CELL-CELL ADHESION AND CELL JUNCTION

SUBMITTED BY
ASHISH PALODKAR
MSC. BIOTECHNOLOGY
1 SEM SUBMITTED TO
DR ROHINI KESHAVA
GUIDE
 CONTENT
 CELL-CELL INTERACTION
 CELL ADHESION
CADHERINS
SELECTIN
INTEGRINS
IMMUNOGOBULIN FAMILY
 CELL JUNCTION
 OCCULUDING JUNCTION
TIGHT JUNCTION
SEPTATE JUNCTION
 ANCHORING JUNCTION
ADHEREN JUNCTION
FOCAL JUNCTION
DESMOSOMES
HEMI-DESMOSOMES
 COMMUNICATING JUNCTION
GAP JUNCTION
PLASMDESMATA
CHEMICAL SYNPASES
SUMMARY
 BIBLOGRAPHY
 CELL ADHESION

 Cell-cell adhesion is a selective process such that cells

adhere only to other cell of specific types.
 This selectivity was first demonstrated in classical
studies of embryo development, which showed that cells
from one tissue (e .g. liver) specifically adhere to cell of
the some tissue rather than to cells of a different tissue
(e.g. brain).
 Such selective cell-cell adhesion is mediated by trans-
membrane protein called ‘cell adhesion molecules’
(CAM)
 CELL ADHESION
TYPES OF CELL ADHESION
1. CELL-CELL ADHESION
2. CELL-EXTRACELLULAR MATRIX
 CELL ADHESION MOLECULES

 Cell adhesion molecules are protein located on the cell

surface involved with the binding with other cells or
with the extracellular matrix (ECM) in the process called
cell adhesion.
 Are typically trans-membrane receptor and are
composed of three domains : an intracellular domains
that interacts with cytoskeleton, a trans membrane
domain and an extracellular domain that interacts with
other CAMs of same kinds (hemophilic binding ) or
with other CAMs or the extracellular matrix
(heterophilic binding)
CELL ADHESION MOLECULES ARE
DIVIDED INTO FOUR MAJOR GROUPS
 1. SELECTIN
 2. INTEGRINS

 3. CADHERINS

 4.IMMUNOGLOBULIN SUPERFAMILY (Ig)

CELL ADHESION INTERACTION
 HOMOPHILIC BINDING : Interaction in which an adhesion
molecule on the surface of one cell binds to the same molecule on
the surface of another cell.
 HETROPHILIC BINDING : Interaction in which an adhesion
molecule on the surface of one cell recognizes a different molecule
on the surface of another cell (eg. selectin and an integrin)
 LINKER DEPENDENT BINDING: Interaction of adjacent cell
adesion molecule on the surface of two cell binds with a help of
linker molecule.
 CADHERIN
 Expressed in both invertebre and vertebrate
 Are main molecules holding cells together in early embryonic
tissue
 Homophilic binding

 Calcium dependent

 formation of adheren junction and desmosomes

 Most cadherin are single pass trans-membrane glycoproteins

about 700-750 amino acid long.
 They associate in the plasma membrane to form dimmers or
larger oligomers as extracellular part of the polypeptide chain
which is usually folded into five or six cadherin repeats, which
are structurally related to immunoglobulin (Ig) domains
 The Ca2+ ions are positioned between each pair
of cadherin repeats, locking the repeats together to form a
stiff, rod like structure: the more Ca2+ ions that are bound, the
more rigid the structure is.
 If Ca2+ is removed, the extracellular part of
the protein becomes floppy and is rapidly degraded
by proteolytic enzymes
THE LINKAGE OF CLASSICAL CADHERINS TO ACTIN FILAMENTS
THE CADHERINS ARE COUPLED INDIRECTLY TO ACTIN FILAMENTS
BY THE ANCHOR PROTEINS Α-CATENIN AND Β-CATENIN. A THIRD
INTRACELLULAR PROTEIN, CALLED P120, ALSO BINDS TO
THE CADHERIN CYTOPLASMIC TAIL AND
REGULATES CADHERIN FUNCTION. Β-CATENIN HAS A SECOND,
AND VERY IMPORTANT, FUNCTION IN INTRACELLULAR
SIGNALLING.
 
