Volume 72 • Number 6

The Dento-Epithelial Junction: Cell

Adhesion by Type I Hemidesmosomes in
the Absence of a True Basal Lamina
Marketta Hormia,*† Katsushi Owaribe,‡ and Ismo Virtanen†

Background: The junctional epithelium (JE) is a unique struc-

ture that makes contact with both a non-renewable hard tooth
surface and with a basement membrane (BM) facing the con-
nective tissue. Ultrastructurally, this attachment occurs through
hemidesmosomes (HD) and a basal lamina-like extracellular
matrix which, on the tooth side, is termed the internal basal
lamina. In this study we investigated the expression of basal cell
markers in the tooth-facing (TF) cells of JE.
Methods: Samples of healthy marginal gingiva were removed

B
by careful dissection. The expression of laminin-5 was used to asal cells of stratified epithelia rest
indicate TF cell preservation in double immunofluorescence on a basement membrane (BM)
labeling and confocal laser scanning microscopy. composed of laminins, entactin/
Results: The results show that integrin α6β4 and laminin-5 nidogen, type IV collagen, and sulfated pro-
colocalize unequivocally in the TF cells. The results also show teoglycans.1 In the dento-epithelial junc-
the specific expression of the basal cytokeratin 14 and the αv tion, however, epithelial cells are interposed
integrin subunit in the TF cells. All 3 major hemidesmosomal between 2 different extracellular matrices
components BP180, BP230, and HD1 antigen are likewise pre- (ECM), the so-called internal (IBL, tooth-
sent. On the other hand, type IV collagen, laminin-1/10, type facing) and external (EBL, connective tis-
VII collagen, and the BM proteoglycan perlecan are all absent sue-facing) basal laminae.2 This epithelial
from the dento-epithelial junction. layer that mediates the adhesion of the gin-
Conclusions: The results indicate that the epithelium-tooth gival tissues to the tooth surface is termed
interface is a unique structure wherein epithelial cells adhere by the junctional epithelium (JE).
means of bona fide hemidesmosomes to an epithelium-derived The ultrastructure of the dento-epithelial
extracellular matrix lacking most of the common BM compo- junction has been described in detail.2-4 The
nents. Moreover, TF cells differ from connective tissue facing JE cells are attached both to the IBL and to
(CTF) cells, not only by their cell surface molecules and their the EBL by means of specialized adhesion
production of extracellular matrix, but also by their cytoskele- devices termed hemidesmosomes (HD).5,6
tal architecture. J Periodontol 2001;72:788-797. While the EBL has an ultrastructure typical
of epithelial BM elsewhere, the IBL often
KEY WORDS shows an indistinct lamina densa and lacks
Epithelium/anatomy and histology; laminin; hemidesmosomes; anchoring filaments,2,3 known to consist of
epithelial attachment; tooth/anatomy and histology; laminin-5 and possibly of the extracellular
basement membrane. domain of BP180.5,6 The pattern of differ-
entiation markers distinguishes the JE from
* Institute of Dentistry, University of Turku, Turku, Finland. other areas of gingival epithelium. This
† Department of Anatomy, Institute of Biomedicine, University of Helsinki, Helsinki. unique phenotype is reflected, for instance,
‡ Unit of Biosystems, Graduate School of Human Informatics, Nagoya University, Nagoya,
Japan. in the cytokeratin (CK) expression,7-10 in
the glycosylation of cell surface mole-
cules,11-14 and in the expression cell sur-
face integrins.15-17 We previously showed16
that the hemidesmosome-associated recep-
tor complex, α6β4 integrin,5,6,18,19 is polar-
ized to the tooth-facing surfaces of JE cells.
Our results, confirmed later by others,20 also
showed that the IBL differs from all other

