Literature DB >> 6394241

Some non-mucin components of mucus and their possible biological roles.

J R Clamp, J M Creeth.   

Abstract

Non-mucin components have essential roles in the protective functions of mucous secretions. Secretory IgA (SIgA) antibodies probably act by blocking the attachment of pathogenic microorganisms to mucosal cells. In addition SIgA1 may render bacteria more 'mucophilic', possibly by virtue of the 'mucus-like' stretch that the immunoglobulin molecule possesses. Lysozyme will attack cell walls of susceptible bacteria. As the enzyme associates strongly with mucus glycoproteins the mucus layer is provided with powerful bactericidal properties. Lactoferrin, normally unsaturated, sequesters any free iron in secretions, so exerting a bacteriostatic action on iron-requiring microorganisms. In addition it may protect mucus glycoproteins from iron-catalysed active oxygen species. This mucoprotective action would be overcome during infections. Attention is also directed towards a possible copper-mediated limited degradation by hydrogen peroxide. Surfactants and free lipid have long been recognized as components of normal bronchial mucus. For example, some lipid is tightly but non-covalently bound to a hydrophobic region of bronchial mucin. More intriguing is the presence of small amounts of covalently bound lipid in normal human gastric mucin. In addition, normal human gastric mucus contains significant amounts of a galactose-rich polysaccharide. The function of this is not known but it may act as a cross-linking strand in the mucus gel structure or as a renewable cell membrane component, perhaps interacting between glycocalyx and the mucus layer.

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Year:  1984        PMID: 6394241     DOI: 10.1002/9780470720905.ch9

Source DB:  PubMed          Journal:  Ciba Found Symp        ISSN: 0300-5208


  13 in total

Review 1.  Mucosal infection with Neisseria gonorrhoeae. Bacterial adaptation and mucosal defenses.

Authors:  M S Cohen; P F Sparling
Journal:  J Clin Invest       Date:  1992-06       Impact factor: 14.808

Review 2.  The role of bacterial adhesion in cystic fibrosis including the staphylococcal aspect.

Authors:  R Ramphal
Journal:  Infection       Date:  1990 Jan-Feb       Impact factor: 3.553

3.  Regulation of metal absorption in the gastrointestinal tract.

Authors:  M W Whitehead; R P Thompson; J J Powell
Journal:  Gut       Date:  1996-11       Impact factor: 23.059

4.  Structural and compositional differences between intracellular and secreted mucin of rat small intestine.

Authors:  R E Fahim; G G Forstner; J F Forstner
Journal:  Biochem J       Date:  1987-12-01       Impact factor: 3.857

5.  Keratin-like components of gland thread cells modulate the properties of mucus from hagfish (Eptatretus stouti).

Authors:  E A Koch; R H Spitzer; R B Pithawalla; S W Downing
Journal:  Cell Tissue Res       Date:  1991-04       Impact factor: 5.249

6.  Adhesion of Pseudomonas aeruginosa to respiratory mucins and expression of mucin-binding proteins are increased by limiting iron during growth.

Authors:  A Scharfman; H Kroczynski; C Carnoy; E Van Brussel; G Lamblin; R Ramphal; P Roussel
Journal:  Infect Immun       Date:  1996-12       Impact factor: 3.441

Review 7.  Chronic rhinosinusitis pathogenesis.

Authors:  Whitney W Stevens; Robert J Lee; Robert P Schleimer; Noam A Cohen
Journal:  J Allergy Clin Immunol       Date:  2015-12       Impact factor: 10.793

8.  Interactions between Yersinia enterocolitica and rabbit ileal mucus: growth, adhesion, penetration, and subsequent changes in surface hydrophobicity and ability to adhere to ileal brush border membrane vesicles.

Authors:  A Paerregaard; F Espersen; O M Jensen; M Skurnik
Journal:  Infect Immun       Date:  1991-01       Impact factor: 3.441

9.  Rat and human colonic mucins bind to and inhibit adherence lectin of Entamoeba histolytica.

Authors:  K Chadee; W A Petri; D J Innes; J I Ravdin
Journal:  J Clin Invest       Date:  1987-11       Impact factor: 14.808

10.  Studies of the limited degradation of mucus glycoproteins. The mechanism of the peroxide reaction.

Authors:  B Cooper; J M Creeth; A S Donald
Journal:  Biochem J       Date:  1985-06-15       Impact factor: 3.857

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