 Divided as classical and non-classical cadherin
 Classical cadherin are E-cadherin, P-cadherin and N-cadherin
and are widely expressed during early differentiation
 E-cadherin is present in epithelial cells; N-cadherin in nerve
cells and P-cadherin in placenta and epidermis.
 Non-classical cadherins include proteins with known
adhesive function such as desmosomal cadherins and
protocadherin found in brain
 SELECTIN
 Single trans-membrane protein with highly consereved
lectin domain
 Heterophilic binding

 Calcium dependent cell-cell adhesion in the

bloodstream.
 Three types of selectin: L-selectin in blood
cells(leukocytes), P-selectin in blood platelets and E-
selectin in endothelial cells
 They are attached to actin filament with an anchor
protein
 they collaborate with integrins, which strengthen the
binding of the blood cells to the endothelium.
(A) The structure of P-selectin. The selectin attaches to the actin cytoskeleton through
anchor proteins that are still poorly characterized. (B) How selectins and integrins
mediate the cell-cell adhesions required
 Are active during inflammatory response
 have an important role in binding white blood cells
to endothelial cells lining blood vessels, thereby enabling
the blood cells to migrate out of the bloodstream into a
tissue
 INTREGRIN
 Heterophilic binding
 Present in verterbrates

 At least 24 integrin heterodimer composed of 18 types of α

subunits and 8 types of β subunits in various combination.
 Integrin subunits span the plasma membrane and in general
have very short cytoplasmic domains of about 40–70 amino
acids where as beta-4 subunits have 1088 amino acid
 The molecular mass of the integrin subunits can vary from
90 kDa to 160 kDa
 Helps in focal adhesion and hemi-desmosomes
 Protein named Talin activates the newly formed integrin
which is bent in position, attaches to the β tail
 Calcium and magnesium dependent

 It is hepls in formation of focal adhesion by forming a

complex of ligand, integrin molecule and associste plaques
protein
 Not only do integrins perform this outside-in signalling, but
they also operate an inside-out mode. Thus,
they transduce information from the ECM to the cell as well
as reveal the status of the cell to the outside, allowing rapid
and flexible responses to changes in the environment, for
example to allow blood coagulation by platelets.
 Integrins bind to extra-cellular proteins via short amino acid
sequences, such as the R-G-D sequence motif (found in
proteins such as fibronectin, laminin, or vitronectin)
 IMMUNOGLOBULIN SUPERFAMILY
 categorized as members of this superfamily based on shared
structural features with immunoglobulins (also known as
antibodies)
 Calcium independent

 Homophilic binding

 Proteins of the IgSF possess a structural domain known as

an immunoglobulin (Ig) domain.
 contain about 70-110 amino acids and are categorized
according to their size and function
 Ig-domains possess a characteristic Ig-fold, which has a
sandwich-like structure formed by two sheets of anti-
parallel beta strands.
 Among IgCAMs are neural CAMs, intercellular CAMs
(ICAMs) which function in the movement of leukocytes into
tissue and junction adhesion molecules (JAMs) which are
present in tight junction.
 NCAMs play important role in he differentiation of muscle,
glial and nerve cell.
 NCAMs comprises of extracellular region with five Ig repeats
and two fibronectin type III repeats, a single membrane-
spanning segment and cytosolic segment that interacts with the
cytoskeleton.
 In human, gene mutation in L1-CAM causes various
neuropathologies(e.g. mental retardation, congential
hydrocephalus and spasticity)
 CELL JUNCTION
 Cell junction is a type of structure that exists within the
tissue of a multi-cellular organism.
 They consist of protein complexes and provide contact
between neighboring cell or between a cell and the extra
cellular matrix or they buildup the paracellular barrier of
epithelia and control the paracellular transport.
 Cell junctions are especially abundant in epithelial
tissue.
CELL JUNCTION CAN BE CLASSIFIED INTO THREE
FUNCTIONAL GROUP

