cellular interaction cellular interactions

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cellular interactions chapter 20 tissues cellular interaction in some organisms, cells interact to form defined tissues extracellular matrix allows for cellular interaction extremely important in certain tissues connective tissue epithelial tissue epidermis dermis extracellular matrix ECM - present in pretty much all animals evolved in some ancestor of the animals sponges mesohyl basic ECM elements type IV collagen spongin laminins what about plants? special ECM cell wall matrix ECM fibers collagens fibrous glycoproteins most abundant protein in humans very strong structure triple helix arranged in staggered array overlap 25% 3 helical polypeptides (sinistral) collagen molecule (dextral triple helix) overlapping collagen fibril mature collagen fiber

Transcript of cellular interaction cellular interactions

Page 1: cellular interaction cellular interactions

cellular interactions

chapter 20

tissues• cellular interaction

• in some organisms, cells interact to form defined tissues

• extracellular matrix• allows for cellular

interaction• extremely important in

certain tissues• connective tissue• epithelial tissue

epid

erm

isde

rmis

extracellular matrix• ECM -

• present in pretty much all animals• evolved in some ancestor of the animals

• sponges• mesohyl • basic ECM elements

• type IV collagen• spongin

• laminins• what about plants?

• special ECM• cell wall matrix

ECM fibers• collagens

• fibrous glycoproteins• most abundant protein

in humans• very strong• structure

• triple helix• arranged in

staggered array• overlap 25%

3 helical polypeptides (sinistral)

collagen molecule (dextral triple helix)

overlapping collagen fibril

mature collagen fiber

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ECM fibers• collagens

• types I-XIX• I-III most common in humans• IV - not fibrillar

• spongin matrix in sponges• cuticle of nemata• bone• cartilage• type III - reticular fibers

• branching network

collagen problems• collagen-related diseases

• type I (osteogenesis imperfecta)

• type II (dwarfism)• type IV

• Alport syndrome• kidney disease

(glomerular nephritis)• blindness (ocular lesions)• hearing loss

• Ehlers-Danlos syndrome• hyperflexibility / extensible

skin

ECM fibers• elastic fibers

• elastin• cross-linked into network

• provide elastic strength• important for organs that stretch

elastic fiber

fibronectin• fibronectin structure

• glycoprotein found in nearly all animal connective tissue • two nearly identical polypeptides• can bind to cells and ECM

COOH

COOH

H2N

H2NFibrin-binding domains

heparin-binding domain

cell-binding domain

collagen-binding domain

S-S S-S

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cell interaction• integrins

• receptors with α and β subunits• each with several domains• many possible

configurations of 26 known subunits

• contain relatively short transmembrane domain

• conformations• inactive - bent• active - unbent / legs apart• can adopt many different

active configurations

α subunitβ subunit

β-propellerβ-I domain

αI domain

interaction with cells• integrins

• cell-binding sites in extracellular proteins• RGD - (arginine-glycine-aspartic acid) recognized• integrin binds with RGD sequence

• two main functions• adhesion of cells to substrate• transmission of signals from external environment

• β subunits• three main classes: β1, β2, β3

• clotting• fibrinogen (RGD sequence) binds to integrin• clot busters - competitive inhibitors

proteoglycan complexes• proteoglycans

• core protein• GAGs (glycosaminoglycans)

• repeating disaccharide structure• cushion cells, help resist crushing

laminin• laminins

• glycoproteins - triple helix (like collagens)• many diverse forms (little homology)• form web-like networks

• resistant to tensile force

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basement membrane• basement membrane

• basal lamina• flattened layer of ECM

• ECM secreted by fibroblasts• reticular layer

• lamina reticularis - reticular fibersepithelial cellshemidesmosome

basal lamina

reticular lamina

basement membrane• basal lamina

• 4 main functions• structural foundation for

epithelium• selective membrane• facilitate access to proteins• serve as guide for

developing neurons

basal lamina• Collagen IV • Laminins• Nidogens (entactins)• Perlecan

(proteoglycan)