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J Periodontol • June 2001
known epithelial BM by lacking 2 ubiquitous compo-
nents, type IV collagen and prototypic laminin (then
considered laminin-1, presently known to be laminin-
10/11).1,21,22 Instead, the main constituent of IBL
appears to be laminin-5 (Ln-5,16,23), an epithelium-
specific laminin variant.1,24
To understand the physiology and pathology of peri-
odontal and peri-implant tissues, it is important to
know what molecules are expressed and operative in
the tooth-facing (TF) cells of JE. However, studies on
the molecular architecture of the JE are continuously
impeded by difficulties in simultaneously preserving
the antigenicity and the morphology of TF cells. Here
we studied tissue samples obtained by carefully dis-
secting the gingiva from the tooth surface and utilized
the expression of Ln-5 as the indicator of TF cell
preservation. We used double immunofluorescence (IF)
labeling and confocal laser scanning microscopy to
investigate the expression of BM components and basal
cell markers in the IBL and TF cells of JE. We verify
the presence of true type I hemidesmosomes (con-
taining the hemidesmosomal components BP180
BP230 - some cells contain so-called type II hemi-
desmosomes lacking these components6) and show
that the internal basal lamina is not a true basal lam-
ina as judged by its molecular composition.
MATERIALS AND METHODS
Tissue Preparation
Human gingival samples were obtained, after informed
consent, from patients undergoing tooth extractions at
the Institute of Dentistry, University of Turku, Turku,
Finland. Tissue samples were taken from periodon-
tally healthy sites by carefully dissecting the gingiva
from the tooth surface. A total of 35 tissue samples was
collected and an average of 60 sections was cut from
each sample. The age of the subjects ranged from 14
to 62 years. The samples were oriented and embed-
ded in a water soluble embedding medium,§ frozen in
liquid nitrogen, and stored at −70°C until use. Cryo-
stat sections were cut 6 µm thick. The sections were
collected on gelatin-coated glass slides, and stored at
-20°C until use. The human experimentation protocols
were approved by the Ethical Committee of the Insti-
tute of Dentistry.
Antibodies
The rabbit polyclonal antibody recognizing the α3, β3,
and γ2 chains of Ln-5 was raised by immunizing a rab-
bit with solubilized ECM of 804G cells. The rat blad-
der carcinoma cell line 804G was maintained in cul-
ture as described earlier.25,26 For preparation of ECM
material the cells were grown to confluency in serum-
free medium on plastic Petri dishes. The growth
medium consisted of 1:1 DMEM and OPTI-MEM media㛳
and 0.1% bovine serum albumin.¶ The cultures were
Hormia, Owaribe, Virtanen
washed with sterile distilled water and then treated for
10 minutes at room temperature with 20 mM NH4OH
according to the method of Gospodarowicz et al.27
Then the Petri dishes were washed 3 times with 2 mM
Tris-HCl, pH 8.0, 5 mM MgCl2 and further treated for
30 minutes with 10 mM Tris-HCl, pH 8.0, 5 mM MgCl2,
containing 25 µg/ml deoxyribonuclease.# After 3
washes in distilled water, the remaining ECM was
treated for 30 minutes with 2 M urea. The matrix was
removed from the dishes by solubilization in 10 mM
Tris-HCl, pH 8.0, 1% sodium dodecyl sulfate (SDS)
and 15 mM β-mercaptoethanol. A rabbit was then
immunized with the ECM material according to routine
methods and serum was collected from the immunized
rabbit.
For immunoprecipitation, immortalized human gin-
gival keratinocytes28 or 804G cells25 were metaboli-
cally labeled with 35S methionine (50 µCi/ml)** for
12 hours and the culture supernatants were processed
for immunoprecipitation with the polyclonal laminin-5
antibody. The proteins were then electrophoresed by
using 6.5% slab gels under reducing conditions29 and
the gels were processed for fluorography by routine
methods. Immunoblotting of electrophoretically sepa-
rated extracellular matrix and culture supernatant pro-
teins of immortalized human skin keratinocytes
(HaCaT),30 rat palatal keratinocytes (RPK; Hormia et
al. unpublished data), and 804G cells was done by the
method of Towbin et al.31 The bound antiserum was
detected by using an avidin/biotin bridge method.††
The antibodies used in this study are listed in Table
1. Tetramethylrhodamine isothiocyanate (TRITC) and
fluorescein isothiocyanate (FITC)-coupled goat anti
rabbit antibodies, TRITC-goat anti-mouse antibodies,
and FITC-goat anti-rat antibodies were used as sec-
ondary antibodies.‡‡
Immunofluorescence Labeling
Frozen sections were fixed in −20°C acetone and incu-
bated consecutively for 1 hour at room temperature
with the 2 primary antibodies (diluted to 10 to 50
µg/ml), separated by 3 washes in phosphate buffered
saline (PBS). The sections were then again washed in
PBS and incubated for 1 hour at room temperature
with a mixture of 2 appropriate secondary antibodies,
one of which was a FITC-conjugate and the other a
TRITC-conjugate. A total of 10 to 30 sections was
studied for each of the antibody combinations. Speci-
ficity controls were carried out by omission of the pri-
mary antibodies or by replacement of the primary anti-
§ Tissue-Tek O.C.T. compound, Miles Laboratories, Elkhart, IN.
㛳 Gibco BRL, Grand Island, NY.
¶ Sigma Chemical Co., St. Louis, MO.
# Type I DNase, Sigma Chemical Co.
** ICN Biomedicals GmbH, Eschwege, Germany.
†† Vectastain, Vector Laboratories, Burlingame, CA.
‡‡ Jackson Immunoresearch Laboratories, West Grove, PA.
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Table 1. bodies with normal rabbit serum (for poly-

