Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Human respiratory mucins.

G Lamblin1, J P Aubert, J M Perini

  • 1Unité INSERM N. 16, Lille, France.

The European Respiratory Journal
|February 1, 1992
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Clinical profiles of four patients with Rett syndrome carrying a novel exon 1 mutation or genomic rearrangement in the MECP2 gene.

Clinical genetics·2006
Same author

Eta' photoproduction on the proton for photon energies from 1.527 to 2.227 GeV.

Physical review letters·2006
Same author

Measurement of two- and three-nucleon short-range correlation probabilities in nuclei.

Physical review letters·2006
Same author

[Ulcerative gingivostomatitis and peridontitis].

HNO·2006
Same author

Search for Theta+ (1540) Pentaquark in High-Statistics Measurement of gammap-->K0K+n at CLAS.

Physical review letters·2006
Same author

[Hematopoietic stem cell transplantation for severe sickle cell disease].

Revue medicale de Bruxelles·2006

Human respiratory mucins are complex glycoproteins crucial for airway defense. Their diverse structures, driven by glycosylation, enable interactions with microorganisms to protect the respiratory mucosa.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Human respiratory mucins are key glycoproteins secreted by goblet cells and mucous glands.
  • Mucins are composed of diverse peptide cores (apomucins) encoded by multiple genes.
  • Glycosylation is a major post-translational modification, accounting for 70-80% of mucin weight.

Purpose of the Study:

  • To elucidate the structural complexity of human respiratory mucins.
  • To understand the role of glycosylation in mucin diversity.
  • To explore the implications of mucin structure for respiratory mucosal defense.

Main Methods:

  • Analysis of mucin peptide composition.
  • Characterization of O-glycosidically linked carbohydrate chains.

Related Experiment Videos

  • Investigating structure-function relationships in respiratory mucins.

    • Main Results:

    • Human respiratory mucins exhibit extraordinary diversity in O-glycosidically linked carbohydrate chains, with hundreds of unique chains per individual.
    • A wide array of mucin peptides (apomucins) contributes to the overall complexity.
    • The structural diversity suggests significant functional roles in host-microorganism interactions.

    Conclusions:

    • The intricate structure of respiratory mucins, particularly their extensive glycosylation, is vital for respiratory mucosal defense.
    • Mucin diversity facilitates interactions with microorganisms, potentially acting as a crucial barrier.
    • Understanding mucin complexity offers insights into respiratory health and disease mechanisms.