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collagens - (glycoprotein) - dextral triple helix of 3 sinistral

alpha helices - high tensile strength - lots of kindselastic fibers - cross-linked networks of elastin

and fibrillin - allow organs to stretch and recoilproteoglycans - - huge protein-GAG complexes - serve as cushioning - form hydrated gelsfibronectin - (glycoprotein) - two identical polypeptides -

homodimer - bind to integrins - can bind to cells and to ECM fibers - important in migration of cells

- anchors cells to proteoglycans or collagen

laminins - (glycoprotein) - triple helix of 3 linked polypeptides - high tensile strength - along with collagen IV, comprises

basis for basal laminaentactin - (glycoprotein) - connects collagen and laminin

networks - web of collagen IV and laminins

connected by entactinintegrins - - heterodimers - attached to PM - bind to various ECM elements - act as cell receptors

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cell-ECM junctions• hemidesmosomes

• different class - β4

• link to intermediate filaments• dense plectin plaque

• linked to ECM by integrins • can be disassembled and

reassembled

cell-cell junctions• junction complex

• found on lateral aspect of plasma membranes

• comprise several types of junctions• tight junctions

• function• paracellular transport• creates membrane polarity:

apical, basal• membrane domains• prevent movement of proteins

between domains

cell-cell junctions• tight junctions

• complex collections of proteins• transmembrane proteins

• claudins• occludins• junctional adhesion molecule (JAM)

• polarity proteins• cytoskeletal proteins• signaling proteins

cell-cell junctions• adherens junctions

• link adjacent cells• located just basal to tight

junctions• transmembrane receptor

proteins• cadherin dimers

• bind to identical cadherins on neighboring cells

• anchor proteins (catenins)• link to actin bundles

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cell-cell junctions• septate junctions

• only in invertebrates• similar in function to tight junctions• located basal to adherens junctions

cell-cell junctions• desmosomes

• cytoplasmic plaques• inner dense plaque• outer dense plaque• connected to

intermediate filaments• main function:

• link cells together• important for cells

exposed to physical stress

cell-cell junctions• junction complexes

• tight junctions• adherens junctions• desmosome• hemidesmosome• (gap junction)

cell-cell communication

hydrophilic channel

cell membrane

cell membrane

cytoplasm

cytoplasm

connexon• gap junctions• analagous to

plasmodesmata• vertebrates

• connexon (2)• connexins (6)

• invertebrates• innexon (2)

• innexins (6)

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cell-cell communication• plasmodesmata

• intercellular cytoplasmic channels • desmotubule

• trapped portions of ER• passage of materials limited

• size constraints• interconnect protoplasts

• symplast cell wall

plasma membrane

Cell wall

Microfibril

Cellulose microfibrils in a plant cell wall

Cellulose molecules

β Glucose monomer

10 μm

0.5 μm

plant cell walls • comparative cell wall composition

• for bacteria - mainly peptidoglycan• for fungi - chitin• for plants cellulose

• cell wall matrix• microfibrils• proteins• pectin• hemicelluloses

cell wall matrix• microfibrils

• arranged in radial arrangement• restrict cell expansion

• cell elongation• influx of water

• increases cell volume• added by cellulose synthase

Cellulose microfibrils

Nucleus

Elongation

Vacuoles

5 µm

microtubule

cellulose synthase complex

microfibril

cell wall matrix• composition of cell wall

matrix• hemicellulose

• highly branched• crosslinked to microfibrils

• pectin• negatively charged

galacturonic acids• form a gel

• microfibrils• glycoproteins

pectin

cellulose microfibril

hemicellulose

soluble protein

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• layers• middle lamella (outer layer of pectin)• primary cell wall

• more flexible, laid down first • secondary cell wall

cell wall matrix

middle lamella

plasma membrane

primary cell wall

cell wall matrix• lignin

• used to stiffen and strengthen cell walls• 2nd most abundant organic polymer• hydrophobic polymer

• p-coumaryl alcohol • coniferyl alcohol• sinapyl alcohol