The Biology of the Basement Membrane Zone

4,864 views 151 slides Mar 14, 2015
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About This Presentation

It is a critical interface between the epidermis and dermis and is a highly specialized structure that allows for communication between different cell types.
Examination of BMZ/Structure of BMZ/Origin of BMZ/Function of BMZ/Examples of Some diseases affecting BMZ

Size: 7.79 MB
Language: en
Added: Mar 14, 2015
Slides: 151 pages

Slide Content

OVERVIEW
*Examination of BMZ
*Structure of BMZ
*Origin of BMZ
*Function of BMZ
*Examples of Some diseases affecting BMZ

???????
*Basement Membrane
*Dermo –Epidermal Junction (DEJ)
*Basal lamina
*Basement Membrane Zone (BMZ)

THE BASEMENT MEMBRANE ZONE
*It is a critical interfacebetween the epidermisand
dermisand is a highlyspecializedstructurethat
allows for communicationbetween different cell
types.

PAS-positive basement membrane.

EXAMINATION OF BMZ
*Relatively poorlydemonstratedwith eosinin H and E
preparations.

*As all basement membranes, it stainsstronglyfor
Glycoproteins and mucopolysaccharides by Periodic
acid schiffstain(PAS).
*It is also stained intensely with silvertechniques.

*The complexity& heterogeneityof BMZ can be
appreciated only at ELECTRONMICROSCOPIC
level.

The basement membrane zone (BMZ) integrates the epidermis
with the underlying dermis. On electron microscopy, the BMZ
has three layers: a central electron-dense region known as the
lamina densa and two regions of lower electron density to
either side of this central region.

Ultrastructure of basement membrane (×37,800).
(1, hemidesmosome; 2, lamina lucida; 3, lamina densa; 4,
sublaminadensa; 5, melanin; 6, tonofilaments)

BMZ
KIF/Hemidesmosome complex
(Basal keratinocyte)
Lamina lucida
Lamina densa
Sub lamina densa

KERATIN INTERMEDIATE
FILAMENTS
*Also called tonofilaments, it is comprising keratin
5&14.
*It is a finefilamentousstructures maintain the
intracellular architecture& organizationof basal cells.
*They course throughthe basalcells& insertedinto
the desmosome& hemidesmosome.

ATOMIC MASS UNIT
*The unified atomic mass unit (symbol: u) or dalton
(symbol: Da) is the standardunitthat is used for
indicating masson an atomicor molecularscale
(atomic mass).

*Onedaltonis approximately the mass of one nucleon
(either a single proton or neutron)
= 1.660538921(73)×10
−27
kg.

HEMIDESMOSOMES (HD)
*Numerous electron-denseplateslocated in the lower
regionof the plasmamembraneof the basalcells.

*It is closely resembling½of the desmosomeseen in
cell–cell junction but basedon chemicalcriteria, these
2 structures appear to be immunologicallydistinctive.

*Characteristicsof HD proteins has been aided by the
use of auto-antibodiespresented in serumsamples of
patients with bullouspemphigoid.
*As result of this, the antigens recognized by these
sera identified proteins ranging in mass from 165-
240kDa.
*These proteins are immunologically& structurally
distinct.

*Monoclonalantibodieshave been constructedto both
intracellular & extracellular regions of HD.

BPAG1
*It is a homodimerwith homologyto desmosomal
desmoplakin.
*It is generally believed that it is the majorcomponent
of the HD inner dense plaque.

PLECTIN
*It is another dimericdesmoplakinhomologue.
*Its tissue distribution is notlimitedto BMZ.

6 4 INTEGRIN
*They are largeclass of trans-membraneextra-
cellularmatrix binding proteins that provide cell
attachment & subsequent signaltransduction.
*It has a selective high affinity for laminin5.

TYPE XVII COLLAGEN (BPAG2)
*180kDa
*It is an unusual trans-membraneprt.
Collagenous extra-cellular
domain interact
with laminin5
Intra-cellulardomain
interact mainly
with BPAG1

LAMINA LUCIDA(LL)
*External to the plasma membrane
*25-50 nm in width.
*Contains the anchoringfilaments.

