3 JunctAdhesionECM Part 2

Gap junction
One connexon is made up of six connexin subunits

Homo- and heteromeric assembly
One gap junction can contain a cluster of a few to many thousands of connexons
Bio 3HH3 Term II 2012
Slide 1
Gap junction
The permeability of gap junctions can be regulated (effect of the neurotransmitter dopamine in neurons)
Pre-treatment
Post-treatment
Slide 2
Occluding junction
Two types
Tight junctions (vertebrates) Septate junctions (invertebrates)
Restrict diffusion of membrane components Help maintain the polarity of epithelial cells Two transport mechanisms where tight junctions are involved
Transcellular transport Paracellular transport
Slide 3
Tight junction
Intestine epithelial cells
Slide 4
Lodish et al., 6-9
Transcellular and paracellular transport
Transport of glucose across epithelial cells of the small intestine is mediated by specific membrane proteins in the apical and basolateral regions.
Slide 5
Tight junctions
Composed of thin bands of plasma membrane proteins in a cell and are in contact with similar bands on adjacent cell.
Slide 6
Alberts et al., 19-5
Tight junction components

Occludin and Claudin are two major components of tight junction. claudin gene family encodes numerous homologous proteins that exhibit distinct tissue-specific expression pattern. Recently a group of Junction Adhesion Molecules (JAMs) have been identified that contain a single transmembrane domain and are component of tight junction.
Slide 7
Tight junction components
Cell-cell interactions are mediated through the extracellular domains of Occludin, Claudin, and JAM.
Slide 8
Tight junction: A model
Slide 9
Alberts et al.,
Tight junction
Role of Ca2+
It has been demonstrated that Ca2+ plays an important role in the formation of tight junctions. Experiments with MDCK cells
Low Ca2+ --> no tight junction between cells High Ca2+ --> tight junctions form within an hour and cells become impermeable to fluids and salts.
MDCK: Madin-Darby canine kidney
Slide 10
Septate junction
Sinuous is a Drosophila claudin required for septate junction organization (J Cell Bio 2004, vol. 164, 313-323) Main occluding junctions in invertebrates Distinct morphology from tight junctions An example of septate junction protein is Disc Large in Drosophila melanogaster
Slide 11
Alberts et al.,
Summary of cell junctions
Slide 12
Anchoring junction
Connects a cell either to its neighbors or to the ECM Provides physical support to cells Particularly important in cells that are subjected to mechanical stress such as heart, muscle, and epidermis Some contain intracellular signaling proteins and mediate cell-cell signaling events Alberts et al.,
Slide 13
Anchoring junction
Composed of two classes of proteins
Intracellular anchor proteins Transmembrane adhesion proteins
Slide 14
Alberts et al.
Anchoring junction
Two types
Cell-cell junction (Adherens junction and desmosomes) Cell-matrix junction (Focal adhesion and hemidesmosomes)
Slide 15
Anchoring junction
Two functionally different forms involving transmembrane adhesion proteins
Cadherins (cell-cell adhesion) Integrins (cell-matrix adhesion)
Slide 16
Alberts et al., 19-9, 19-12
Anchoring junction: Adherens type

Connects bundles of actin filaments from cell to cell In epithelial tissues, adherens junctions take the form of continuous adhesion belt (or zonula adhesion or ZA), just below the tight junctions The network of proteins and macromolecules that connect and are part of adherens junctions play a fundamental role in animal morphogenesis, i.e., changes in shape by movement of epithelial cells
Slide 17
Adherens junctions between epithelial cells in small intestine
Adherens junction: Role

Formation of an epithelial tube
Slide 18
Alberts et al.
Adherens junction
Slide 19
Cadherins in cell junctions

Cadherin superfamily includes members of the six subfamilies, distinguished on the basis of protein domain composition, genomic structure, and phylogenetic analysis
Type I and II Desmosomal cadherins Desmocollins Desmogleins Protocadherins Flamingo
Slide 20
Desmosomes and Hemidesmosomes
Desmosomes
! are button-like points of intercellular contact that rivet cells together ! serve as anchoring sites for IFs ! mediate cell-cell adhesion ! are formed by desmosomal cadherins (desmoglein and desmocollin) and intracellular anchor proteins plakoglobin and desmoplakin
Hemidesmosomes
! are half-desmosomes ! connect cells to ECM through IFs ! mediate cell-matrix adhesion
Slide 21
Slide 22
Alberts et al.

