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Differential Expression of the Tight Junction Proteins Claudin-1 Claudin-4 Occludin ZO-1 and PAR3 in the Ameloblasts of Rat Upper Incisors.

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THE ANATOMICAL RECORD 291:577–585 (2008)
Differential Expression of the Tight
Junction Proteins, Claudin-1, Claudin-4,
Occludin, ZO-1, and PAR3, in the
Ameloblasts of Rat Upper Incisors
TETSUICHIRO INAI,1* AKIHITO SENGOKU,1 EIJI HIROSE,1
HIROSHI IIDA,2 AND YOSABURO SHIBATA1
1
Department of Developmental Molecular Anatomy, Graduate School of Medical Sciences,
Kyushu University, Higashi-ku, Fukuoka, Japan
2
Laboratory of Zoology, Graduate School of Agriculture, Kyushu University, Higashi-ku,
Fukuoka, Japan
ABSTRACT
Tight junctions (TJs) create a paracellular permeability barrier to
restrict the passage of ions, small solutes, and water. Ameloblasts are
enamel-forming cells that sequentially differentiate into preameloblasts,
secretory, transition, and ruffle-ended and smooth-ended maturation ameloblasts (RAs and SAs). TJs are located at the proximal and distal ends of ameloblasts. TJs at the distal ends of secretory ameloblasts and RAs are welldeveloped zonula occludens, but other TJs are moderately developed but
incomplete zonula occludens (ZO) or less-developed macula occludens. We
herein examined the immunofluorescence localization of TJ proteins, 10 claudin isoforms, occludin, ZO-1, and PAR3, a cell polarity-related protein, in
ameloblasts of rat upper incisors. ZO-1 and claudin-1 were detected at both
ends of all ameloblasts except for the distal ends of SAs. Claudin-4 and occludin were detected at both ends of transition and maturation ameloblasts
except for the distal ends of SAs. PAR3 was detected at the proximal TJs of
all ameloblasts and faintly at the distal TJs of early RAs. These results indicate that functional zonula occludens formed at the distal ends of the secretory ameloblasts and RAs consisted of different TJ proteins. Therefore, the
distal TJs of secretory ameloblasts and RAs may differentially regulate the
paracellular permeability to create a microenvironment suitable for enamel
deposition and enamel maturation, respectively. In addition, PAR3 may be
principally involved in the formation and maintenance of the proximal, but
not distal, TJs. Anat Rec, 291:577–585, 2008. Ó 2008 Wiley-Liss, Inc.
Key words: ameloblast; tight junction; claudin; PAR3; occludin
Tight junctions (TJs) function as a barrier to regulate
the paracellular transport of ions, small solutes, and
water (Gumbiner, 1993). In addition, TJs are a multiprotein complex consisting of integral membrane proteins
and cytoplasmic plaque proteins and play a role in the
regulation of cell polarity, proliferation, and differentiation (Shin et al., 2006). Claudins, occludin, tricellulin,
and junctional adhesion molecules (JAMs) are integral
membrane proteins at the TJs. Claudins form a multigene family (Morita et al., 1999) composed of at least 24
members in mice. More than two claudin isoforms are
usually expressed in a single cell, and the combination
and mixing ratios of claudins determine the TJ properÓ 2008 WILEY-LISS, INC.
Grant sponsor: Ministry of Education, Culture, Sports,
Science and Technology, Japan; Grant numbers: 11770008,
13670018, 16590146, 18590187.
*Correspondence to: Tetsuichiro Inai, Department of Developmental Molecular Anatomy, Graduate School of Medical Sciences, Kyushu University, Maidashi 3-1-1, Higashi-ku, 812-8582
Fukuoka, Japan. Fax: 81-92-642-6202.
E-mail: inai@ana2.med. kyushu-u.ac.jp
Received 12 November 2007; Accepted 16 January 2008
DOI 10.1002/ar.20683
Published online 1 April 2008 in Wiley InterScience (www.
interscience.wiley.com).
578
INAI ET AL.
TABLE 1. Summary for the expression pattern of ZO-1, claudin-1, claudin-4, occludin,
and PAR3 in the ameloblasts during differentiationa
Maturation ameloblasts
Preameloblasts
ZO-1
prox.
dist.
Claudin-1
prox.
dist.
Claudin-4
prox.
dist.
