Publication: Gel-forming mucins. Notions from in vitro studies
Authors
Perez-Vilar, J. ; Mabolo, R.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Mucus secretions form a protective barrier in
the mucosa of the auditory, gastrointestinal, respiratory,
and urogenital systems, and the conjunctiva in the eyes.
A family of glycoproteins known as gel forming mucins
is the major component of the mucus. Gel-forming
mucins are among the largest and most complex proteins
known. Their polypeptide chains comprise thousands of
amino acid residues organized into different domains
with diverse post-translational modifications, including
O- and N-glycosylation, sulfation, proteolysis, and likely
C-mannosylation. Moreover, these glycoproteins form
disulfide-linked oligomers/multimers with molecular
weights in the millions. Molecular polydispersity in
terms of length, carbohydrate content and composition,
is an invariable feature of purified mucins. This
structural complexity makes it technically very difficult
to study mucin biochemical and physical properties. It is
not surprising, therefore, that our knowledge on mucin
structure, biosynthesis and function still is incomplete.
During the last decade, the use of recombinant mucins
has allowed researchers to study the biochemical
properties of protein domains, peptide motifs and amino
acid residues common to all gel-forming mucins, and to
propose specific roles for them. We review here the
relative impact that these in vitro studies have had for our current understanding of two of the most important
features of these macromolecules: formation of disulfide
linked oligomers and mucin intragranular packaging.
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