Hemidesmosomes are halfdesmosomes. Like desomosomes, hemidesmosomes also connect to IFs and act as rivets to distribute tensile or shearing forces through an epithelium. One difference between hemidesmosomes and desomosomes is that while desmosomes connect adjacent epithelial cells, hemidesmosomes connect cells to the underlying basal lamina.
Slide 23
Alberts et al.
Cell adhesion
Protein families that mediate cell-cell and cell-matrix adhesion in eukaryotes include
Cadherins (many cell types) Selectins (leukocytes) Neural CAMs (neurons) Integrins (many cell types) Fibronectins (fibroblasts and many other cell types)
Slide 24
Cell adhesion
Slide 26
CAMs
Slide 27
CAMs in leukocytes
The cell adhesion properties of leukocytes (white blood cells) are regulated such that they circulate as unattached in bloodstream but selectively adhere at sites of infection in tissues. Selectins are transmembrane glycoproteins that mediate leukocyte-vascular cell interactions. Selectins contain an extracellular Ca2+-dependent lectin domain that plays an important role in binding leukocytes to endothelial cells lining blood vessels. [lectin domain is a sugar-binding domain]
Slide 28
CAMs in leukocytes
There are at least three types of selectins
L-selectin (on leukocytes) P-selectin (on blood platlets and endothelial cells) E-selectin (on endothelial cells)
The extracellular lectin domain in these proteins binds to a specific oligosaccharide on another cell.
Slide 29
CAMs in leukocytes
Slide 30
CAMs in leukocytes: Function

Selectins act together with integrins to facilitate migration of leukocytes out of the bloodstream into the site of inflammation. Selectin-mediated adhesions are weak and reversible because of low affinity binding between the receptor (lectin domain) and the ligand (carbohydrate). The rolling of leukocytes continues until cells activate integrins. Integrin-mediated adhesions are strong.
Slide 31
CAMs in leukocytes: Function
MOVIE
Slide 32
Neural CAM: N-CAM

The Ca2+-independent cell adhesion molecules (CAMs) belong to the immunoglobulin (Ig) superfamily of proteins and include neural CAMs. One type of neural CAMs, N-CAM, is particularly important in vertebrates. It is expressed by a variety of cell types, including most nerve cells and plays an important role in the differentiation of muscle, glial, and nerve cells. N-CAM is the most prevalent of the Ca2+-independent cell-cell adhesion molecules in vertebrates. Like cadherins, N-CAM is thought to primarily function as homophilic dimers.
Slide 33
Neural CAM: N-CAM isoforms

In vertebrates there are numerous isoforms of N-CAM, all generated by alternative splicing of an RNA transcript from a single gene. In all forms, the extracellular part contains five Ig-like domains. The N-CAM isoforms also differ in glycosylation.
Some carry an unusually large quantity of sialic acid
Slide 34
Neural CAM: Fasciclin III