Occludin
prox.
dist.
PAR3
prox.
dist.
Early
Late
Secretory
ameloblasts
Transition
ameloblasts
Early
RA
Mid
SA
Mid
RA
Late
SA
Late
RA
11
1
111
11
111
111
111
111
111
1111
111
6
111
111
11
6
11
111
61
6
1
1
1
111
1
1
2
111
6
2
61
111
1
6
1
111
2
2
2
2
2
2
61
61
1
11
61
6
1
11
1
6
1
1
2
2
2
2
2
2
1
1
1
1111
1
6
1
1111
1
2
11
1111
61
2
1 11
2
111
2
111
2
111
61
11
2
11
2
1
2
1
2
a
prox., proximal ends of the lateral membrane of ameloblasts; dist., distal ends of the lateral membrane of ameloblasts; ZO,
zonula occludens; PAR, partitioning defective. Intensity of immunostaining: 2, negative; 6, weak (occasionally expressed);
1, weak (always expressed); 11, moderate; 111, strong; 1111, very strong.
ties including paracellular permeability. Zonula occludens (ZO)-1, ZO-2, and ZO-3 are three of the well-characterized proteins among many cytoplasmic plaque proteins at TJs. They link occludin and claudins to the
actin cytoskeleton to stabilize the TJ structure or to promote the clustering of claudins/occludin to polymerize
into TJ strands (Furuse et al., 1994; Haskins et al.,
1998; Itoh et al., 1999a,b, 1997).
The establishment of epithelial cell polarity requires
atypical protein kinase C (aPKC) activity (Suzuki et al.,
2001). The Crumbs complex and the partitioning defective (PAR) complex have been shown to play critical
roles in the development of cell polarity (Shin et al.,
2006). The PAR3/PAR6/aPKC complex localizes at TJs
(Ohno, 2001; Macara, 2004). PAR6 links PAR3/PAR6/
aPKC complex to the active form of Cdc42, a Rho
GTPase, and these interactions are important for the
formation or maintenance of TJs in MDCK epithelial
cells (Joberty et al., 2000).
The first sign of TJ formation was observed in preameloblasts abutting the unmineralized dentine at the
distal ends of the lateral membrane, and later, TJ
strands formed an anastomosing meshwork at the proximal and distal ends of the preameloblasts. However,
these TJs did not form a complete seal around the cell
body circumference (Sasaki et al., 1982, 1990). When the
newly secreted enamel matrix reached 7–8 mm in thickness, the distal TJ in the secretory ameloblasts exhibited
a functional zonular TJ (zonula occludens). The proximal
TJ formed by two secretory ameloblasts was moderately
developed but there was an open space at the corner
formed by three secretory ameloblasts (Sasaki et al.,
1982, 1990). In transition ameloblasts, the proximal and
distal TJs did not completely occlude the extracellular
space (Sasaki et al., 1990). In RAs, the distal TJ is a
zonula occludens but the proximal TJ is a macula occludens (Sasaki et al., 1983a, 1990). In SAs, the proximal
TJ is a structurally incomplete zonula occludens but the
distal TJ is a macula occludens (Sasaki et al., 1983b,
1990).
Intercellular junctions, tight, adherens, and gap junctions, not only organize tissue architecture but also are
involved in physiological function, morphogenesis, and
cell differentiation. The distributions of integral membrane proteins forming intercellular junctions such as
occludin, claudins, cadherins, and connexins in ameloblasts have been reported previously (Inai et al., 1997;
Obara et al., 1998; João and Arana-Chavez, 2004; Bello
et al., 2007; Ohazama and Sharpe, 2007). Early and
late differentiating rat ameloblasts at the bell stage
expressed claudin-1 at the proximal and distal TJs and
also expressed occludin except for the distal TJs of late
differentiating ameloblasts (João and Arana-Chavez,
2004). In developing human teeth, strong immunoreactivities for claudin-1 and -7 were detected in the enamel
organ, ameloblasts, and enamel matrix, but moderate
staining for claudin-4 was detected in the outer enamel
epithelium (Bello et al., 2007). An in situ hybridization
analysis of claudin-1 to -11 showed that only claudin-2
was expressed in mouse ameloblasts at the early bell
stage (Ohazama and Sharpe, 2007). We herein examined
the expression of TJ proteins, including 10 claudins,
occludin, ZO-1, and PAR3 in preameloblasts, secretory,
transition, and maturation ameloblasts, because no
researchers have reported the localization of TJ proteins
in maturation ameloblasts.