ANCHORING FILAMENTS
*Seriesof filaments traversingthe laminalucidafrom
the epidermal basalcells& insertinto the lamina
densa.
*Severalantigensforming anchoringfilamentproteins.

LAMININS
*Immunolocalizedto basallamina(= LL+LD).
*Numerous glycoproteinfamily with semirigid&
extendedstructures.

*It is hetrotrimetricmolecule, where each laminin
isoformconsisting of
alpha chain.
Beta chain.
Gamma chain.

*The 4extremitiesof the crosslikestructure contain
globulardomains, the 3 short arms contain extra
domain, approximately 20 nm from their free end.

LAMININ5
*Its generalstructureas lamininfamily.
*It has shortarmscomparing to other laminins.

*Its shapeis consistentwith its potential to be the
anchoringfilamentprotein.
*It has a high affinityfor integrins.
*It also bind to the NC-1 domain of type VIIcollagen
(the anchoring fibril protein).

LAMINA DENSA (LD)
*Appears as an electron-denseamorphous structure.
*20-50 nm in width.
*At high magnification, it has a granularfibrous
appearance.
*Account for 40-65%of totalbasementmembrane
proteins.

*Majorproteins componentis type IV collagen where it
appears as a filament of variable thickness which is
morphologicallydistinctfrom the collagenfibersin the
subjacentdermis.

TYPE IV COLLAGEN
*Immunolocalizedmainly to LD& also found in
anchoringplaque.
*It has a structurecloselyrelatedto the intracellular
or procollagenform, typical of all members of the
collagen protein family.

*The triplehelicalnatureof the aminoterminusof
type IV collagen is unique & has been designatedas
the 7-Sdomain.
*Covalentinteractions among 7-Sdomain of the type
IV collagen are the basis for the specializedfiber
formcharacteristic of basement membrane.

NIDOGEN
*It is a glycoproteinwith dumbbellconfiguration
localized to the LD.
*It is attached to one of the short arms of lamininat
the gamma 1 chain forming a stable complex.
*Nidogenaloneas well as laminin-nidogencomplex
specifically bind to type IVcollagen.

PERLECAN
*It is a Heparan sulfate proteoglycan.
*It consists of a coreproteinof various length with
differentnumbersof covalentlyassociated
glycosaminoglycanchains.

*High sulfatecontent makes this molecule with highly
negativecharge & hydrophilic.
*It swellwith hydration& have a major role in
determining which proteinsor ionscan transversethe
laminalucida& access the epidermal intracellular
spaces.

SUB LAMINA DENSA
*It’smajor component isanchoringfibrilswhich appear
as condensedfibrousaggregatesof typeVII
collagen.

ANCHORING FIBRILS
*Type VII collagen appears to have a major triple-
helicaldomainis approximately 450 nm in length.

*Type VII collagen is synthesized& secretedas
monomericprotein but rapidly dimerizesat the amino
terminals.
*These structures are proteolyticallycleavedafter
formation of the centrosymmetricdimer.
*The dimers then aggregates laterally to form the
anchoring fibrils.

*The complex NC-1 domain binds to laminin5& also to
componentsof the laminadensa.

*Many of the anchoring fibrilsinsertedtheir distal
endsinto electron-denseamorphous-appearing
structurescompletely independent of lamina densa,
known anchoringplaques.

ANCHORING PLAQUES
*The anchoring plaques are electron-densestructure
composed of type IV collagen & laminin.
*They are independentof laminadensa, & distributed
randomlyin the papillarydermisbelow lamina densa &
are inter-related by additional anchoring filaments.

REFERENCES
*Adel A. Al-GhamdiDermatology Department King
Fahd Hospital of university (Presentation).
*The Basement Membrane Zone-Making the
Connection Vidal MD, AAD.
*Google images.

THANK YOU
Tags
structure of bmz diseases affecting bmz function of bmz origin of bmz examples of some it is a critical interface between the epidermis and dermis and is a highly specialized structure that allows examination of bmz
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