ArticleAmerican journal of physiology. Lung cellular and molecular physiology2016
Biosynthesis of the polymeric gel-forming mucin MUC5B.
Article in American journal of physiology. Lung cellular and molecular physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 28 citations in OpenAlex.
- Intranasal micro-optical coherence tomography imaging for cystic fibrosis studies.Science translational medicine · 2019Trial
- Airway Mucosal Defense: Mucins, Innate Immunity, and Contemporary Mucoactive Strategies.Biomedicines · 2026Review
- Simple and accessible methods for quantifying isolated mucins for further evaluation.MethodsX · 2025Article
- Structure of the MUC5AC VWD3 assembly responsible for the formation of net-like mucin polymers.EMBO reports · 2025Article
- A technical note on the Kamranmeter; a manually operated device for measuring salivary spinnbarkeit.Clinical oral investigations · 2024Article
- Emerging cell and molecular targets for treating mucus hypersecretion in asthma.Allergology international : official journal of the Japanese Society of Allergology · 2024Review
- Exploring the Correlation between Salivary Spinnbarkeit and Caries Scores.Caries research · 2024Article
- Mucins and their receptors in chronic lung disease.Clinical & translational immunology · 2020Article
- The MUC5B mucin polymer is dominated by repeating structural motifs and its topology is regulated by calcium and pH.Scientific reports · 2019Article
- Mucin CYS domain stiffens the mucus gel hindering bacteria and spermatozoa.Scientific reports · 2019Article
- The C-terminal dimerization domain of the respiratory mucin MUC5B functions in mucin stability and intracellular packaging before secretion.The Journal of biological chemistry · 2019Article
- A glycopolymer improves vascoelasticity and mucociliary transport of abnormal cystic fibrosis mucus.JCI insight · 2019Article
- Intracellular Processing of Human Secreted Polymeric Airway Mucins.Annals of the American Thoracic Society · 2018Review
- Mucins: the frontline defence of the lung.Biochemical Society transactions · 2018Review
- Role of mucins in lung homeostasis: regulated expression and biosynthesis in health and disease.Biochemical Society transactions · 2018Review
- Functional characterization of the mucus barrier on theProceedings of the National Academy of Sciences of the United States of America · 2018Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
MUC5B is a major polymeric mucin in the airway mucus gel and is an essential component of innate defense of the respiratory epithelium. Knowledge of the synthesis and intracellular processing of MUC5B is incomplete. We investigated the molecular details of MUC5B assembly in primary human bronchial epithelial cells (HBECs) grown at an air-liquid interface (ALI). Electrophoretic and centrifugal separations of intracellular forms of MUC5B probed with antibodies specific for non-O-glycosylated and O-glycosylated forms of the mucin identified three major intracellular populations of MUC5B (non-O-glycosylated monomer and dimer, and O-glycosylated polymers). Biophysical analysis of recombinant MUC5B COOH-terminus (CT5B; D4-B-C-CK) expressed in 293-EBNA cells showed that MUC5B dimerizes by disulfide linkage. Pulse-chase studies in the HBEC ALI cultures showed that non-O-glycosylated MUC5B was synthesized within 20 min of metabolic labeling and O-glycosylated, polymeric mucin within 2 h. Radiolabeled O-glycosylated mucin polymers were secreted within 2 h and the majority were released by 48 h. These data indicate that MUC5B follows a similar assembly to the related glycoprotein, von Willebrand factor (vWF); however, unlike vWF the MUC5B polypeptide shows no evidence of major proteolytic processing of D-domains during the production of the mature secreted polymeric mucin in normal and cystic fibrosis (CF) primary bronchial epithelial cells. In contrast, MUC5B D-domains were modified by neutrophil elastase, a protease commonly found in CF sputum, demonstrating that proteolytic degradation of MUC5B is an extracellular event in CF sputum. These results define the pathway for synthesis of MUC5B in primary human goblet cells.
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