Mucins: Structural diversity, biosynthesis, its role in pathogenesis and as possible therapeutic targets
Abstract
Mucins are the main structural components of mucus that create a selective protective barrier for epithelial surface and also execute wide range of other physiological functions. Mucins can be classified into two types, namely secreted mucins and membrane bounded mucins. Alterations in mucin expression or glycosylation and mislocalization have been seen in various types of pathological conditions such as cancers, inflammatory bowel disease and ocular disease, which highlight the importance of mucin in maintaining homeostasis. Hence mucins can be used as attractive target for therapeutic intervention. In this review, we discuss in detail about the structural diversity of mucins; their biosynthesis; its role in pathogenesis; regulation and as possible therapeutic targets.
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Secreted mucins are a family of heavily glycosylated proteins produced in epithelial cells in most animals and humans.
“Secreted mucins are a family of heavily glycosylated proteins produced in epithelial cells in most animals and humans [13,26].”
From Chemical Variability and Biological Potential of Cornu aspersum Mucus as a Source for the Development of New Cosmetic and Pharmaceutical Products (2025) · cites this paper as [26]
The length of the glycosylation domain and the number of repeats are individual for different mucins and determine their chemical and biological properties.
“The length of the glycosylation domain and the number of repeats are individual for different mucins and determine their chemical and biological properties.”
From Chemical Variability and Biological Potential of Cornu aspersum Mucus as a Source for the Development of New Cosmetic and Pharmaceutical Products (2025) · cites this paper as [26]
A mucin molecule consists of a long peptide chain (apomucin) and several hundred oligosaccharide chains attached to it; its central PTS/VNTR domain rich in serine, threonine, and proline serves as an anchor for glycosylation; the mucin adopts an extended bottle brush conformation and cysteine-rich sites form disulfide bonds.
“A mucin molecule consists of a long peptide chain (apomucin) and several hundred oligosaccharide chains attached to it. In the center of the protein backbone, there is a tandem repeat domain rich in serine, threonine, and proline, which is called the PTS (proline, threonine, serine) or VNTR (Variable Number Tandem Repeat) region. This domain serves as an anchor for glycosylation. The PTS domain is”
From Chemical Variability and Biological Potential of Cornu aspersum Mucus as a Source for the Development of New Cosmetic and Pharmaceutical Products (2025) · cites this paper as [26]
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Hudz, N., Turkina, V., Alyokhina, T., Motyka, O., Chemerys, N., Rumynska, T., Lozynskyi, A., Jasicka-Misiak, I., & Kobylinska, L. (2025) · Molecules · doi:10.3390/molecules30214197 · Cited by 4 · see citing works
- Authors
- Dhanisha, S. S., Guruvayoorappan, C., Drishya, S., & Abeesh, P.
- Affiliations
- Regional Cancer Center, Thiruvananthapuram (IN)
- Corresponding author
- Guruvayoorappan, Chandrasekharan
- Venue
- Critical Reviews in Oncology/Hematology
- Publisher
- Elsevier BV
- Published
- 2018-02
- Volume
- 122
- Pages
- 98-122
- ISSN
- 1040-8428 (ISSN-L)
- OpenAlex
- W2776567026
- Cited by
- 194
- References
- 4
- Citations by year
- 2026: 24 · 2025: 24 · 2024: 28 · 2023: 23 · 2022: 19 · 2021: 23 · 2020: 23 · 2019: 22 · 2018: 8
- FWCI
- 1.36
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Critical Reviews in Oncology/Hematology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Keywords
- mucin, mucus, mucin production, mucin glycosylation, secreted mucins, membrane-bound mucins, epithelial barrier function, cancer, inflammatory bowel disease, eye diseases
- MeSH terms
- Animals, Humans, Mucins, Neoplasms, Molecular Targeted Therapy
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