MATERIALS AND METHODS
Antibodies
Primary antibodies and their working dilutions are as
follows: rabbit anti–claudin-1 polyclonal antibody (pAb;
1:50), mouse anti–claudin-2 monoclonal antibody (mAb;
1:100), anti–claudin-3 pAb (1:100), anti–claudin-4 mAb
(1:100), anti–claudin-5 mAb (1:200), anti–claudin-6 pAb
(1:100), anti–claudin-7 pAb (1:100), anti–claudin-8 pAb
TIGHT JUNCTION PROTEINS IN AMELOBLASTS
579
(1:100), anti–claudin-12 pAb (1:50), anti–claudin-15 pAb
(1:50), anti-occludin mAb (1:200), anti-occludin pAb
(1:200), anti–ZO-1 pAb (1:400), and anti–ZO-1 mAb
(1:1,000). Anti–claudin-6 pAb and anti–claudin-7 pAb
were purchased from IBL (Takasaki, Japan), and the
remaining antibodies were purchased from Zymed
(South San Francisco, CA). Anti-mouse Ig and anti-rabbit Ig conjugated with either Alexa 488 or Alexa 594
(Molecular Probes, Eugene, OR) were used as secondary
antibodies at a 1:400 dilution.
ameloblasts, intense staining for claudin-1 was detected
at the distal ends and weak staining was detected at the
proximal ends (Fig. 1). Weak staining for claudin-1 was
detected at both ends of transition ameloblasts (Fig. 2).
In RAs, negative to weak staining for claudin-1 was
observed at the proximal ends and intense staining was
detected at the distal ends (Fig. 2). In the SAs, negative
to weak staining for claudin-1 was observed at the proximal ends and no staining was detected at the distal
ends (Fig. 2).
Specimens
Claudin-4
Three 21-day-old Wistar rats were purchased from
Kyudo (Tosu, Japan). They were anesthetized intraperitoneally with Nembutal (30 mg/kg body weight) before
perfusion with fixative. They were perfused systemically
from the left ventricle with 1% paraformaldehyde in
phosphate buffered saline (PBS, pH 7.4) under anesthesia. The upper incisors were dissected and then were
immersed in the same fixative on ice for 4 hr. After
washing in PBS, the upper incisors were decalcified in
10% ethylenediaminetetraacetic acid, pH 7.4, for 4 days
at 48C, washed with PBS, and rapidly frozen in liquid
nitrogen-cooled OCT compound. Cryosections (5 mm) were
cut and mounted on glass slides.
Claudin-4 was not detected in the preameloblasts and
secretory ameloblasts (data not shown). Claudin-4 was
first detected at both ends of the late transition ameloblasts (Fig. 2). Moderate staining for claudin-4 was
observed at the distal ends of early and mid RAs. Weak
staining was detected at the proximal ends of the RAs
and SAs and at the distal ends of late RAs (Fig. 2).
Staining for claudin-4 was not detected at the distal
ends of the SAs (Fig. 2).
Immunohistochemistry
The cryosections were washed in PBS, incubated in
0.2% Triton X-100 in PBS for 15 min, washed again in
PBS, and then incubated with 1% bovine serum albumin
in PBS for 30 min at room temperature to block nonspecific binding. They were incubated with primary antibodies for 1 hr in a moist chamber. After rinsing in PBS 5
times for 3 min each, they were incubated with secondary
antibodies for 30 min in the dark. They were washed 5
times in PBS for 3 min each and mounted in Vectashield
mounting medium (Vecta Laboratories, Burlingame, CA).
The specimens were then examined with a Zeiss LSM
510 confocal microscope (Oberkochen, Germany).
RESULTS
The upper incisors contained preameloblasts, secretory, transition, and maturation ameloblasts. We examined the localization of 10 claudin isoforms and only
claudin-1 and -4 were detected in the ameloblasts. Claudin-5 was expressed in vascular endothelial cells but not
in ameloblasts.