Fasciclin III (FAS3) is an N-CAM-like protein in Drosophila that is transiently expressed in some motor neurons and their innervating target muscle cells. FAS3 mediates synaptic connections by a homophilic matchmaking mechanism.
fas3 mutant neurons fail to recognize their muscle targets Forced expression of FAS3 in neurons that normally do not express FAS3 causes them to synapse with FAS3-expressing muscle cells.
Slide 35
Cadherins
Cadherins are a class of cell adhesion molecules (CAMs) in eukaryotic tissues. Cadherin superfamily members are Ca2+ dependent transmembrane proteins with broad range of functions including cell-cell adhesion and cell signaling Cadherin-mediated cell junctions are involved in cell polarity and cell migration Abnormal function of cadherins is linked to many human malignancies.
Slide 36
Cadherins
Most cadherins are single-pass transmembrane proteins characterized by the presence of distinctive cadherin repeat sequences in their extracellular domain. ~700-750 amino acids Extracellular domain fold into 5 or 6 cadherin repeats (classical) Ca2+ ions positioned between each pair of repeats
Slide 37
Cadherin function: Role of Ca2+

In the absence of the Ca2+, the extracellular part of cadherin is floppy and gets degraded by proteolytic enzymes. As the amount of extracellular Ca2+ increases, the extracellular part of cadherin dimer extends from the cell surface and can bind to a cadherin dimer on a neighboring cell. Three Ca2+ ions bind between each successive domain pair. Ca2+ is positioned between repeats to form a stiff rodlike structure
Slide 38
Cadherin function: Role of Ca2+
Slide 39
Cadherin superfamily
Cadherin superfamily includes members of the six subfamilies, distinguished on the basis of protein domain composition, genomic structure, and phylogenetic analysis
Type I Classical Type II Desmosomal cadherins
Desmocollins Desmogleins
Protocadherins found in the brain/neurons Flamingo seven pass transmembrane Type I and II cadherins are linked to actin filaments Desmosomal cadherins are linked to intermediate filaments
Slide 40
Cadherin superfamily
Cadherins are expressed in both invertebrates and vertebrates. Virtually all vertebrate cells appear to express one or more cadherins. Classical cadherins all contain five extracellular cadherin repeats of approximately 110 amino acids.
Slide 41
Classical Cadherins
Type 1
! E-Cadherin- present on many types of epithelial cells/parts of the brain. ! N-Cadherin- present on neural, muscle & lens cells/fibroblast. ! P-Cadherin- present on placenta & epidermis.
Type 2
! VE-Cadherin- present on endothelial cells
Slide 42
Classical cadherins: E-Cadherin

Among the best characterized cadherins in mammals. First expressed in mammalian development In mouse embryo (~8 cell stage), it is expressed in blastomeres and causes them to become tightly packed and joined by intercellular junctions.
Slide 43
Cadherins in development
The crucial roles of cadherins in vertebrate development is recognized by their dynamic presence in cells that correlates with major morphogenetic events in which tissues segregate from one another (formation of cell layers) Example: Separation of neural tube from the ectoderm, mediated by Ecadherin and N-cadherin expressing cells
Overlaying ectoderm
E-cadherin
Neural tube
N-cadherin Formation of chick neural tube

Slide 44
Specificity of interactions
Which of these mechanisms are involved in cadherine-mediated cell-cell adhesion?
Homophilic binding? Heterophilic binding? Linker-dependent binding?
Slide 45
Generation of Cell-Cell ddhesions
Slide 46
Mechanism of cell-cell adhesion
Cadherins usually link cells by the homophilic adhesion mechanism Experiments to demonstrate specificity
Cultured fibrobalst cells (L cells) do not express cadherin or adhere to one another. when transfected with DNA encoding E-cadherin, adhere to each other. If L cells are transfected with two different cadherins, they sort out and aggregate separately. If L cells expressing different amounts of the same cadherin are mixed together, they sort out and aggregate separately.
Both qualitative and quantitative differences are important.