 OCCULUDING JUNCTION: Junction that seal cell

together in an epithelium in a way that prevents even
small molecule from leaking from one side of the sheet
to the other.
 ANCHORING JUNCTION: Mechanically attaches cell
(and their cytoskeletons) to their neighbors or to the
extracellular matrix.
 COMMUNICATING JUNCTION: Mediates the passage of
chemical or electrical signal from one interacting cell to
its proteins
1.Occluding junctions
a.tight junctions
b.sepate junction
2. Anchoring junctions
    a. actin filament attachment sites
      i. cell-cell adherens junctions (e.g., adhesion belts)
      ii. cell-matrix adherens junctions (e.g., focal
contacts)
    b. intermediate filament attachment sites
      i. cell-cell adhesion (desmosomes)
      ii. cell-matrix adhesion (hemi-desmosomes)
3. Communicating junctions
    a. gap junctions
    b. chemical synapses
    c. plasmodesmata (plants only)
 OCCLUDING JUNCTION
TIGHT JUNCTION:
 present in vertebrates.

 the epithelial cells lining the small intestine form a barrier that
keeps the gut contents in the gut cavity, the lumen.
 the tight junctions between epithelial cells are thought to have both
of these roles.
 first, they function as barrier to the diffusion of some membrane
proteins between apical and basolateral domains of the plasma
membrane. Mixing of such protein and lipid occur if tight junction
are disrupted by removing the extra cellular Ca2+ that is required
for tight junction integrity.
 Second, tight junction seal neighboring cells together so that if a
low-molecular weight tracer is added to one side of an epithelium, it
will generally not pass beyond the tight junction. Although all tight
junction are impermeable to macromolecule, their permeability to
small molecule varies greatly in different epithelia.
 SIMPLIFIED DRAWING OF A CROSS-SECTION THROUGH PART
OF THE WALL OF THE INTESTINE. THIS LONG, TUBELIKE
ORGAN IS CONSTRUCTED FROM EPITHELIAL TISSUES
(RED), CONNECTIVE TISSUES (GREEN), AND MUSCLE
TISSUES (YELLOW). EACH TISSUE IS AN ORGANIZED
ASSEMBLY OF CELLS HELD TOGETHER BY CELL-CELL
ADHESIONS, EXTRACELLULAR MATRIX, OR BOTH.
 Impermeable to macromolecule, their permeability to
small molecules varies greatly in different epithelia.
 ability to restrict the passage of ions through the spaces
between cell is found logarithmically with increasing
number of strands in the network,thus suggesting that
strands acts as independent barrier to ion flow
 Major trans membrane protein are claudin and occludin
and also ZO which is essential for formation of and
function of tight junction.
Role of tight junction in transcellular protein:   Transport proteins are confined to different regions of the
plasma membrane in epithelial cells of the small intestine. This segregation permits a vectorial transfer of
nutrients across the epithelial sheet from the gut lumen to the blood. In the example shown, glucose is
actively transported into the cell by Na+-driven glucose symports at the apical surface, and it diffuses out of
the cell by facilitated diffusion mediated by glucose carriers in the basolateral membrane. Tight junctions are
thought to confine the transport proteins to their appropriate membrane domains by acting as diffusion
barriers within the lipid bilayer of the plasma membrane; these junctions also block the backflow of glucose
from the basal side of the epithelium into the gut lumen
DISORDER RELATED TO TIGHT
JUNCTION
 Disruption of TJs leads to intestinal hyperpermeability
(the so-called "leaky gut") which has been proposed by
some researchers to involve a relationship with acute and
chronic diseases such as systemic inflammatory response
syndrome (SIRS frequently a response of the immune
system to infection), inflammatory bowel disease, type-1
diabetes, allergies, asthma,
and autism(impaired social interaction and
communication and restricted and repetative behaviour)
 SEPTATE JUNCTION
 Discovered by R.L. Wood 1959
 found in invertebrate tissues adhesion, sealing,
communication septa walls regularly spaced cross bars
15-17 nm .
 This are main occluding junction in invertebrates regular
in structure than a tight junction , they likewise form
continuous band around each epithielial cell. But their
morphology is proteins that are arranged in parallel rows
with a regular periodicity .
Electron micrograph of a septate junction between two epithelial cells of a mollusk.
The interacting plasma membranes, seen in cross-section, are connected by parallel
rows of junctional proteins. The rows, which have a regular periodicity, are seen as
dense bars or septa. (From N.B. Gilula, in Cell Communication [R.P. Cox, ed.], pp.
1-29)
 A protein called Disc-large, which is required for the
formation of septate junction in Drosophila is
structurally related to the ZO protein found in vertebrate
tight junction.
 Mutant flies that are deficient in this protein not only
lack septate function but also develop epithelial tumors.
 This observation suggests that the normal regulation of
cell proliferation in epithelial tissue may depend in part
on intra cellular signal that emanate from occluding
junction.
 ANCHORING JUNCTION