ZO-1
ZO-1 was first detected at the proximal ends of very
early preameloblasts and eventually at the distal ends
(Fig. 1). Intense signals for ZO-1 were consistently
observed at the proximal and distal ends of preameloblasts, secretory, transition, and maturation ameloblasts
(Figs. 1–5) although not at the distal ends of the SAs
(Figs. 2, 5).
Claudin-1
Claudin-1 was first detected at the proximal ends of
early preameloblasts and eventually at the distal ends
(Fig. 1). Staining for claudin-1 gradually increased toward the late preameloblasts (Fig. 1). In the secretory
Occludin
Occludin was not detected in either the preameloblasts or secretory ameloblasts, but it was detected in
the stratum intermedium, stellate reticulum, and papillary layer (Figs. 1, 2). Occludin was first detected at the
proximal and distal ends of the transition ameloblasts
(Fig. 2). Intense or weak staining for occludin was
observed at the distal or proximal ends of RAs, respectively (Fig. 2). Occludin was negative at the distal ends
of SAs but weak signals for occludin were detected at
the proximal ends of SAs (Fig. 2).
PAR3
PAR3 was first detected at the proximal ends of early
preameloblasts and gradually increased toward the late
preameloblasts (Fig. 3). Intense staining for PAR3 was
observed at the proximal ends of secretory and transition ameloblasts (Fig. 4). PAR3 was localized slightly apical to ZO-1 and not perfectly colocalized with ZO-1 (Fig.
4). Intense staining for PAR3 was detected at the proximal ends of early RAs, and thereafter, it gradually
decreased with the development of the ameloblasts (Fig.
5). PAR3 was not detected at the distal ends of ameloblasts except for early RAs (Figs. 3–5).
DISCUSSION
The distribution and signal intensity of claudin-1 and
-4, TJ-forming integral membrane proteins, in this study
closely coincided with the development of TJs in the
ameloblasts as previously examined by freeze-fracture
electron microscopy. The distal TJs in the secretory ameloblasts and RAs are a well-developed zonula occludens
which encircles each cell body, the proximal TJs in secretory ameloblasts and SAs are a moderately developed
but incomplete zonular type, and other proximal and
distal TJs in ameloblasts are basically a less-developed
macula occludens (Sasaki et al., 1982, 1983a,b, 1990).
Intense immunoreactivity for ZO-1 was constantly
detected at both ends of ameloblasts, although development of the proximal TJs was generally insufficient.
580
INAI ET AL.
Fig. 1. Immunofluorescence localization of claudin-1, zonula occludens (ZO) -1, and occludin in the preameloblasts and secretory ameloblasts. Cryosections were doubly stained with anti–claudin-1 and
anti–ZO-1 antibodies or anti-occludin and anti–ZO-1 antibodies. Green
signals for claudin-1 are first detected at the proximal ends of early
preameloblasts and then at the distal ends of preameloblasts (long
arrow). Red signals for ZO-1 are first detected at the proximal ends of
early preameloblasts and then at the distal ends of preameloblasts
(short arrow). Signals for claudin-1 are weak at the proximal and distal
ends of preameloblasts and at the proximal ends of secretory ameloblasts, but strong at the distal ends of secretory ameloblasts. Dot-like
staining for claudin-1 is also detected in the cytoplasm of secretory
ameloblasts. The signals for ZO-1 are moderate to strong at the proximal ends of preameloblasts, weak to moderate at the distal ends of
preameloblasts, and strong at the both ends of secretory ameloblasts.
The signals for occludin are detected in the stellate reticulum and stratum intermedium, but not in secretory ameloblasts. An asterisk indicates the artificial gap between late preameloblasts and predentin/
dentin located between the arrowheads. An oblique arrow indicates
Tomes’ processes of secretory ameloblasts. cldn-1, claudin-1; pAm,
preameloblast; Am, ameloblast; SI, stratum intermedium; SR, stellate
reticulum; Od, odontoblast. Scale bars 5 20 mm.
This phenomenon is probably due to the fact that ZO-1
can associate with not only TJ proteins such as occludin
and claudins (Furuse et al., 1994; Itoh et al., 1999a) but
also with adherens junction proteins such as cadherin/
catenin complex (Itoh et al., 1997) or with gap junction
proteins such as connexin (Cx) 43 (Giepmans and Moolenaar, 1998; Toyofuku et al., 1998). Indeed, Cx43 and ZO1 always coexisted in differentiating ameloblasts, thus
suggesting the existence of a close relationship between
the two proteins (João and Arana-Chavez, 2003).