clonal antibodies) or with antibodies with
Antibodies Used in the Study
known and unrelated specificity (monoclonal
antibodies). The expression of Ln-5 was
Specificity Host Animal Clone Source or Reference
used as the indicator of TF cell preservation
integrin ß4 Mouse AA3 32 as shown earlier.23 After washes in PBS, the
specimens were embedded in water-soluble
Integrin α3 Mouse P1B5 Gibco BRL, Life Technologies
mounting medium§§ and studied in a con-
Inc, Gaithersburg, MD
focal laser scanning microscope.㛳 㛳
Integrin αv Mouse VNR147 Gibco BRL
RESULTS
Cytokeratin 14 Mouse LL002 Biogenex, San Ramon, CA
Under immunofluorescence microscopy, the
Cytokeratin 19 Mouse RCK108 Biogenex, San Ramon, CA polyclonal Ln-5 antibody bound to BMs of
Laminin-5 Rabbit See materials and methods
human, rodent, and porcine epithelial tis-
sues (data not shown). In immunoblotting
Laminin-1 (EHS) Rabbit Sigma Chemical Company, of the extracellular matrix and culture super-
St. Louis, MO natant of human keratinocytes and rat
Human laminin Mouse LAM-89 Sigma Chemical Company epithelial cells (HaCaT, RPK, 804G), the anti-
body recognized typical polypeptide bands
Laminin α3 chain Mouse BM2 24 with molecular weights of c.a. 190 kDa, 160
Type IV collagen Mouse COL-94 Sigma Chemical Company kDa, 150 kDa, 140 kDa, and c.a. 100-90
kDa (Fig. 1). Immunoprecipitation of the
Type VII collagen Mouse 32 Chemicon International Inc., culture medium of radioactively labeled cells
Temecula, CA with the antibody revealed a typical set of
Perlecan Rat Chemicon International Inc. c.a. 165-140 kDa and c.a. 100 kDa poly-
peptides (Fig. 2). In addition, a fainter band
HD1 (plectin) Mouse mAb-121 33 of c.a. 200 kDa was precipitated from cul-
BP 180 Mouse mAb-233 34 ture supernatant of human gingival ker-
atinocytes (Fig. 2), possibly representing the
BP 230 Mouse mAb-R815 34 unprocessed form of the α3 laminin chain.
The gingival samples used for immuno-
labeling were obtained by carefully dissecting the tis-
sue free from the tooth surface while making every
effort to preserve the innermost, tooth-facing cell layer
of JE. The success of this effort could be monitored
by immunolabeling with antibodies to Ln-5, a marker
of TF cells. The results are summarized in Table 2.
Double IF labeling of tissue sections for Ln-5 and
laminin-1/10 (Ln-1/Ln-10) (Fig. 3 A, B, and C) or
type IV collagen (Fig. 3 D, E, and F) showed that
these ubiquitous basement membrane components
are co-expressed with Ln-5 in the connective tissue
facing (CTF) basement membrane of the JE, but are
absent from the tooth-epithelium interface. Double
immunolabeling for Ln-5 and type VII collagen (Fig.
3 G, H, and I) or the BM proteoglycan perlecan (Fig.
3 J, K, and L) showed that these components, while
present in the EBL, are also absent at the TF aspect
Figure 1.
Immunoblotting of epithelial cell (RPK, HaCaT, 804G) extracellular
of JE.
matrix proteins and secreted proteins with the polyclonal rabbit The expression of 2 cytokeratins CK 14 and CK 19,
antibody to laminin-5.The antibody recognizes typical polypeptide both of which are basal cell markers in human strati-
bands with molecular weights of c.a. 160 kDa, 150 kDa, 140 kDa fied squamous epithelia, was studied so as to clarify
(α3, γ2 and ß3 chains, respectively) and c.a. 100-90 kDa (processed the possible association between cytoskeletal and
form of the γ2 chain). In RPK cells an additional band of ca 200 kDa
is labeled possibly representing the unprocessed form of the α3
polypeptide. §§ Mowiol, Calbiochem Novabiochem, La Jolla, CA.
㛳㛳 Leica TCS 4D, Leica Microsystems, Mannheim, Germany.