 widely distributed in animal tissue and are most

abundant in tissue that are subjected to serve mechanical
stress such as heart, muscle and epidermis.
 composed of two main classes of protein-Intra cellular
anchor protein and Trans-membrane adhesion proteins.
 Intracellular anchor protein:
proteins form a distinct plaque on the cytoplasmic face of
the plasma membrane and connect the junctional
complex to either actin filaments or intermediate
filaments.
 Trans-membrane adhesion protein :

protein have a cytoplasmic tail that binds to one or more

intracellular anchor protein and an extracellular domains
that interacts with either the extracellular matrix or the
extracellular domains of specific trans-membrane
adhesion protein on another cell.
 Anchoring Junction occurs in two functionally different
forms:
 1. Adheren junction and desmosomes hold cell together
and are formed by trans-membrane adhesion protein that
belong to the cadherin family.
 2. Focal adhesion and hemi-desmosomes bind cells to
the extra cellular matrix and are formed by trans-
membrane adhesion protein of the integrin family
 Depending upon Cytoskeleton attachment sites
anchoring junction is classified as
A). Actin filament attachment sites
1. adherens junction
2. focal adhesion
B). Intermedite filament attachment sites
1. Desmosomes
2. Hemi-desmosomes
 ADHEREN JUNCTION
 An adhern junction is defined as cell junction whose cytoplasmic
face is linked to the actin cytoskeleton .They can appear as band
encircling the cell (zonula adherens) or as spots of attachment to the
extracellular matrix (adhesion plaques ).
 In many non-epithelial tissues they take the form of small punctuate
or streak like attachment that indirectly connect the cortical actin
filament beneath the plasma membrane of two interacting cells. But
the prototypical examples of adheren junction occur in epithelia,
where they often form a continuous adhesion belt (zonula adherens)
just below tight junction, encircling each of the interacting cells in
the sheet.
 The adhesion belt are directly opposed in adjacent epithielial cells
with the interacting plasma membrane held together by the
cadherins that serve here as trans-membrane adhesion proteins.
The assembly of the tight junction between epithelial cell seem to
require the prior formation of adherens junction also block the
formation of tight junction.
 FOCAL ADHESION
 Integrin mediated junction
 Enable cells to get hold on the extra-cellular matrix through
integrins that link intra cellularly to actin filaments .In this
way muscle cells for example attach to their tendous at the
myotendinous junction.
 Likewise, when cultured fibroblast migrates on an artificial
substratum coated with extra-cellular matrix molecules,
they also grip the substratum at focal adhesion where
bundle of actin filament terminate.
 At all such adhesion , the extracellular domains of trans-
membrane integrin protein bind to a protein component of
the extra-cellular matrix , while their intra-cellular domain
bind indirectly to bundles of actin filament via the intra-
cellular anchor protein talin, α-actinin, filamin and vinculin.
