Biopolymers for Biomedical and Biotechnological Applications 2020
DOI: 10.1002/9783527818310.ch6
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Advances in Mucin Biopolymer Research: Purification, Characterization, and Applications

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Cited by 10 publications
(7 citation statements)
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“…Due to its location, it is highly susceptible to external environmental influences and requires complex and well-developed defense mechanisms to maintain its integrity. Mucins are located in the epithelial layer, with secreted mucins having appeared early in the evolution of metazoans and formed transmembrane structures involved in the protection, repair, and survival of vertebrate epithelia [ 5 , 15 , 16 , 17 ]. The family of mucins to which MUC1 belongs is that of large, highly glycosylated proteins [ 7 ].…”
Section: The Structure Of Muc1mentioning
confidence: 99%
See 1 more Smart Citation
“…Due to its location, it is highly susceptible to external environmental influences and requires complex and well-developed defense mechanisms to maintain its integrity. Mucins are located in the epithelial layer, with secreted mucins having appeared early in the evolution of metazoans and formed transmembrane structures involved in the protection, repair, and survival of vertebrate epithelia [ 5 , 15 , 16 , 17 ]. The family of mucins to which MUC1 belongs is that of large, highly glycosylated proteins [ 7 ].…”
Section: The Structure Of Muc1mentioning
confidence: 99%
“…The family of mucins to which MUC1 belongs is that of large, highly glycosylated proteins [ 7 ]. There are three types of mucins: trans-membrane (e.g., MUC1, MUC4, and MUC16), secreted (gel-forming) (e.g., MUC2, MUC5AC, and MUC6), and soluble (non-gel-forming) (e.g., MUC7, MUC8, MUC9, and MUC20) [ 17 , 18 , 19 ]. MUC1, the best-characterized transmembrane mucin, has a variable number of highly glycosylated, 20-amino acid tandem repeats (VNTR), a sperm protein-enterokinase-agarin (SEA) domain (extracellular), a transmembrane domain, and a 72-amino acid cytoplasmic tail domain that extends up to 200–500 nm out of the cell surface ( Figure 1 A) [ 20 , 21 , 22 , 23 ].…”
Section: The Structure Of Muc1mentioning
confidence: 99%
“…The adhesion strategy used by hagfishes ( Myxine glutinosa ) is based on cross-linked networks made from mucin-like glycoproteins and protein filaments. Mucins are large glycoproteins that are ubiquitous in the animal kingdom, where they are involved in a broad range of functions such as providing anti-bacterial/anti-viral barriers, lubricity and tissue hydration [ 231 , 232 ]. The chemical structure of the mucin glycoproteins can be simply described as the protein core domain where serine and threonine residues are connected to branched oligosaccharides through O -glycoside bonds [ 233 ].…”
Section: Chemistry Of Biological Adhesives and Their Biomedical Applicationsmentioning
confidence: 99%
“…The individual qniumucins can then oligomerize and form a network. Differently from mammalian mucins, where oligomerization is established via cysteines [ 231 ], the content of cysteines in qniumucin is comparably low [ 242 ]. Based on NMR investigations, Uzawa et al.…”
Section: Chemistry Of Biological Adhesives and Their Biomedical Applicationsmentioning
confidence: 99%
“…Although we are able to extract and purify different types of mucins from animals, humans, or other organisms, [95] development and testing of bacterial and plant-based extracellular polymeric substances are still important and desirable since biological mucin coated surfaces, particularly developed for implants, do not always provide a broad spectrum biofilm growth prevention, limited by the bound glycans. [96] Snail mucins may overcome this problem as they are becoming increasingly popular.…”
Section: Snail Produced Mucin Proteinsmentioning
confidence: 99%