Mucus glycoprotein secretion by duodenal mucosa in response to luminal arachidonic acid

1986 ◽  
Vol 884 (3) ◽  
pp. 419-428 ◽  
Author(s):  
Malgorzata Kosmala ◽  
Steven R. Carter ◽  
Stanislaw J. Konturek ◽  
Amalia Slomiany ◽  
Bronislaw L. Slomiany
Keyword(s):  
Arachidonic Acid ◽  
Duodenal Mucosa ◽  
Mucus Glycoprotein ◽  
Glycoprotein Secretion

VIP augments cholinergic-induced glycoconjugate secretion in tracheal submucosal glands

1988 ◽  
Vol 65 (6) ◽  
pp. 2537-2544 ◽  
Author(s):  
S. Shimura ◽  
T. Sasaki ◽  
K. Ikeda ◽  
H. Sasaki ◽  
T. Takishima
Keyword(s):  
Vasoactive Intestinal Peptide ◽  
Secretory Cells ◽  
Cholinergic Stimulation ◽  
Low Concentration ◽  
Mucus Glycoprotein ◽  
Submucosal Glands ◽  
Glycoprotein Secretion ◽  
Dose Dependent Increase ◽  
Dose Dependent

Using isolated submucosal glands from feline trachea, we examined the effect of vasoactive intestinal peptide (VIP) on mucus glycoprotein secretion and glandular contraction by measuring released radiolabeled glycoconjugates and induced tension, respectively. VIP (10(-10) to 10(-6) M) produced a dose-dependent increase in [3H]glycoconjugate release of up to 300% of controls, which was inhibited by VIP antiserum and not inhibited by atropine, propranolol, or phentolamine. VIP at a low concentration (10(-9) M), which did not produce any significant increases over controls, produced a 2.4- to 5-fold augmentation of the glycoconjugate release induced by 10(-9) to 10(-7) M methacholine (MCh). Atropine or VIP antiserum abolished the augmentation. VIP did not produce any alteration in isoproterenol- or phenylephrine-evoked glycoconjugate secretion. VIP (up to 10(-5) M) did not produce any alteration in the tension, even when the gland had contracted with MCh, or any augmentation of contraction induced by MCh (10(-9) to 10(-7) M). These results indicate that VIP induces mucus glycoprotein release from secretory cells and also that it potentiates the secretion induced by cholinergic stimulation.

Intracellular calcium concentration of acinar cells in feline tracheal submucosal glands

1990 ◽  
Vol 259 (6) ◽  
pp. L345-L350 ◽  
Author(s):  
H. Ishihara ◽  
S. Shimura ◽  
M. Sato ◽  
T. Masuda ◽  
N. Ishide ◽  
...  
Keyword(s):  
Acinar Cells ◽  
Ion Concentration ◽  
Free Calcium ◽  
Adrenergic Agonists ◽  
Initial Transient ◽  
Mucus Glycoprotein ◽  
Transient Rise ◽  
Submucosal Glands ◽  
Dose Dependent Fashion ◽  
Glycoprotein Secretion

We measured the intracellular free calcium ion concentration [( Ca2+]i) of acinar cells in isolated feline tracheal submucosal glands in response to secretagogues using the Ca2(+)-sensitive fluorescent dye fura-2. The secretagogues included cholinergic, adrenergic agonists, substance P (SP), and vasoactive intestinal polypeptide (VIP) which induce mucus glycoprotein secretion from feline tracheal submucosal glands. Methacholine (MCh) produced a significant increase in [Ca2+]i of up to 9.8 times that of control in a dose-dependent fashion at concentrations of 10(-8) to 10(-3) M. [Ca2+]i increase by MCh reached a peak within 30 s after stimulation and thereafter showed a sustained rise. In Ca2(+)-free medium, MCh produced an initial transient rise, which was less than 30% of that in a Ca2(+)-containing solution, and which lasted for 60 s with no prolonged sustained rise in [Ca2+]i. Atropine abolished MCh-evoked [Ca2+]i increase. Phenylephrine and SP produced a prolonged increase in [Ca2+]i without an initial transient increase. Phenylephrine (up to 10(-4) M) evoked an increase in [Ca2+]i by up to 240% that of control, which was abolished by prazosin. SP (up to 10(-4) M) also evoked an increase in [Ca2+]i by 155% that of control, which was abolished by atropine. By contrast, both isoproterenol (up to 10(-5) M) and VIP (up to 10(-5) M) failed to alter [Ca2+]i. These findings indicate that the mucus glycoprotein secretion evoked by muscarinic cholinergic, alpha-adrenergic agonist or SP can be mediated by intracellular Ca2+, whereas that by beta-adrenergic agonists or VIP cannot.

