Immunologic and Neuropharmacologic Stimulation of Mucous Glycoprotein Release from Human Airways In Vitro

Shelhamer, James H.; Marom, Zvi; Kaliner, Michael

doi:10.1172/jci109993

Cited by 223 publications

(73 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Labeled mucins secreted in both periods were isolated from other labeled macromolecules using an automatic BioGel A-Sm gel filtration system (19) and counted using appropriate quench correction. DPM of Na235SO4 in 0.5 ml of the void volume fraction of P1 and P2 culture media were 16 (18,20,21). The index theoretically is 1.0 if mucin release is not stimulated or inhibited.…”

Section: Methodsmentioning

confidence: 99%

Proteinases of Pseudomonas aeruginosa evoke mucin release by tracheal epithelium.

et al. 1984

View full text Add to dashboard Cite

Abstract. We have determined the potential of exoproducts from pathogenic bacteria to stimulate the release of high molecular weight mucins from goblet cells of airway epithelium in a rabbit tracheal explant system. Culture supernatants from proteolytic strains of Pseudomonas aeruginosa and Serratia marcescens, but not supernatants from a number of non-proteolytic strains, released mucins from goblet cells. Highly purified elastase and alkaline proteinase from P. aeruginosa stimulated goblet cell mucin release in a dose-dependent fashion. Lipopolysaccharide, exotoxin A, and alginate of P. aeruginosa did not possess mucin release properties. Proteolytic activity was required for mucin release by P. aeruginosa elastase, but such release in goblet cells was not mediated by cyclic AMP. Morphologic studies suggested rapid release of mucins from goblet cells in response to elastase by a process resembling apocrine secretion. Several nonbacterial proteinases mimicked the effect of Pseudomonas proteases. These studies provide support for the hypothesis that bacterial and other proteinases play a role in the pathogenesis of mucus hypersecretion in acute and chronic lung infections.

show abstract

Section: Methodsmentioning

confidence: 99%

Proteinases of Pseudomonas aeruginosa evoke mucin release by tracheal epithelium.

et al. 1984

View full text Add to dashboard Cite

show abstract

“…The common carboxy-terminal sequence is essential for receptor recognition and biological activity. Other GRP-related peptides include GRP [18][19][20][21][22][23][24][25][26][27] (GRP [10]; neuromedin C), and GRP [14][15][16][17][18][19][20][21][22][23][24][25][26][27] (GRP [14]; references 3 and 4). GRP is located in nerve fibers (1) and pulmonary neuroendocrine cells (1), and can be detected in plasma (5,6).…”

Section: Introductionmentioning

confidence: 99%

Gastrin-releasing peptide in human nasal mucosa.

Baraniuk¹,

Lundgren²,

Goff³

et al. 1990

J. Clin. Invest.

View full text Add to dashboard Cite

Gastrin-releasing peptide (GRP), the 27 amino acid mammalian form of bombesin, was studied in human inferior turbinate nasal mucosa. The GRP content of the mucosa measured by radioimmunoassay was 0.60±0.25 pmol/g tissue (n = 9 patients; mean±SEM). GRP-immunoreactive nerves detected by the immunogold method of indirect immunohistochemistry were found predominantly in small muscular arteries, arterioles, venous sinusoids, and between submucosal gland acini.I25I-GRP binding sites determined by autoradiography were exclusively and specifically localized to nasal epithelium and submucosal glands. There was no binding to vessels. The effects of GRP on submucosal gland product release were studied in short-term explant culture. GRP (10 ALM) significantly stimulated the release of the serous cell-specific product lactoferrin, and [3Hlglucosamine-labeled glycoconjugates which are products of epithelial goblet cells and submucosal gland cells. These observations indicate that GRP released from nerve fibers probably acts on glandular GRP receptors to induce glycoconjugate release from submucosal glands and epithelium and lactoferrin release from serous cells, but that GRP would probably not affect vascular permeability. (J. Clin. Invest. 1990. 85:998-1005.) gastrin-releasing peptide -human inferior turbinate nasal mucosa * respiratory glycoconjugateslactoferrin * explant culture

show abstract

“…In addition, the labeled glycoprotein pool may also represent mucins derived from different secretory elements in the respiratory tract (goblet cells and/or submucosal glands). Furthermore, in the previous reports 7,8 the effects of INDO were obtained in tissues constantly exposed to hydrocortisone. The relative contribution of INDO to the increase glycoprotein release may therefore be difficult to determine.…”

Section: Discussionmentioning

confidence: 99%

“…7,8 Initial reports have indicated that exposure of human airway cultured cell explants to indomethacin caused an increase in mucus secretion, when the incorporation of 3 H-glucosamine was used as the index of glycoprotein secretory activity. 8 However, these data were obtained in tissues constantly exposed to hydrocortisone and therefore the direct effects of indomethacin may be compromised by the continuous steroid exposure.…”

Section: Introductionmentioning

confidence: 99%

MUC5AC mucin release from human airways in vitro: Effects of indomethacin and Bay X1005

Roger

Gascard

Bara

et al. 2001

Mediators of Inflammation

View full text Add to dashboard Cite

Immunologic and Neuropharmacologic Stimulation of Mucous Glycoprotein Release from Human Airways In Vitro

Cited by 223 publications

References 30 publications

Proteinases of Pseudomonas aeruginosa evoke mucin release by tracheal epithelium.

Proteinases of Pseudomonas aeruginosa evoke mucin release by tracheal epithelium.

Gastrin-releasing peptide in human nasal mucosa.

MUC5AC mucin release from human airways in vitro: Effects of indomethacin and Bay X1005

Contact Info

Product

Resources

About