Slide 47
Slide 48
Promiscuity of interactions
Recent studies have shown that although homophilic binding is preferred, many type I cadherins can interact with other type I cadherins (e.g., N- and E-cadherins). Likewise type II cadherins will co-aggregate. Despite the cross-reactivity within the same subfamily, the binding specificities of type I and type II cadherins are orthogonal.
Graded affinities for members within same class
Slide 49
Structural basis of adhesion

Type I and type II cadherins each contain five extracellular cadherin repeats (EC1 - EC5). QUESTION Which of the ECs mediates binding and provides specifity?
Slide 50
Structural basis of adhesion

Domain swapping experiment
Behavior of the chimeric proteins in cell aggregation assays The EC1 domain (at the N-terminus) and/or regions close to it is the primary site for mediating adhesion and specificity
E-Cad EC1
N-Cad
Slide 51
Cadherins in adherens junction

Most cadherins function as transmembrane adhesion molecules that indirectly link the actin filaments. The cytoplasmic tail of cadherins interacts with intracellular anchor proteins called catenins. This interaction is essential for efficient cell-cell adhesion. Catenins
! a group of Intracellular anchoring proteins ! abundant at adherence junction ! involves in the regulation cell-cell adhesion
Slide 52
p120ctn regulates E-Cadherin turnover and Stability
Nucleus
Source: Andl, C.D. and Rustgi, A.K. 2005 Cancer Biol. & Ther.
Slide 53
p120ctn regulates E-Cadherin turnover and Stability
Source: Xiao, K. et al., 2006 BBA.
Interaction of E-Cadherin and EGFR regulates Cell-Adhesion
Slide 55
Interaction of E-Cadherin and EGFR regulates Cell-Adhesion
Slide 56
Cadherins in signaling
Slide 57
Old vs. New Model
Source: Benjamine, J & Nelson , W. Seminars in cancer Biology 2008 Bio 3HH3 Term II 2012
Slide 58
Integrins
Integrins are a large family of transmembrane proteins that play important role in cellmatrix Integrins are involved in bidirectional signaling Integrins interact with several types of ligands (e.g., laminin, fibronectin)
Slide 59
Integrins: Structure
An integrin is composed of two noncovalently associated transmembrane glycoprotein subunits called ! and ". The binding of ligand depends upon Ca2+ or Mg2+ divalent ions.
Slide 60
Slide 61
Integrins: Role
Besides adhesion, integrins also play crucial role in cytoskeletal organization, cell signaling and motility. Experiments in various organisms have shown that disruption of integrin function frequently causes lethality The importance of integrins in human is demonstrated by numerous disorders that are associated with disruption of integrin function such as thrombosis, atherosclerosis, cancer, and chronic inflammatory diseases.
Slide 62
Integrins
Role of " Integrin (myospheroid) in Drosophila wing
Wild type
Mutant
Slide 63
Integrins: Diversity
Multiple genes encoding subunits Variety of heterodimers
Humans contain 18 ! and 8 " subunits that combine to produce at least 24 different heterodimers, each of which can bind to a specific ligand.
Slide 64
Integrin function
While the extracellular domains of integrins bind to a wide variety of ligands (e.g., fibronectins and laminin), the intracellular domains anchor to cytoskeletal proteins. In this manner, the exterior and interior of a cell are physically linked (allows bidirectional signal).
Slide 65
Integrin activation & signaling

In their resting state, integrins bind ligand that activate them with low affinity. A cellular signal induces conformational change in the cytoplasmic domain of integrin (mediated by a cytoskeletal actin-binding protein Talin) that propagates to the extracellular domain (inside-out signaling). The integrins are now transformed from a low- to highaffinity ligand binding state. The activated integrins may undergo clustering (homotypic oligomerization) that initiates outside-in signaling. The outside-in signaling then regulates a variety of cellular responses.
Slide 66
inside-out signaling
Outside-in signaling
Slide 67

Inside-out signaling
Cellular stimulation induces conformational change in talin that exposes talin head domain.
Slide 68
Qin et al., PLoS Biology, 2004

The talin head domain binds to the " cytoplasmic tail which displaces the ! tail from its complex with the " tail. The binding of talin to the " cytoplasmic tail leads to an unclasping and a membraneassociated structural change. The unclasping initiates the opening of the integrin C-terminus stalks which is necessary for the switchblade shift of the extracellular head piece from the bent to the extended form.
Slide 69
"
Qin et al., PLoS Biology, 2004

