Na+and 2 K+ in/per one ATP
hydrolyzed.
Specificity: Specific for Na+, but it can substitute
for the K+.
The structure of the Na+-K+ pump is a tetramer of
two types of subunits, 22. The Na+-K+ ATPase
is specifically inhibited by the ouabain.
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Proposed mechanism of the Na+/K+ ATPase

Na+ attaches on the inside of the cell


membrane.
The protein conformation changes due to
phosphorylation of the protein by ATP, and
the affinity of the protein for Na+
decreases.
Na+ leaves.
K+ from the outside binds.
K+ dephosphorylates the enzyme.
The conformation now returns to the
original state.
K+ now dissociates.
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Na+ linked glucose transport


Na+ linked glucose transport is found
in intestinal mucosal cells.
It is a symport system; glucose is
transported against its gradient by
Na+ flowing down its gradient.
Both are transported into the cell
from the intestinal lumen.
Na+ is required; one Na+ is carried
with each glucose.
The Na+ gradient is essential; it is
maintained by the Na+-K+ ATPase.
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Membrane receptors

Cell-cell communication is by chemical messenger.


There are four types of signals.
Nerve transmission
Hormone release
Muscle contraction
Growth stimulation
There are four types of messenger
molecules:i)steroids ii)small organic

molecules iii)peptides iv) proteins

The messenger interact with the cell by either:


By diffusion through the cell membrane (e.g..
steroid hormones).
Binding to a receptor on the plasma
membrane.
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Signaling
.

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Some receptors involve second messengers

Formation of an intracellular molecule called a


second messenger.
Second messenger formation is a means of
amplifying the original signal.
The formation and removal of the second
messenger can be controlled and modulated.
Cyclic AMP (cAMP) is a second messenger that
mediates many cellular responses.
The mechanism of action of cAMP is to activate
an inactive protein kinase A. This process is an
amplification of the original signal.
Since the protein kinase is activated by cAMP
it is called protein kinase A.
cAMP is synthesized by the enzyme, adenyl
cyclase.
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Inositol triphosphate (IP3) and diacylglycerol (DG)

IP3 and DG are synthesized by , phospholipase C, which


has phosphatidylinositol 4,5-bisphosphate (PIP2)
phosphodiesterase activity..
The phosphodiesterase is controlled by a G-protein in the
membrane.
Mechanism: IP3 and DG have separate effects.
IP3 releases Ca++ from the endoplasmic reticulum.
The Ca++ then activates certain intracellular protein
kinases.
DG activates protein kinase c, Note that both IP3 and
DG activate protein kinases, which in turn
phosphorylate and affect the activities of other
proteins.
Termination of the signal occurs at several levels.
IP3 is hydrolyzed.
Ca++ is returned to the endoplasmic reticulum or
pumped out of the cell.
The GTPase activity of the G-protein hydrolyses the
GTP, terminating the activity of the phospholipase C.

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Insulin (IR) and growth factor receptors.

IR a tetramer with two kinds of subunits, alpha and beta.


Many of the cellular responses are well known, e.g.
Glucose transport and protein phosphorylation
Insulin and many growth factors activate a protein kinase
which phosphorylates a tyrosyl residue in the target
proteins, including the receptor itself.
The phosphorylation of tyrosyl residues is unusual;
usually seryl or threonyl residues become
phosphorylated.
Termination of the insulin signals involves internalization
and degradation .The receptor-insulin complex migrates
to a region of the plasma membrane with the protein
clathrin coating its inner surface.
This region forms a "coated pit," a region that invaginates
and pinches off, forming an intracellular "coated vesicle."

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Second messengers.
Adenyl cyclase is controlled by Gs and Gi.
The action of the G-proteins.
Structure: G-proteins are complexes of three different subunits,
alpha, beta and gamma. Mechanism: Receptor-messenger
interaction stimulates binding of GTP to the alpha-subunits. The
alpha-subunit with its bound GTP then dissociates from the
beta-gamma complex. The alpha-subunit with its bound GTP
then acts on adenyl cyclase. alphas-GTP stimulates adenyl
cyclase. alphai-GTP inhibits adenyl cyclase.
Termination of the signal occurs at several levels.
The alpha-subunit of the G-protein has GTPase activity. cAMP
already formed is cleaved by cAMP phosphodiesterase.
The hormone gradually and spontaneously dissociates from the
receptor.
cAMP is degraded by cAMP phosphodiesterase.
cAMP + H2O -> AMP
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Disease process and membrane receptors

HIV and CD4 receptors/CCRX co receptors


Cholera toxin and GM1 receptor.
The adenosine diphosphate (ADP)ribosyltransferases bind nicotinamide adenine
dinucleotide (NAD), and catalyze the transfer of
the ADP-rebose moiety to an acceptor
nucleophile.

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Cholera toxin
Cholera toxin catalyzes covalent modification of
Gs. ADP-ribose is transferred from NAD+ to an
arginine residue at the GTPase active site of
Gs. This ADP-ribosylation prevents Gs from
hydrolyzing GTP. Thus Gs becomes
permanently activated.
Pertussis toxin (whooping cough disease)
catalyzes ADP-ribosylation at a cysteine residue
of Gi, making the inhibitory G incapable of
exchanging GDP for GTP. Thus the inhibitory
pathway is blocked.
ADP-ribosylation is a general mechanism by
which activity of many proteins is regulated, in
eukaryotes (including mammals) as well as in
prokaryotes.
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Mechanisms of ADP Ribosylation

88

Cholera toxin (CT)


ADP ribosylated G protein loses GTPase activity
and perpetually activate adenylate cyclase
Cholera toxin has ADP ribosylating activity
CT has A and B fragments
The B fragment is responsible for GM1receptor
recognition and translocation of the A-fragment
A is the catalytic domain.The A1 fragment of
cholera toxin (CTA), catalyze the transfer of ADPribose to arginine-201 of the -subunit of the
adenylate cyclase regulatory protein Gs.
GTPase action of G protein is lost
c-AMP accumulates, triggering a signaling
cascade which eventually culminates in massive
diarrhea

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Glucose 6-Phosphate Dehydrogenase Deficiency

It is the most common genetic alteration


in the world (>400 million people).
There are varying degrees of this
deficiency (depending on the mutation
that occurs in the gene for G6P DH)
The most severe are eliminated early in
development, however, the majority are
phenotypically silent.
Even the latter can develop a phenotype
under conditions that stress the NADPH
levels (i.e. oxidative stress); these
include:
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Glucose 6-Phosphate Dehydrogenase Deficiency

Metabolic stress can be triggered


by:
i. Sulfur Drugs
ii. Malaria Drugs
iii. Infection with some viruses and
bacteria
iv. Fava Beans
Hemolytic Anemia develops if
oxidative species, like H2O2, cannot
be properly detoxified by RBCs
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G6PD

92

G6PD

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Oxidation and reduction of Glutathione


H2O2
2 H 2O
Glutathione Peroxidase
2 GSH
GS-SG
Glutathione Reductase

NADP+

NADPH
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