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J Periodontol • June 2001 Hormia, Owaribe, Virtanen

Table 2.
Expression of Basal Cell Markers in
Junctional Epithelium

Molecule TF Cells* CTF Cells† JE‡

Laminin-5 ++ ++ –

Laminin-1 (10) – + –

Type IV collagen – ++ –

Type VII collagen – ++ –

Perlecan - ++ –

Cytokeratin 14 ++ + +

Cytokeratin 19 + – +

Integrin ß4 ++ ++ –

Integrin α3 ++ ++ +

Figure 2.
Immunoprecipitation of culture medium of human keratinocytes (GK)
and gingival 804G cells with polyclonal antibody to laminin-5. Ab:
immunoprecipitation with antibody. C: control with normal rabbit
serum. Polyacrylamide gel electrophoresis run under reducing
conditions reveals a typical set of c.a. 165-140 kDa and 100 kDa
polypeptides. In addition, a fainter band of ca 200 kDa is precipitated
from culture supernatant of human gingival keratinocytes, possibly
representing the unprocessed form of the α3 laminin chain.
Immunoprecipitation with normal rabbit serum does not reveal any
polypeptide bands.
extracellular markers. The results showed that CK 14
was expressed throughout the JE (Fig. 4 A, B, and
C). However, in the TF cells, it was specifically orga-
nized in cell peripheries and appeared to surround
laminin-5–positive areas (Fig. 4 C, insert) indicating
that the TF cells differ from CTF cells also by their
cytoskeletal architecture. CK 19 had a more uneven
distribution in the JE and, although it was most strongly
expressed in Ln-5 positive cells, it did not appear to
have a similar envelope-like peripheral distribution as
CK 14 in the TF cells (Fig. 4 D, E, and F, compared
to A, B, and C).
In the JE, the hemidesmosome-associated inte-
grin α6β4 colocalized with Ln-5 in both CTF basal
cells and in TF cells (Fig 5 A, B, and C). The α3
integrin subunit, forming a heterodimer with the inte-
grin β1 subunit and also known to be a ligand for
Ln-5, was distributed in a more uniform cell mem-
brane-type pattern throughout the JE and, while
being more intensely expressed in basal cells, was
not polarized towards their basal aspects (Fig. 5 D,
E, and F).
Interestingly, strong immunolabeling for the αv inte-
grin subunit was present in the TF cells of the JE.
Integrin αv ++ + +
BP180 ++ ++ –
BP 230 ++ ++ –
HD1 (Plectin) ++ ++ –
* Tooth facing cells.
† Connective tissue facing cells.
‡ Suprabasal and middle cells of junctional epithelium.
++ strong staining; + detectable staining; − no staining.
Other cell layers, on the other hand, showed only occa-
sional scattered immunoreactivity for the integrin αv
subunit (Fig. 5 G, H, and I).
The hemidesmosomal molecules BP180 (Fig. 6 A,
B, and C), BP230 (Fig. 6 D, E, and F), and HD1 anti-
gen (Fig. 6 G, H, and I) showed a practically com-
plete colocalization with Ln-5 both in TF and in CTF
cells of JE.
DISCUSSION
The present results show that α6β4 integrin and Ln-5
are present in the same TF cells of the JE thus serv-
ing as TF cell markers. Since Ln-5 is an extracellu-
lar molecule found in epithelial BMs, its presence in
the TF cell layer also means that at least part of the
IBL is preserved in these specimens. We used double
immunofluorescence labeling and the presence of Ln-
5 as a marker of TF cells and IBL to detect other
molecules in the same location. Our results show that
γ1 chain containing laminins (all laminins but Ln-5)
and type IV collagen are absent in the IBL. Moreover,
confocal laser scanning microscopy demonstrates the
absence of 2 additional BM components, type VII col-
lagen and perlecan, in the IBL. On the other hand,
hemidesmosomal components BP180, BP230, and
HD1 antigen are present on the TF aspects of JE