It has been proposed that each claudin isoform may
form pores with a unique charge selectivity determined
by charged amino acids in the first extracellular loop of
each claudin in the TJ (Colegio et al., 2002; Van Itallie
et al., 2003), thus suggesting that the overall physiological properties of the paracellular space may be deter-
TIGHT JUNCTION PROTEINS IN AMELOBLASTS
581
Fig. 2. Immunofluorescence localization of claudin-1, claudin-4,
occludin, and zonula occludens (ZO) -1 in transition and maturation
ameloblasts. Cryosections were doubly stained with anti–claudin-1
and anti–ZO-1 antibodies, anti–claudin-4 and anti–ZO-1 antibodies, or
anti-occludin and anti–ZO-1 antibodies. In transition ameloblasts,
weak signals for claudin-1, strong signals for ZO-1, negative to weak
signals for claudin-4, and weak signals for occludin are detected at
both ends. In maturation ameloblasts, intense red signals for ZO-1 are
detected at both ends of the RAs and at the proximal ends of the
SAs, but are negative to weak at the distal ends of the SAs. At the
proximal ends of the RAs, negative to weak signals for claudin-1,
weak signals for claudin-4, and weak to moderate signals for occludin
are detected. At the distal ends of the RAs, strong signals for claudin1, moderate to weak signals for claudin-4, and very strong signals for
occludin are detected. At the proximal ends of SAs, negative to weak
signals for claudin-1 and claudin-4, and weak signals for occludin are
detected. At the distal ends of the SAs, negligible signals for claudin1, claudin-4, and occludin are detected. Dot-like staining for claudin-1
is also detected in the cytoplasm of ameloblasts. The signals for claudin-4 detected in the papillary layer may be nonspecific staining,
especially in the transition ameloblasts and early RAs. RA, ruffleended ameloblast; SA, smooth-ended ameloblast; PL, papillary layer.
Scale bar 5 20 mm.
mined by the combination and mixing ratios of claudin
isoforms expressed in the cells. In occludin-deficient
mice, the morphology of TJs and barrier function of intestinal epithelium were normal, but histological abnormalities were found in several tissue specimens (Saitou
et al., 2000). In contrast, the second extracellular domain peptide of occludin reduced the amount of occludin
localized at the TJ and reversibly disrupted the transepithelial permeability barrier (Wong and Gumbiner,
1997). Therefore, the function of occludin is still obscure,
but occludin may nevertheless modulate the TJ permeability in epithelial cells. Speculating from these results,
the paracellular permeability of TJs at the distal ends of
RAs may be different from that of secretory ameloblasts
because of the difference in combinations of TJ proteins
regulating paracellular permeability. This speculation is
supported by the findings of a previous report that
describe the distal TJ in RAs to be closed to calcium,
whereas the proximal and distal TJs in secretory ameloblasts were not (Kawamoto and Shimizu, 1997).
Calcium ions are provided from blood vessels to mineralizing enamel across the layer of ameloblasts through
the paracellular pathway and/or transcellular pathway.
45
Ca autoradiography of rat lower incisors with accurate
control of exposure time showed that the proximal TJ in
SAs and the distal TJ in RAs were closed to calcium,
whereas the distal TJ in SAs, the proximal TJs in RAs,
and the proximal and distal TJs in secretory ameloblasts
were not (Kawamoto and Shimizu, 1997). High radioactivity was detected in RAs and the time for calcium to
582
INAI ET AL.
Fig. 3. Immunofluorescence localization of partitioning defective
(PAR) 3 and zonula occludens (ZO) -1 in preameloblasts. Cryosections
were doubly stained with anti-PAR3 and anti–ZO-1 antibodies. Very
weak signals for PAR3 are first detected at the proximal ends of early
preameloblasts and gradually increase toward late preameloblasts.
However, PAR3 is not detected at the distal ends of preameloblasts.