 Function as signal carriers (sensors), which inform the
cell about the condition of the ECM and thus affect their
behavior
 important role in the immune system, in which white
blood cells migrate along the connective endothelium
following cellular signals and to damaged biological
tissue
 Also active signalling during cell motility to cell cycle
 DESMOSOMES
 Discovered by K.R. Porter in 1954
 Homophilic interaction between trans-membrane
protein(Cadherin)
 Through desmosomes the intermediate filament of adjacent
cell are linked into a net that extends throughout the many cell
of a tissue .
 The particular type of intermediate filament attached to the
desmosomes depend on cell type: they are keratin filament in
heart muscle cells .
 The junction has a dense cytoplasmic plaque composed of a
complex of intra cellular anchor proteins (plakoglobin and
desmoplakin) that are responsible for connecting the
cytoskeleton to the trans-membrane adhesion proteins.
 Found in muscle cells
 Blistering diseases such as Pemphigus vulgaris or
Pemphigus foliaceus can be due to genetic defects in
desmosomal proteins.(epithelial cells of skin)
 patients who suffer from autoimmune diseases
characterized by skin and mucous membrane blistering
produce autoantibodies against desmogleins 1 and 3
(DSG1, DSG3). These two observations suggested that
the loss of normal desmosome function could lead to
tissue fragility disorders.(cadherin based protein
desmoglein and desmocolin)
 HEMI-DESMOSOMES
 This are half-desmosomes resemble desmosomes
morphologically and in connecting to intermediate
filament and like desmosomes they act as rivets to
distribute tensile or shearing forces through an
epithelium .Instead of joining adjacent epithelial surface
of an epithelial cell to underlying basal lamina.
 The extracellular domains of the integrins that mediate
the adhesion bind to laminin protein in the basal lamina
while an intracellular domain binds via an anchor protein
(plectin) to keratin intermediate filaments.
DISORDER DUE TO HEMI-DESMOSOMES
 Epidermolysis Bullosa is a set of genetically inherited
conditions affecting 1 in 17,000 of the population. A
fault in a gene causes the skin to be extremely fragile.
The layers of the skin do not adhere properly and painful
widespread blisters occur very easily. These can lead to
increasing disfigurement, disability and in the most
severe forms death in early childhood.
 Genes encoding different components of
hemidesmosomes have been found to be mutated in
various forms of hereditary bullous skin disorders
 Table 19-2  Anchoring Junctions

Intracellular
Transmembrane Linker Cytoskeletal Some Intracellular
Junction Protein Extracellular Ligand Attachment Attachment Proteins
Adherens cadherin (E-cadherin) cadherin in neighboring actin catenins, vinculin,  -
(cell-cell) cell filaments actinin, plakoglobin

Desmosome cadherin (desmogleins cadherin in neighboring intermediate desmoplakins,

& desmocollins) cell filaments plakoglobin

Adherens integrin extracellular matrix actin talin, vinculin,  -actinin

(cell-matrix) proteins filaments

Hemidesmos integrin extracellular matrix (basal intermediate desmoplakinlike protein