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Figure 3.
Immunolocalization of basement membrane components in human junctional epithelium. Double immunolabeling with antibodies to laminin-5 (B, E,
H, K) and laminin-1/10 (A), type IV collagen (D), type VII collagen (G), and perlecan (J). Note that laminin-5 is localized on both sides of the JE
whereas all other components are only seen in the connective tissue facing basement membrane and some of them also in vascular basement
membranes.TRITC-and FITC images are superimposed in C, F, I, and L (bars = 50 µm).

cells, showing at a molecular level that the JE is Hemidesmosomes are transmembrane cell-matrix
attached to the tooth surface by means of true type junctional complexes5,6 that are intracellularly con-
I hemidesmosomes.6 nected to the cytokeratin filaments of epithelial cells.35

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J Periodontol • June 2001 Hormia, Owaribe, Virtanen

Figure 4.
Immunolocalization of cytokeratins (A, D), as compared to laminin-5 (B, E) expression in human junctional epithelium. Double immunofluorescence
labeling for CK 14 (A) and laminin-5 reveals that CK 14 is present throughout the JE but is most intensely expressed in the cell layer originally facing
the tooth surface. Superimposition of CK 14 and laminin-5 immunolabeling (C, and insert) reveals a peripheral CK 14 -specific staining encircling the
laminin-5-positive areas. Cytokeratin 19 (D) also appears to be most intensely expressed in the tooth-facing layers of JE, but has an uneven, patchy
distribution that does not fully colocalize with laminin-5 (E). A superimposition of CK 19 and laminin-5 is shown in F (bars = 50 µm).

There is evidence that this connection occurs specifi-
cally to filaments composed of the basal cytokeratins
5 and 14.36 The junctional epithelium has earlier been
shown to express both the basal CK 14 and the sim-
ple epithelial marker CK 19.7-10 In this study we show
that both CK 19 and CK 14 are more intensely
expressed in the cell layers close to the tooth surface.
However, of these 2 cytokeratins, CK 14 appears to be
specifically concentrated in the TF cells. The distinct
peripheral organization of CK 14 in TF cells indicates
that these cells differ from CTF cells not only by their
cell surface molecules and ECM production but also
by their cytoskeletal architecture.
Several integrin receptor molecules are expressed
by epithelial cells.19 The JE of human gingiva has
been shown to express laminin–binding integrin recep-
tors α6β4, α3β1, and, less intensely, the collagen and
laminin-binding integrin receptor α2β1.15-17 The present
results demonstrate the specific expression of the αv
integrin subunit in the TF cells of JE.
The integrin α6β4 is considered to function as a
receptor for Ln-5 and to form tight adhesive junc-
tions between cells and the BM by being a compo-
nent of type I or type II hemidesmosomes.1,5,18,19 In
line with this, our earlier results showed that α6β4
integrin is strictly polarized to the basal aspects of
the TF cells.16 On the other hand, the integrin α3β1
that has been shown to play a role in the initial adhe-
sion of many epithelial cells to laminin-5,19,37 was
present in a non-polar fashion in JE. Its role in the
adhesion of the JE to the tooth surface remains to be
determined.
In addition to the integrin subunits β4 and α3 pres-
ent in laminin-binding integrins, we studied the expres-
sion of the αv subunit in JE since it has been shown
to be expressed in oral mucosa, particularly during
wound healing,38,39 but its presence in JE has not been
studied earlier. Unlike the integrin subunits β4 and α3,
the αv subunit was mainly expressed in the TF cells,
the CTF cells showing only faint incidental staining.
Two αv integrins appear to be expressed in stratified
epithelia, the αvβ5 and the αvβ6 heterodimer.19,40 The
former of these is known to be a vitronectin receptor
whereas the latter is a receptor for fibronectin and
probably tenascin.19,41 Recent studies have, however,
shown that αvβ6 might also have other ligands.36 Since
neither vitronectin nor fibronectin or tenascin is present
in the tooth-epithelium interface (Hormia et al., unpub-
lished data) the expression of αvβ6 indicates that some,
as yet unknown ligand, for the integrin exists in the

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Type I Hemidesmosomes in the Dento-Epithelial Junction Volume 72 • Number 6

