LTB4-induced Nasal Gland Serous Cell Secretion Mediated by Neutrophil Elastase

1999 ◽  
Vol 160 (2) ◽  
pp. 411-414 ◽  
Author(s):  
LARS-OLAF CARDELL ◽  
CARLOS AGUSTÍ ◽  
KIYOSHI TAKEYAMA ◽  
PÄR STJÄRNE ◽  
JAY A. NADEL
Keyword(s):  
Neutrophil Elastase ◽  
Cell Secretion ◽  
Serous Cell

Neural regulation of lysozyme secretion from tracheal submucosal glands of ferrets in vivo

1991 ◽  
Vol 71 (3) ◽  
pp. 939-944 ◽  
Author(s):  
B. Davis ◽  
H. C. Tseng
Keyword(s):  
Substance P ◽  
Peripheral Nerves ◽  
Specific Marker ◽  
Cell Secretion ◽  
P Content ◽  
Submucosal Glands ◽  
Serous Cell ◽  
The Central Nervous System

To investigate how central and peripheral nerves affect lysozyme secretion from tracheal submucosal glands in ferrets we injected substance P (20 nmol/kg in 200 microliters) intracisternally or intravenously into anesthetized artificially ventilated ferrets. We collected 3-ml samples from a perfused (3 ml/5 min) segment of trachea in situ during 15 min before and 45 min after injection of substance P. Content of lysozyme, a specific marker of tracheal submucosal gland serous cell secretion in ferrets, was measured spectrophotometrically in each sample. Intracisternal substance P increased peak lysozyme output threefold compared with baseline. This increase was abolished completely by cutting both superior laryngeal nerves (SLN) and was partially inhibited by atropine, phentolamine, or propranolol. Intravenous substance P increased peak lysozyme output 10-fold compared with baseline. This increase was partly abolished by cutting both SLN. We concluded that intracisternal substance P stimulated the central nervous system (CNS) and activated cholinergic, adrenergic, and nonadrenergic noncholinergic secretomotor nerves to tracheal glands and that intravenous substance P increased lysozyme secretion both by acting directly on tracheal glands and indirectly on the CNS to activate secretomotor nerves.

Transport of albumin by the rabbit trachea in vitro

1990 ◽  
Vol 68 (2) ◽  
pp. 726-730 ◽  
Author(s):  
A. M. Price ◽  
S. E. Webber ◽  
J. G. Widdicombe
Keyword(s):  
Bovine Serum Albumin ◽  
Sodium Cyanide ◽  
Organ Bath ◽  
Submucosal Gland ◽  
Cell Secretion ◽  
Mucosal Transport ◽  
Submucosal Glands ◽  
Serous Cell ◽  
Fluorescent Dextran

The rabbit whole trachea was mounted in vitro in an organ bath containing Krebs-Henseleit (KH) solution. When the trachea was air filled there was no resting secretion and none was induced by methacholine (0.02 mM). Histology showed that the trachea has very few submucosal glands. When the trachea was filled with KH, with fluorescent bovine serum albumin in the surrounding KH solution, the rate of transport of albumin into the lumen was measured. Methacholine (0.02 mM) and phenylephrine (0.1 mM) more than doubled the output of albumin, and albuterol (0.1 mM) increased it more than fourfold. Cooling the preparation to 4 degrees C decreased the spontaneous output of albumin to less than one-half control and abolished the increase in output due to albuterol. Addition of sodium cyanide (1 mM) to the preparation abolished the increase in albumin transport due to albuterol. Serosal-to-mucosal transport of fluorescent dextran (mol wt 70,000) was less than one-third that of albumin and was not enhanced by methacholine, phenylephrine, or albuterol. Lysozyme output, an index of serous cell secretion, was barely detectable in controls and was not enhanced by any of the drugs. We conclude that the rabbit trachea has no measurable submucosal gland secretion and that it can actively transport albumin into the lumen via the epithelium. The transport rate is enhanced by methacholine, phenylephrine, and especially by albuterol.