ome lamina) proteins filaments
 COMMUNICATING JUNCTION
GAP JUNCTION
Discovered by J.P. Revel & M.J. Karnovsky in 1967.
 Found in animal cells including epithelial cell,
endothelial cell, cells of cardiac and muscle-
communication
 Are open channels allowing ions and small molecules to
diffuse freely between
 Couples both the metabolic activities and the electric
responses
 allows passages of some intracellular signalling
molecules such as cAMP and Ca2+
Gap junctions as seen in the electron microscope. Thin-section (A) and freeze-
fracture (B) electron micrographs of a large and a small gap junction between fibroblasts
in culture. In (B) each gap junction is seen as a cluster of homogeneous intra-membrane
particles associated exclusively with the cytoplasmic fracture face (P face) of the plasma
membrane. (From N.B. Gilula, in Cell Communication [R.P. Cox, ed.], pp. 1-29)
 Permits the passage of molecules as large as 1.2 nm in
diameter (mammalian) and 2 nm in insects
 Molecules smaller than 1200 Da can pass but lager than that
wont
 Thus ion, low-molecular weight precursors of cellular
macromolecules, products of intermediary metabolism and
small intracellular signaling molecules can pass
 Gap junction composed of connexins, a family of
structurally related trans-membrane proteins which consist
of 21 different human protein.
 Innexins forms gap junction in invertebrates
 Determining the size of a gap-junction channel.    When
fluorescent molecules of various sizes are injected into one of two
cells coupled by gap junctions, molecules smaller than about 1000
daltons can pass into the other cell but larger molecules cannot.
 Vertebrate hexagonal particle consists of 12 connexin
molecules: 6 of the molecules are arranged in connexon
hemi-channel
 Hexagonal cylinder of one plasma membrane when
joined to adjacent cell hemi-channel they form a
continuous aqueous channel between the cell
 Homotypic connexon : single type of connexin

 Hetero-oligomeric connexon : two or more type of

connexin
 plays a crucial role in the maintenance of homeostasis,
morphogenesis, cell differentiation, and growth control
in multicellular organisms
A MODEL OF A GAP JUNCTION.  THE DRAWING SHOWS THE INTERACTING
PLASMA MEMBRANES OF TWO ADJACENT CELLS. THE APPOSED LIPID
BILAYERS (RED) ARE PENETRATED BY PROTEIN ASSEMBLIES CALLED
CONNEXONS (GREEN), EACH OF WHICH IS THOUGHT TO BE FORMED BY SIX
IDENTICAL PROTEIN SUBUNITS (CALLED CONNEXINS). TWO CONNEXONS
JOIN ACROSS THE INTERCELLULAR GAP TO FORM A CONTINUOUS
AQUEOUS CHANNEL CONNECTING THE TWO CELLS.
 Gap junctions are not always open
 Opening & closing is regulated by changes in pH and
Ca2+ concentration
 High Ca2+, Low pH – closed

 Low Ca2+, high pH – open

 DISORDERS IN GAP JUNCTION
 Connexin 32 mutations cause X-linked Charcot-Marie-
Tooth disease, an inherited peripheral demyelinating
neuropathy.
 Connexin 26 mutations have been found in hereditary
nonsyndromic sensorineural deafness. Connexin 43
knockout mice die shortly after delivery because of
cardiac malformation.
 Neuronal gap junctions are involved in electrical
coupling and may also contribute to the recovery of
function after cell injury. Astrocytes are involved in the
pathology of most neuronal disorders, including brain
ischemia, Alzheimer's disease and epilepsy.
 In the pathology of brain tumors, gap junctions may be
related to the degree of malignancy and metastasis
 PLASMODESMATA
 Plays a key role in plant development
 Adhesion between plant cells is mediated by their cell walls
rather than by trans-membrane proteins. In particular,
specializes pectin-rich region of the cell wall called the middle
lamella acts as a glue to hold adjacent cells together.
 Because of the rigidity of plant cell walls, stable association
between plant cells do not require the formation of cytoskeleton
links such as those provided by the desmosomes and adherens
junction of animal cells.
 adjacent plant cell communicate with each other through
cytoplasmic connection called plasmodesmata (singular,
plasmodesma).
 Although distinct in structure, plasmodesmata function
analogously to gap junction as means of direct communication
between adjacent cells in tissues.
PLASMODESMATA.    (A) THE CYTOPLASMIC CHANNELS OF
PLASMODESMATA PIERCE THE PLANT CELL WALL AND
CONNECT ALL CELLS IN A PLANT TOGETHER. (B) EACH
PLASMODESMA IS LINED WITH PLASMA MEMBRANE COMMON
TO TWO CONNECTED CELLS. IT USUALLY ALSO CONTAINS A
FINE TUBULAR STRUCTURE (20-40NM), THE DESMOTUBULE,
DERIVED FROM SMOOTH ENDOPLASMIC RETICULUM
 An extension of the smooth endoplasmic reticulum
passes through the pore, leaving a ring of surrounding
cytoplasm through which ions and small molecules are
able to pass freely between the cells.
 Extension of endoplasmic reticulum called as
desmotubule
 Permits a passage of 10,000 Da