Electron micrographs of integrin conformation in the presence/absence of RGD peptide
The inside-out signaling protects cells from unwanted adhesion (e.g., aggregation of blood cells) that could have profound pathological consequences.
Slide 70

Extracellular signals (such as G-protein-coupled receptors and receptor tyrosine kinase) can induce conformational change in talin and thereby activating integrins Loss of talin function abolishes integrin activation
Slide 71

Outside-in signaling
The outside-in signaling initiates various cellular responses including cell adhesion and migration. This is mediated by integrin clusters that result in the formation of highly organized intracellular complexes known as focal adhesions. Focal adhesions are connected to the cytoskeleton and incorporate a variety of molecules including cytoskeletal proteins and signaling molecules. This facilitates protein-protein interactions and propagation of the intracellular responses.
Slide 72
Slide 73
Localization of integrin clusters
!-Actin
!-Vinculin
Slide 74
Localization of integrin clusters
A fibroblast cultured cell Green: actin filaments Red: proteins located at sites where cell attaches to the substratum
Slide 75
Focal adhesion sites

Enable cells to bind to ECM through transmembrane adhesion proteins of integrin family. The extracellular domains of integrins bind to ECM, while their intracellular domains bind indirectly to bundles of AFs Can be involved in signaling events mediated by focal adhesion kinase (FAK) that allows communication between the ECM and inside of the cell
Slide 76
Focal adhesion proteins

Focal adhesion proteins that are involved in establishing and maintaining the integrincytoskeleton linkage
! Integrin-bound proteins that directly bind actin (e.g., talin) ! Integrin-bound proteins that indirectly associate with/regulate the cytoskeleton (e.g., integrin-linked kinase or ILK, FAK) ! Non-integrin-bound actin-binding proteins (e.g., vinculin) ! Adaptor and signaling proteins that regulate above proteins
Slide 77
Focal adhesion proteins

FAKs are protein tyrosine kinases that bind to "-integrins and phosphorylate many cellular proteins at the focal adhesion sites and together with Src tyrosine kinases relay the signal inside the cell FAKs are not necessary for the formation of initial nascent FAs or their initial connection with actin filaments FAKs are required to stabilize the linkage between FAs and actin filaments FAs appear to play an essential role in promoting FA turnover ILKs are multi-domain adaptor proteins that bind directly to " -integrins, and associate indirectly to with actin. In the absence of ILK, FA formation is severely delays. Once formed, FAs are smaller in size and poorly linked to a disorganized actin cytoskeleton
Slide 78
The ECM
What is the role of ECM?
! ECM plays an essential role in the assembly of tissues and organs
What is ECM?
! ECM is a complex interdigitating meshwork of proteins and polysaccharides secreted by cells into spaces between them
Slide 79
The ECM
Slide 80
Lodish et al., 6-1
The ECM
In addition to providing structural integrity to tissues, ECM also plays an essential role in many cell communication events. These lead to various changes such as cell proliferation, cell survival, and cell migration.
Slide 81
The ECM
The ECM of epithelial sheets
! Proteoglycans
" Hyaluronan, Chondroitin sulfate, Heparin, Keratan sulfate
! Basal lamina
The ECM of nonepithelial tissues

! e.g., connective, muscle, and neural tissues ! Collagens: Major fibrous proteins in the ECM of connective tissues (such as tendon and cartilage)
Fibronectins
Slide 82
The components of ECM

Three highly abundant ECM molecules are ! Proteoglycans ! Collagens ! Soluble matrix proteins
Slide 83
Proteoglycans
Proteoglycans are a group of glycoproteins that contain covalently linked specialized polysaccharide chains called GAGs (glycosaminoglycans).
Protein core
GAG
GAGs are long linear polymers of specific repeating disaccharides
Uronic acid or D-galactose