Figure 5.
Immunolocalization of integrins (A, D, G) and laminin-5 (B, E, H) in human junctional epithelium. Double immunofluorescence labeling for the ß4
integrin subunit (A) and laminin-5 reveals a practically complete colocalization (C).The integrin subunit α3 is localized throughout the JE but most
intense expression is seen in basal and parabasal cells towards both the tooth facing and the connective tissue facing aspect (D).When compared to
integrin α3 (D), laminin-5 (E) has a more restricted expression that can be superimposed on α3 positive areas (F).The integrin subunit αv (G) shows
a cell membrane type localization in most JE cells. It shows, however, a specific, intense localization in tooth-facing laminin-5 positive (H) cells.The
basal aspects of connective tissue-facing basal cells appear to be negative for αv integrin subunit. A superimposition of αv and laminin-5 is seen in I
(bars = 50 µm).

dento-epithelial junction. This possibility is particularly
intriguing since αvβ6 has been shown to be specifically
up-regulated during re-epithelialization of wounds when
keratinocytes migrate on a provisional extracellular
matrix composed of fibrinogen, fibronectin, vitronectin,
and tenascin.38,39
Laminins are a growing family of large cruciform or
Y-shaped trimeric molecules composed α, β, and γ
subunit chains.1,42 To date 5 alpha, 3 beta, and 3
gamma chains have been identified and, out of the
many possible combinations of these chains, in vivo
evidence exists for at least 14 different heterotrimers.1
Originally laminin was thought to consist of a single
trimer, α1β1γ1, which was later termed Ln-1. For a
long time this laminin was regarded the prototypic
and ubiquitous laminin. However, it has become evi-
dent that antibodies thought to react with Ln-1, in fact,
recognize laminin-10 (α5β1γ1). Consequently, laminin-
10 is considered the major laminin variant of epithe-
lial BM whereas Ln-1 has a rather restricted distribu-
tion.1,21,22,42
The commercial antibodies used in our study (anti-
EHS laminin and anti-human laminin) recognize all γ1
chain containing laminins and gave identical results

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J Periodontol • June 2001 Hormia, Owaribe, Virtanen

Figure 6.
Immunolocalization of hemidesmosomal components (A, D, G) and laminin-5 (B, E, H) in human junctional epithelium. Double immunolabeling with
antibodies to BP180 (A), BP230 (D) and HD-1 antigen (G) and laminin-5 (B, E, H). Superimposition of TRITC and FITC images are shown in C, F,
and I. Note that all components are localized on both sides of the JE and that hemidesmosomal components can be fully superimposed on laminin-5-
specific immunofluorescence in JE (bars = 50 µm).

in immunofluorescence microscopy. Our present results
indicate, therefore, that neither Ln-1 nor laminin-10 is
present in the IBL. As we have shown earlier,23 the
only thus far known basal lamina component present
in the tooth-epithelium interface is Ln-5.
On the basis of the molecular structure of Ln-5
(lacking the domain VI in the α chain and being inca-
pable of binding nidogen), it has been postulated that
Ln-5 does not self-assemble into a network but instead
binds to the BM proper; e.g., by forming complexes
with other laminin isoforms (laminin-6 or laminin-7) or
by directly binding to type VII collagen, the structural
component of so-called anchoring fibrils,43 in the BM.44
Our earlier16,23 and present results suggest that nei-
ther can be the case in the dento-epithelial junction
since such other molecules are absent from this loca-
tion.
In epithelial BM, Ln-5, together with BP180, is a
component of anchoring filaments, 2 to 8 nm fila-
mentous structures traversing the lamina lucida
beneath HDs.1,42,45,46 However, the dento-epithelial
junction lacks distinct anchoring filaments,2-4 sug-
gesting that in this location Ln-5 either binds to other
still unknown molecules in the IBL, binds directly to the
tooth surface, or is somehow associated with the cell
surface. The molecular interactions and ultrastructural
localization of Ln-5 in the IBL remain to be studied.
The exclusive expression of Ln-5 in IBL indicates
that the IBL is not a basal lamina by definition but a
simple extracellular matrix with no network structure.

795
Type I Hemidesmosomes in the Dento-Epithelial Junction
Understanding the molecular architecture and func-
tion of the tooth-epithelium attachment may aid in the
understanding of the onset, progression, and healing
of periodontal disease and may provide new possibil-
ities for manipulating periodontal healing.
ACKNOWLEDGMENTS
The authors thank Ms. Leila Saarinen and Ms. Ritva
Koskinen for technical assistance and Mr. Tomas
Bymark for assistance in confocal microscopy. Con-
focal microscopy was done at the Institute of Cell Biol-
ogy, Åbo Akademi University, Turku, Finland. This
study was supported by grants from the Finnish Den-
tal Society and the ITT Foundation.
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