
INVESTIGATION OF THE N-TERMINAL CODING REGION
OF MUC7 ALTERATIONS IN DENTISTRY STUDENTS
WITH AND WITHOUT CARIES Koç Öztürk L, Yarat A, Akyuz S, Furuncuoglu H, Ulucan K, *Corresponding Author: Dr. Korkut Ulucan, Department of Molecular Biology and Genetics, Faculty of
Engineering and Natural Sciences, Üsküdar University, Haluk Turksoy Sok. No. 14, Üsküdar, İstanbul 34662,
Turkey. Tel: +90-216-400-2222-2409. Fax: +90-216-400-2222; Mobile: +90-532-692-1922.
E-Mail: korkutulucan@hotmail.com page: 71
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DISCUSSION
Mucins coat the gastrointestinal, genito-urinal
and respiratory tracts, as well as the oral cavity. In the
oral cavity, they have a variety of functions such as
lubricating and protecting the oral cavity and providing
a nonspecific immune defense [10].
In our cohort, OHI-S, GI, salivary pH, flow rate,
buffering capacity and total protein levels were not
significantly different between the two groups. These
parameters have important effects on oral hygiene,
and also for dental caries. But in our study cohort,
all of these parameters did not affect dental caries
formation.
Low-molecular weight mucin contains 377
amino acids. The first 20 of these are located in the
N-terminal domain and are very hydrophobic. It
contains a central part, made of six tandem repeats
of 23 amino acids that are rich in proline and hydroxylated
amino acids, and having approximately
90-100 O-linked chains. A histatin-like domain with
a leucine-zipper segment, followed by a moderately
glycosylated region, constitute the N-terminal domain;
a heavily glycosylated domain, and a second leucine-zipper segment for the C-terminal extremity.
The distal regions of MUC7 do not exhibit any
cysteine-rich domains, only two cysteine residues are
present towards its N-terminal end. So far, MG2 has
no sequence homology with any other mucins. The
N-terminal region of the protein binds Streptococcus
mutans (S. mutans). It also exhibits a candidacidal activity
and, after cleavage, a subdomain of this region
is microbicidal against a periodontal pathogen, Actinobacillus
actinomycetemcomitans. Furthermore, a
MUC7 20-mer displays potent killing activity against
a variety of fungi and both gram-positive and gramnegative
bacteria [4,11,12]. The two cysteine residues
located in the N-terminal region of MUC7 seem to be
directly implicated in these activities [12].
Low-molecular weight mucin has been reported
to interact with several strains of streptococci by
promoting their agglutination [13]. The N-terminal
region of MG2 has a broad-spectrum fungicidal and
bactericidal activity in vitro [14,15]. Low-molecular
weight mucin peptides derived from the N-terminal
of MG2 are the cationic anti-microbial peptides derived
from the human low molecular weight salivary
mucin, a component of innate immunity (the first-line
of the host defense system against pathogens). Lowmolecular
weight mucin (357 amino acid residues in
saliva), protects the oral cavity from microbial infections
through more general protective mechanisms
rather than the direct killing of microorganisms [16].
It was shown that a 20 kDa MG2 fragment, containing
the N-terminal region, was present in the saliva
and suggested that cleavage of MG2 in vivo may lead
to the fragments with microbicidal properties [17]. The
MG2 20-mer, sub-domain of N- terminal domain, has
been shown to be able to cross the fungal cell membrane
and accumulate inside the cells, suggesting a
possibility that MG2 peptides may also exert killing
activity against S. mutans [18]. In some conditions,
rather than killing the bacteria directly, they disturb
cariogenic and periodontal pathogen activity by interacting
with them, binding the bacteria via their cysteine
residues within their N-terminal domain [19,20].
The peptides derived from the N-terminal region of
MG2 present somewhat preferential antimicrobial
activity against S. mutans. They also have an effect
on in vitro formation and reduction of the preformed
S. mutans biofilm [15]. We did not detect any statistically
significant polymorphisms between caries and
caries-free groups in the present study. There was one
common SNP, affecting the amino acid at position 80,
changing the natural amino acid asparagine to lysine.
This SNP seemed to have no effect on dental caries
in individuals, but seems to be an important polymorphism
in the examined Turkish subjects.
In conclusion, the SNP detected in this study may
be a specific polymorphism effecting the Turkish population.
Further studies with a larger number of individuals
are necessary in order to clarify our findings.
Declaration of Interest. The authors report no
conflicts of interest. The authors alone are responsible
for the content and writing of this article.
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