scholarly journals Rhinovirus infection induces mucus hypersecretion

1998 ◽  
Vol 274 (6) ◽  
pp. L1017-L1023 ◽  
Author(s):  
Atsushi Yuta ◽  
William J. Doyle ◽  
Ethan Gaumond ◽  
Mushtaq Ali ◽  
Lawrence Tamarkin ◽  
...  
Keyword(s):  
Common Cold ◽  
Lavage Fluid ◽  
Blue Staining ◽  
Alcian Blue Staining ◽  
Cell Secretion ◽  
Rhinovirus Infection ◽  
Prominent Symptom ◽  
Serous Cell ◽  
The Common ◽  
Gel Phase

Rhinorrhea is a prominent symptom of the common cold. Although increases in vascular permeability and serous cell secretion have been demonstrated in human nasal mucus during active rhinovirus infections, changes in mucin constituents have not been quantified. Nonallergic ( n= 48) and asymptomatic allergic rhinitis ( n = 32) subjects were inoculated with rhinovirus type hanks before the spring allergy season. Nasal lavages were performed before inoculation ( day 0), then daily for 5 days afterward. The subjects were divided into infected and noninfected groups on the basis of evidence of successful rhinovirus infection (nasal shedding of virus or fourfold increases in specific serum antibodies). Concentrations of interleukin (IL)-8, markers of vascular leak (IgG), seromucous cells (lysozyme), and mucoglycoprotein exocytosis [7F10-immunoreactive mucin (7F10-irm) and Alcian blue staining of acidic mucoglycoproteins] were measured in lavage fluids. The infected subgroup had maximal increases in nasal lavage fluid concentrations of IL-8 (sevenfold), IgG (fourfold), total protein (twofold), and gel-phase 7F10-irm (twofold) on day 3. There were no differences between infected allergic and nonallergic subjects. IL-8 and gel-phase 7F10-irm were significantly higher in infected than in noninfected subjects. In addition to promoting plasma exudation, rhinovirus hanks infection increases IL-8 and gel-phase mucin secretion. These processes may contribute to a progression from watery rhinorrhea to mucoid discharge, with mild neutrophilic infiltration during the common cold.

Bombesin stimulates human nasal mucous and serous cell secretion in vivo

1992 ◽  
Vol 262 (1) ◽  
pp. L48-L52 ◽  
Author(s):  
J. N. Baraniuk ◽  
P. B. Silver ◽  
J. D. Lundgren ◽  
P. Cole ◽  
M. A. Kaliner ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Vascular Permeability ◽  
Total Protein ◽  
Mucous Cell ◽  
Sensory Nerves ◽  
Cell Marker ◽  
Cell Secretion ◽  
Submucosal Glands ◽  
Serous Cell

Bombesin, gastrin-related peptide (GRP), and related peptides sharing the common carboxyterminal sequence stimulate lactoferrin (serous cell marker) and glycoconjugate (mucous cell and goblet cell marker) release from human nasal mucosal explants in vitro. In vivo, GRP released from trigeminal sensory nerves may act upon GRP-bombesin binding sites on respiratory epithelial cells and submucosal glands. To determine whether GRP-bombesin can stimulate nasal secretion in vivo, bombesin was administered to eight normal subjects by unilateral, topical administration. Secretions from both nostrils were collected for measurement of total protein, lysozyme, hexose-containing glycoconjugates, and albumin (marker of vascular permeability). Baseline secretions contained 72.0 +/- 17.3 micrograms/ml of total protein, 14 +/- 2 micrograms/ml of lysozyme, 113 +/- 44 micrograms/ml of hexose-containing glycoconjugates, and 7.8 +/- 3.4 micrograms/ml of albumin. Hexose-containing glycoconjugate secretion was significantly increased after 1 nmol (385 +/- 63 micrograms/ml, P less than 0.001 by analysis of variance), 10, 100, and 1,000 nmol of bombesin, but the secretion was not dose dependent. Significant lysozyme (24 +/- 3 micrograms/ml, P less than 0.05) and total protein (155 +/- 23 micrograms/ml, P less than 0.01) secretion occurred after 1,000 nmol. No statistically significant changes in albumin secretion occurred at any dose. Saline had no significant effects on secretion. Therefore, bombesin stimulated secretion from submucosal glands and possibly epithelial cells in the human nose without affecting vascular permeability.