N-acetylglucosamine or N-acetylgalactosamine
Slide 84
Glycoproteins: A comparison
Proteoglycans At least one sugar side chain must be GAG As much as 95% carbohydrate by weight Mostly unbranched long GAG chains Other glycoproteins 1-60% carbohydrate by weight Mostly short, branched oligosaccharide chains
Slide 85
Glycosaminoglycan (GAG) chains

The four main groups of GAGs are Hyaluronan
! Disaccharide unit: GlcUA-Glu(NAc)
Chondroitin sulfate Heparin (hypersulfated form of heparan sulfate) Keratan sulfate

! Disaccharide unit: [GlcUA-SO4]-[Glu(NAc)-(SO4)2] ! Disaccharide unit: [Gal- SO4]-[Glu(NAc)-SO4]
GlcUA: Glu(NAc): Gal(NAc):
! Disaccharide unit: GlcUA-[Gal(NAc)-SO4]
glucuronic acid (uric acid) N-acetylglucosamine N-acetylgalactosamine

Slide 86
Slide 87
Aggrecan: predominant proteoglycan in cartilage gives gel-like properties and resistance to deformation essential for distributing the load in weight-bearing joints
Slide 88
Hyaluronan
AKA hyaluronic acid or hyaluronate Simplest GAG, nonsulfated Very large chain length (~25,000 disaccharide units) Generally not covalently linked to any core protein Role
! Resists compressive forces in tissues and joints ! Important as a space filler during embryonic development and to force a change in the shape ! Facilitates cell migration
Slide 89
Proteoglycans
Modification of GAG chains can determine function of proteoglycans (e.g., addition of sulfate groups) Heparin
! Used as an anticlotting drug because of its ability to activate a natural blood clotting inhibitor antithrombin III.
Slide 90
Proteoglycans: Function
Four-suger linker (Xyl-Gal-Gal-Glu) is attached to the serine (or asparagine) residues in a core protein
Chondroitin sulfate: D-glucoronic acid and N-acetyl-D-galactosamine Heparan sufate: D-glucosamine and N-acetyle-D-glucosamine Keratan sulfate: D-galactose and N-acetyle-D-glucosamine
Slide 91
Experiments in several model organisms (e.g., Drosophila melanogaster, C. elegans, and mice) have shown that proteoglycans play crucial roles during development. In C. elegans, disruption of proteoglycan synthesis leads to defects in the development of hermaphrodite vulva (an organ required for mating and laying fertilized eggs).
Slide 92
In the soil-nematode C. elegans failure to modify some proteins (by addition of GAG chains) can cause morphological defects in the vulval tissue sqv-3
Wild type
sqv-3 mutant
Slide 93
ECM in tissues
Epithelial tissues contain very little ECM (only a thin mat called basal lamina) Connective tissues, on the other hand, are rich in ECM (mostly collagen)
Slide 94
The basal lamina

Thin (40-120 nm) mat of specialized ECM. Surrounds all epithelial cell sheets and tubes as well as individual muscle cells, fat cells, and schwann cells. Largely synthesized by cells that rest on it. Mostly contains type IV collagen, heparan sulfate proteoglycan perlecan, and the glycoproteins laminin and nidogen (also called entactin ).
Slide 95
Basal lamina in epithelia

Basement membrane is a structure in thin epithelia (e.g., skin) that consists of basal lamina and a collagen containing layer. One side of the basal lamina is linked to cells by adhesion receptors whereas the other side is anchored to the adjacent connective tissue. This anchoring is mediated by collagen.
Slide 96
The basal lamina
Scanning EM of the basal lamina in the cornea of a chick embryo. E: epithelial cell BL: basal lamina C: collagen fibrils
Slide 97
Role of the basal lamina

Molecular filter in the kidney Selective barrier to the movement of cells (prevent fibroblasts in the underlying connective tissue from making contact with the epithelial cells) Important in tissue regeneration after injury (by providing a scaffold for regenerating cells). Example: wound healing Instructive role of basal lamina in regeneration ! Example of the frog neuromuscular junction ! Localization of AChRs at the neuromuscular junction
Slide 98
The basal lamina: Examples
BLOOD URINE
Slide 99
The basal lamina: A model
Slide 100
Components of basal lamina