Red signals for ZO-1 are first detected at the proximal ends of early
preameloblasts, after a while at the distal ends (arrow), and later at
both ends. An asterisk indicates the artificial gap between late preameloblasts and predentin/dentin. pAm, preameloblast. Scale bar 5
20 mm.
diffuse across RAs was much longer than that across
SAs and secretory ameloblasts. From these results, the
authors concluded that calcium moves to mineralizing
enamel through the paracellular pathway in SAs and secretory ameloblasts but through the transcellular pathway in RAs. Because claudin-4 formed pores in TJs
reducing cation entry (Van Itallie et al., 2001, 2003;
Colegio et al., 2002), the distal TJ in RAs constituted by
claudin-4 may restrict the calcium movement between
the extracellular fluid and enamel matrix fluid and
maintain concentration of calcium ions transported
through cytoplasm of RAs. Although the overexpression
of claudin-1 increased transepithelial electrical resistance in MDCK cells (Inai et al., 1999), the charge selectivity of the pores formed by claudin-1 has not yet been
determined. Therefore, it is premature to discuss the
function of claudin-1 in ameloblasts.
The PAR3/PAR6/aPKC complex localizes at TJs
(Macara, 2004; Ohno, 2001) and it also plays a role in
the formation or maintenance of TJs (Joberty et al.,
2000). The number of TJ strands was higher in the
distal rather than proximal renal tubules, but there was
no significant difference in the signal intensity for PAR3
between the proximal and distal renal tubules (Hirose
et al., 2002). These results suggest that the expression
level of PAR3 may not be related to the development of
TJ. Therefore, it is not surprising that PAR3 was consistently localized at the proximal ends of ameloblasts
where less-developed TJs were usually observed. Double
immunogold labeling of the distal renal tubules for
PAR3 and ZO-1 showed that PAR3 was detected in the
cytoplasm located at the apical edge of the TJ, but ZO-1
distributed alongside the TJ slightly basal to PAR3
(Hirose et al., 2002). This result is consistent with the
present result; PAR3 was localized slightly apical to ZO1 in the proximal TJ of secretory ameloblasts (Fig. 4).
The present result raises a new question as to why TJs
are formed at the distal ends of ameloblasts without
PAR3.
In summary, the proximal and distal TJs in ameloblasts differentially expressed TJ proteins including ZO1, claudin-1, claudin-4, and occludin during ameloblast
TIGHT JUNCTION PROTEINS IN AMELOBLASTS
Fig. 4. Immunofluorescence localization of partitioning defective
(PAR) 3 and zonula occludens (ZO) -1 in the secretory and transition
ameloblasts. Cryosections were doubly stained with anti-PAR3 and
anti–ZO-1 antibodies. Strong signals for PAR3 are detected at the
proximal ends of early secretory, mid secretory, and transition amelo-
583
blasts, but not at the distal ends. Strong signals for ZO-1 are detected
at both ends. Green signals for PAR3 are not perfectly colocalized
with red signals for ZO-1 and PAR3 is localized slightly apical to ZO-1.
sAm, secretory ameloblast; Am, ameloblast; SI, stratum intermedium.
Upper short scale bar 5 20 mm. Lower long scale bar 5 10 mm.
584
INAI ET AL.
Fig. 5. Immunofluorescence localization of partitioning defective
(PAR) 3 and zonula occludens (ZO) -1 in maturation ameloblasts. Cryosections were doubly stained with anti-PAR3 and anti–ZO-1 antibodies. Green signals for PAR3 are basically detected at the proximal
ends of maturation ameloblasts, including the RAs and SAs, and then
they gradually decrease toward the late RAs. Very weak signals for
PAR3 are also detected at the distal ends of the early RAs (arrowheads). Red signals for ZO-1 are detected at both ends in the early,
mid, and late RAs, and only at the proximal ends of the mid SAs. RA,
ruffle-ended ameloblast; SA, smooth-ended ameloblast; PL, papillary
layer. Scale bar 5 20 mm.
development. In particular, the distal TJ of secretory
ameloblasts consisted of claudin-1, while that of the RAs
consisted of claudin-1, claudin-4, and occludin. Therefore, the distal TJs in secretory ameloblasts and RAs
may differently regulate the paracellular permeability
against the enamel surface to perform their functions
appropriately; namely, enamel formation and enamel
maturation, respectively. In addition, the consistent
localization of PAR3 at the proximal TJ during ameloblast development suggests that the proximal, but not
distal, TJ in the ameloblasts may be formed or maintained by the PAR3/PAR6/aPKC complex.
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expressions, par3, junction, protein, differential, upper, claudio, rat, incisors, occluding, tight, ameloblasts
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