Interaction between bacterial peptides, neutrophils and goblet cells: a possible mechanism for neutrophil recruitment and goblet cell depletion in colitis

2001 ◽  
Vol 101 (4) ◽  
pp. 395-402 ◽  
Author(s):  
Keith LEIPER ◽  
Barry J. CAMPBELL ◽  
Michael D. JENKINSON ◽  
Jeremy MILTON ◽  
Lu-Gang YU ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Cell Lines ◽  
Goblet Cell ◽  
Neutrophil Elastase ◽  
Specific Inhibitor ◽  
Cell Depletion ◽  
Mucosal Inflammation ◽  
Cell Secretion ◽  
Colon Cancer Cell Lines ◽  
Activated Neutrophils

Goblet cell depletion occurs in various forms of colitis, but its mechanism is unknown. We have investigated two linked hypotheses: (i) that bacterial peptides, such as formyl-methionyl-leucyl-phenylalanine (fMLP), interact with epithelial cells inducing the release of chemokines, including interleukin-8 (IL-8), which in turn leads to the recruitment of neutrophils which release mucin secretagogues; (ii) that fMLP acts directly on epithelial cells to cause mucus secretion. Studies were performed to measure the effects of fMLP on the synthesis and secretion of IL-8 and mucus by the goblet cell differentiated colon cancer cell lines HT29-MTX (methotrexate-conditioned HT29 colonic adenocarcinoma cell line) and LS174T, and to assess the effects of neutrophil-derived secretagogues on goblet cell secretion in these cell lines. fMLP (0.1μM) increased the secretion of IL-8 by 105% (P < 0.0001) in HT29-MTX cells and by 401% (P < 0.0001) in LS174T cells. fMLP also increased the synthesis and secretion of mucins by these cell lines, with maximal effects of 65% above control values for synthesis (P < 0.01) and 73% for secretion (P < 0.01). A dose-related increase (up to 67%; P < 0.01) in mucin secretion was demonstrated in HT29-MTX cells in response to incubation with supernatant from activated neutrophils. This effect was largely (83%; P < 0.02) inhibited by ICI 200,355, a specific inhibitor of neutrophil elastase. In conclusion, the bacterial peptide fMLP and neutrophil elastase are both potent mucus secretagogues for colon epithelial cells. fMLP also elicits release of the potent neutrophil chemoattractant IL-8 from colon epithelial cells. These findings support the hypothesis that the mucosal inflammation and mucus depletion seen in ulcerative colitis could result from interaction between bacterial peptides and the mucosa.

scholarly journals Effect of IL-8 on airway goblet cell secretion: a role of neutrophil elastase.

Ensho ◽  
1994 ◽  
Vol 14 (2) ◽  
pp. 157-158
Author(s):  
Jun Tamaoki ◽  
Kiyoshi Takeyama ◽  
Etsuko Tagaya ◽  
Atsushi Chiyotani ◽  
Kimio Konno
Keyword(s):  
Goblet Cell ◽  
Neutrophil Elastase ◽  
Cell Secretion

262 Bombesin stimulates mucous and serous cell secretion in human nasal provocation tests

1991 ◽  
Vol 87 (1) ◽  
pp. 205 ◽  
Author(s):  
J BARANIUK ◽  
P BRAYTON ◽  
J LUNDGREN ◽  
P COLE ◽  
M KALINER ◽  
...  
Keyword(s):  
Cell Secretion ◽  
Provocation Tests ◽  
Nasal Provocation ◽  
Serous Cell