The components of basal lamina include the following four major components
! Type IV collagen ! Laminins ! Nidogen (also called Entactin ) ! Perlecan
Slide 101

Type IV collagen
! A major component of all basal lamina, forms 2D network ! All collagens are trimeric proteins made from three a chains that could either be identical (homomeric) or different (heteromeric)
Slide 102

Laminins
! Heterotrimeric proteins that form 2D network with type IV collagen and integrins ! Possess various domains that interact with collagen, other matrix components, cell surface receptors, and ECM signaling molecules (multiadhesive properties)
Slide 103

Nidogen (or Entactin)
! A rodlike molecule that cross-links type IV collagen and laminin
Perlecan
! Binds to and cross-links many ECM components and cell surface molecules
Slide 104
Fibronectins
Found in all vertebrates Produced by cells such as fibroblasts and hepatocytes. Help attach cells to the matrix by binding to other ECM components (such as collagens) Because of their role in cell-matrix adhesion, fibronectins control migratory behavior of many cell types.
! Morphogenetic changes during embryonic development ! wound healing by promoting blood clotting and movement of immune cells such as macrophases and others
Tumorigenic cells lack fibronectins

Slide 105
Fibronectins
Dimer formation, chains are linked by two S-S bonds Each chain is approximately 2500 amino acids long (extremely large!) Six domains Three types of repeat sequences Fibronectins differ from each other in the number of repeat sequences, all encoded by the same gene The alternative spliced form, lacking EIIIA and EIIIB (green boxes) exons, is secreted by hepatocytes (does not adhere tightly to cells)
Slide 106
Fibronectins: RGD sequence

The tripeptide sequence RGD (ArgGly-Asp) plays crucial role in integrin binding
Slide 107

3 JunctAdhesionECM Part 2

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Gap junction

One connexon is made up of six connexin subunits

Bio 3HH3 Term II 2012

Intestine epithelial cells

Bio 3HH3 Term II 2012

Lodish et al., 6-9

Transcellular and paracellular transport

Bio 3HH3 Term II 2012

Alberts et al., 19-5

Tight junction components

Tight junction components

Bio 3HH3 Term II 2012

Tight junction: A model

Bio 3HH3 Term II 2012

Bio 3HH3 Term II 2012

Summary of cell junctions

Bio 3HH3 Term II 2012

Bio 3HH3 Term II 2012

Bio 3HH3 Term II 2012

Bio 3HH3 Term II 2012

Bio 3HH3 Term II 2012

Alberts et al., 19-9, 19-12

Anchoring junction: Adherens type

Adherens junctions between epithelial cells in small intestine

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Adherens junction: Role

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Bio 3HH3 Term II 2012

Cadherins in cell junctions

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Desmosomes and Hemidesmosomes

Desmosomes and Hemidesmosomes

Bio 3HH3 Term II 2012

Desmosomes and Hemidesmosomes

Bio 3HH3 Term II 2012

Bio 3HH3 Term II 2012

Bio 3HH3 Term II 2012

Bio 3HH3 Term II 2012

CAMs in leukocytes: Function

CAMs in leukocytes: Function

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Neural CAM: N-CAM

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Neural CAM: N-CAM isoforms

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Neural CAM: Fasciclin III

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Cadherin function: Role of Ca2+

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Cadherin function: Role of Ca2+

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Bio 3HH3 Term II 2012

Classical cadherins: E-Cadherin

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N-cadherin Formation of chick neural tube

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Bio 3HH3 Term II 2012

Generation of Cell-Cell ddhesions

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Both qualitative and quantitative differences are important.

Bio 3HH3 Term II 2012

Bio 3HH3 Term II 2012

Structural basis of adhesion