Effect of Lipoxygenase Inhibition on Mucous Glycoprotein Secretion from Chinchilla Middle Ear Fpithelial Cells in Vitro

1996 ◽  
Vol 105 (11) ◽  
pp. 916-921 ◽  
Author(s):  
Jizhen Lin ◽  
Youngki Kim ◽  
Frank Ondrey ◽  
Chris Lees ◽  
Steven K. Juhn
Keyword(s):  
Arachidonic Acid ◽  
Epithelial Cells ◽  
Middle Ear ◽  
Platelet Activating Factor ◽  
Lipoxygenase Inhibitor ◽  
Lipoxygenase Inhibition ◽  
Arachidonic Acid Metabolites ◽  
Acid Metabolites ◽  
Glycoprotein Secretion

Lipoxygenase is an enzyme that metabolizes arachidonic acid down to leukotrienes. Recent studies have shown that the enzyme is implicated in mucous glycoprotein (MGP) secretion stimulated by inflammatory mediators in the airways, suggesting its possible role in secretion of MGP from middle ear epithelial cells. To investigate a correlation between MGP secretion and the arachidonic acid metabolites, we examined the effects of nordihydroguaretic acid (NDGA, both a cyclooxygenase and lipoxygenase inhibitor), low-dose indomethacin (an inhibitor of cyclooxygenase), and A63162 (an inhibitor of lipoxygenase) on MGP secretion in cultured chinchilla middle ear epithelial cells. It was found that lipoxygenase inhibition led to reduction of MGP secretion from cultured chinchilla middle ear epithelial cells, while cyclooxygenase inhibition did not. Both cyclooxygenase and lipoxygenase inhibition resulted in profound blockage of MGP secretion in baseline and platelet activating factor-stimulated MGP secretion. It was concluded, therefore, that MGP secretion was linked to arachidonic acid metabolites, especially lipoxygenase products.

P2 purinergic receptor regulation of mucus glycoprotein secretion by rabbit gastric mucous cells in a primary culture

1994 ◽  
Vol 106 (6) ◽  
pp. 1485-1492 ◽  
Author(s):  
Shinichi Ota ◽  
Kenta Yoshiura ◽  
Morio Takahashi ◽  
Yasuo Hata ◽  
Osami Kohmoto ◽  
...  
Keyword(s):  
Primary Culture ◽  
Purinergic Receptor ◽  
Receptor Regulation ◽  
Mucous Cells ◽  
Mucus Glycoprotein ◽  
Glycoprotein Secretion ◽  
Gastric Mucous

Fish oil (eicosapentaenoic acid) inhibits two pathways of mucus glycoprotein secretion in gallbladder epithelial cells

2000 ◽  
Vol 118 (4) ◽  
pp. A714-A715 ◽  
Author(s):  
Masato Abei ◽  
Michio Shimizu ◽  
Matsuzaki Yasushi ◽  
Junichi Shoda ◽  
Naomi Tanaka
Keyword(s):  
Epithelial Cells ◽  
Eicosapentaenoic Acid ◽  
Fish Oil ◽  
Mucus Glycoprotein ◽  
Glycoprotein Secretion

Mucin Secretion by Duodenal Mucosa in Response to Arachidonic Acid

1988 ◽  
Vol 529 (1 Fourth Colloq) ◽  
pp. 250-253 ◽  
Author(s):  
M. KOSMALA ◽  
S. R. CARTER ◽  
J. BILSKI ◽  
A. SLOMIANY ◽  
B. L. SLOMIANY
Keyword(s):  
Arachidonic Acid ◽  
Duodenal Mucosa ◽  
Mucin Secretion

Use of the ileal conduit as a model for studying human small intestinal mucus glycoprotein secretion

1991 ◽  
Vol 261 (5) ◽  
pp. G728-G734 ◽  
Author(s):  
A. M. Roberton ◽  
B. Rabel ◽  
C. A. Harding ◽  
C. Tasman-Jones ◽  
P. J. Harris ◽  
...  
Keyword(s):  
Ileal Conduit ◽  
Human Model ◽  
Enzyme Linked Immunosorbent Assay ◽  
Specific Enzyme ◽  
Individual Subject ◽  
Mucus Glycoprotein ◽  
Experimental Systems ◽  
Intestinal Mucus ◽  
Small Intestinal ◽  
Glycoprotein Secretion

To establish a human model system for investigating control of mucus secretion by the small intestine, we have studied the output of mucus glycoprotein in the urine of patients with ileal conduits. A highly specific enzyme-linked immunosorbent assay (ELISA) was used to measure mucus glycoprotein with a sensitivity down to 0.3 ng protein of mucus glycoprotein. The assay detects human ileal mucus glycoprotein in the urine of ileal conduit patients; for an individual subject, the amount hardly varied from day to day, although there were substantial differences between individuals in the amounts secreted. Control urine from persons with normal bladders did not contain any mucus glycoprotein that reacted in the ELISA. The model has many advantages over other experimental systems for studying the rate of mucus glycoprotein secretion from the human ileum and can also be used as a reproducible resource of undegraded mucus glycoprotein.

Substance P and Mucus Glycoprotein Secretion

1987 ◽  
Vol 66 (2) ◽  
pp. 588-589 ◽  
Author(s):  
N. Fleming ◽  
P.T. Bilan ◽  
E. Sliwinski-Lis
Keyword(s):  
Substance P ◽  
Mucus Glycoprotein ◽  
Glycoprotein Secretion
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