Prostaglandins alter methacholine-induced secretion in ferret in vitro trachea

1990 ◽  
Vol 258 (2) ◽  
pp. L75-L80 ◽  
Author(s):  
M. E. Deffebach ◽  
H. Islami ◽  
A. Price ◽  
S. E. Webber ◽  
J. G. Widdicombe
Keyword(s):  
Bovine Serum Albumin ◽  
Bovine Serum ◽  
Specific Marker ◽  
Albumin Concentration ◽  
Organ Bath ◽  
Cell Secretion ◽  
Serous Cell ◽  
Dose Dependent ◽  
Tracheal Secretion

The ferret trachea was mounted in an organ bath containing Krebs-Henseleit solution with additional bovine serum albumin (BSA). Tracheal secretions were collected and analyzed for albumin, and lysozyme, a specific marker of serous cell secretion. The total secretion volume and output and concentrations of albumin and lysozyme were calculated. Secretion was stimulated with methacholine (20 microM) (Mch), and the effects of the prostaglandins PGD2, PGE1, and PGF2 alpha on methacholine-induced secretion were studied. All responses were dose dependent. PGF2 alpha at 10(-5) M increased the volume of Mch-stimulated secretion twofold, the lysozyme output sixfold, and concentration over threefold, while decreasing the albumin transport by one-half. PGD2 at 10(-5) M reduced Mch-induced secretion volume to 75% control, increased albumin transport to 135%, without affecting lysozyme secretion. PGE1 at 10(-5) M increased Mch-stimulated albumin transport and concentration over twofold, decreased lysozyme release to less than one-third of control, and had no effect on secretion volume. PGE1 caused the albumin concentration to exceed that of the outer bath, indicating active transport. We conclude that prostaglandins selectively alter tracheal secretion induced by cholinergic stimuli.

Neutrophil Elastase Potentiates Cathepsin G-lnduced Platelet Activation

1992 ◽  
Vol 68 (05) ◽  
pp. 570-576 ◽  
Author(s):  
Mary A Selak
Keyword(s):  
Neutrophil Elastase ◽  
Cell Activation ◽  
Thromboxane A2 ◽  
Creatine Phosphate ◽  
Dense Granule ◽  
Cathepsin G ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Low Concentrations ◽  
High Concentrations

SummaryWe have previously demonstrated that human neutrophil cathepsin G is a strong platelet agonist that binds to a specific receptor. This work describes the effect of neutrophil elastase on cathepsin G-induced platelet responses. While platelets were not activated by high concentrations of neutrophil elastase by itself, elastase enhanced aggregation, secretion and calcium mobilization induced by low concentrations of cathepsin G. Platelet aggregation and secretion were potentiated in a concentration-dependent manner by neutrophil elastase with maximal responses observable at 200 nM. Enhancement was observed when elastase was preincubated with platelets for time intervals of 10–60 s prior to addition of a low concentration of cathepsin G and required catalytically-active elastase since phenylmethanesulphonyl fluoride-inhibited enzyme failed to potentiate cell activation. Neutrophil elastase potentiation of platelet responses induced by low concentrations of cathepsin G was markedly inhibited by creatine phosphate/creatine phosphokinase and/or indomethacin, indicating that the synergism between elastase and cathepsin G required the participation of ADP and thromboxane A2. On the other hand, platelet responses were not attenuated by the PAF antagonist BN 52021, signifying that PAF-acether did not play a role in elastase potentiation. At higher concentrations porcine pancreatic elastase exhibits similar effects to neutrophil elastase, demonstrating that the effect of elastase was not unique to the neutrophil protease. While neutrophil elastase failed to alter the ability of cathepsin G to hydrolyze a synthetic chromogenic substrate, preincubation of platelets with elastase increased the apparent affinity of cathepsin G binding to platelets. In contrast to their effect on cathepsin G-induced platelet responses, neither neutrophil nor pancreatic elasatse potentiated aggregation or dense granule release initiated by ADP, PAF-acether, arachidonic acid or U46619, a thromboxane A2 mimetic. Moreover, unlike its effect on cathepsin G, neutrophil elastase inhibited thrombin-induced responses. The current observations demonstrate that elastase can potentiate platelet responses mediated by low concentrations of cathepsin G, suggesting that both enzymes may function synergistically to activate platelets under conditions where neutrophil degranulation occurs.

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