 Increase conc. of Ca2+ affects permeability, reverse

inhibiting movement of molecules
 Molecules like protein, nucleic acids, metabolic product
and plant virus pass through plasmadesmota also
membrane bound molecules
 CHEMICAL SYNAPSES
 The term was introduced by British neurophysiologist
Charles Sherrington, who argued, on the basis of his own
observations of reflex responses and the studies of the
great Spanish anatomist, Ramóny Cajal,
 Serves as one-way communication devices, transmitting
information in one direction only
 Consist of pre-synaptic cell which transmits information
to post-synaptic cell which recieves information
 Pre-synaptic cell and post-synaptic cell are are separated
by minute gap called synaptic cleft
 Neurotransmitter act as median for transmission
 Cytoplasm of pre-synaptic cell is full of small vesicles
 When an action potential arrives in the terminal it
stimulates the opening of calcium channels in the
terminal membrane. As a consequence, calcium ions
flood into the cell and cause the synaptic vesicles to
release their contents into the synaptic cleft.
 Binding of neurotransmitter molecule produces a change in
the three-dimensional shape of the receptors that opens a tiny
intrinsic pore in the protein.
 Major neurotransmitters:

 Amino acids: glutamate, aspartate, D-serine, γ-aminobutyric

acid (GABA), glycine
 Monoamines and other biogenic amines: dopamine (DA),
norepinephrine (noradrenaline; NE, NA), epinephrine
(adrenaline), histamine, serotonin (SE, 5-HT), melatonin
 Others: acetylcholine (ACh), adenosine, anandamide, nitric
oxide
DISORDERS RELATED TO CHEMICAL SYNAPSES
 the inherited neuromuscular disorder, myasthenia
gravis(deficency of enzyme that breaks down
acetylcholine), occurs when the body produces
antibodies to the acetylcholine receptors on muscle
fibres.
 Epilepsy : decrease in the efficiency of inhibitory
transmission in the brain, leading to over-excitability of
networks of neurons.
 There is some evidence that the major psychiatric
conditions, depression and schizophrenia, involve
disorders of synapses in which serotonin and dopamine,
respectively, act as neurotransmitters.
 SUMMARY
 What is cell adhesion and its role
 Types of cell adhesion

 Cell adhesion and its molecules (CAM)

integrin, selectin, cadherins and immunglobulin

superfamily
 Cell Junction

gap junction, septate junction

anchoring junction (adherens and focal ) and (desmosomes
and hemi-desmosomes)
Gap junction plasmadesmota and chemical synapses
 BIBLOGRAPHY
 Bruce Alberts, Dennis Bray, Karen Hoplein, Alexander
Johnson, Julian Lewis, Martin Raff, Keith Roberts and
Peter Walter. (2004). “Molecular biology of the cell” ,
Ed:4, Garland science publications, New York,
 Geoffery M. Cooper, Robert E. Hausman (2009). “The
Cell A Molecular Approach”, Ed:4, ASM Press and
Sinauer Associates, Inc.
 Gerald Karp (2002) “Cell and Molecular Biology
Concept and Experiment”, Ed: 3, page no: 258-268
THANK YOU