Synthesis and secretion of an albumin-like protein by cultured bovine tracheal gland serous cells

Jacquot, Jacky; Goldstein, Gary; Sommerhoff, Christian P.; Benali, Rachid; Puchelle, Édith; Basbaum, Carol

doi:10.1016/s0006-291x(88)80574-6

Cited by 16 publications

(9 citation statements)

References 9 publications

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“…Since proteins in ASL are numerous and their concentrations are unknown, we used albumin as a generic polypeptide during microtitrations. While this is clearly an oversimplification, it is compatible with the early studies reporting synthesis and release of “albumin-like” protein from submucosal gland acinar cells (Jacquot et al, 1988). Albumin caused significant buffering at 1–10 mg/ml and would contribute to the buffer capacity of ASL, especially at low pH.…”

Section: Discussionsupporting

confidence: 79%

“…Protein is released into the airway lumen passively (exudates), by transepithelial transport (Webber and Widdicombe, 1989), and can be synthesized and released by submucosal gland acinar cells (Jacquot et al, 1988). Airway secretions, which were reported to contain “albumin-like protein” (Jacquot et al, 1988), have more recently been found to comprise ~175 proteins.…”

Section: Resultsmentioning

confidence: 99%

“…Airway secretions, which were reported to contain “albumin-like protein” (Jacquot et al, 1988), have more recently been found to comprise ~175 proteins. To estimate the buffer capacity that may be mediated by proteins we used albumin as a model protein.…”

Section: Resultsmentioning

confidence: 99%

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The buffer capacity of airway epithelial secretions

2014

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The pH of airway epithelial secretions influences bacterial killing and mucus properties and is reduced by acidic pollutants, gastric reflux, and respiratory diseases such as cystic fibrosis (CF). The effect of acute acid loads depends on buffer capacity, however the buffering of airway secretions has not been well characterized. In this work we develop a method for titrating micro-scale (30 μl) volumes and use it to study fluid secreted by the human airway epithelial cell line Calu-3, a widely used model for submucosal gland serous cells. Microtitration curves revealed that HCO−3 is the major buffer. Peak buffer capacity (β) increased from 17 to 28 mM/pH during forskolin stimulation, and was reduced by >50% in fluid secreted by cystic fibrosis transmembrane conductance regulator (CFTR)-deficient Calu-3 monolayers, confirming an important role of CFTR in HCO−3 secretion. Back-titration with NaOH revealed non-volatile buffer capacity due to proteins synthesized and released by the epithelial cells. Lysozyme and mucin concentrations were too low to buffer Calu-3 fluid significantly, however model titrations of porcine gastric mucins at concentrations near the sol-gel transition suggest that mucins may contribute to the buffer capacity of ASL in vivo. We conclude that CFTR-dependent HCO−3 secretion and epithelially-derived proteins are the predominant buffers in Calu-3 secretions.

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Section: Discussionsupporting

confidence: 79%

Section: Resultsmentioning

confidence: 99%

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The buffer capacity of airway epithelial secretions

2014

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“…Three major polypeptides of apparent M, values of 67 000, 47 000 and 32 000 respectively (lane 1, FCS), were found at greatly increased levels in the medium from cells cultured in RPMI/lO% FCS compared to those of medium from cells cultured in RPM1/2% UG (lane 1, UG). Based on the molecular weight, immunoreactive cross-reactivity and surface molecular charge characteristics, the labeled M, 67 000 protein band has previously been identified as an albumin-like protein [4]. The amount of albumin-like supplemented medium, albumin-like protein is inprotein released during the 3.5 h pulse (lane 1, FCS) hibited 95% whereas lysozyme synthesis is stimulated and 1 h chase (lane 2, FCS), was approximately 25 ng in Ultroser G-supplemented medium.…”

Section: Resultsmentioning

confidence: 99%

“…Recently, we have demonstrated that an albumin-like protein is synthesized de novo by cultured bovine tracheal gland serous cells maintained in serum-supplemented medium [4]. The major site of albumin synthesis is the liver [5].…”

Section: Introductionmentioning

confidence: 99%

Modulation of albumin‐like protein and lysozyme production by bovine tracheal gland serous cells

et al. 1990

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Bovine tracheal submucosal gland serous cells were cultured in medium supplemented with either 10% fetal calf serum or 2% Ultroser G, a commercial serum substitute for cell culture. The proteins synthesized and secreted into the culture medium during PsS]methionine pulse, chase and isoproterenol-stimulated periods were analyzed. Marked differences in the patterns of secretory radiolabeled proteins with M, values ranging from 15080 to 95000 were observed between pulse and chase media of cells cultured in fetal calf serum and Ultroser G. In the presence of Ultroser G, albumin-like protein production was inhibited 9596 as compared to cultures incubated with fetal calf serum. A bovine lysoxyme-type enzymatic activity was detected only in medium from stimulated cells cultured in Ultroser G. The results suggest that bovine tracheal serous cells synthesize different proteins according to the composition of culture medium and release certain proteins when adrenergically stimulated.

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Proteins of the mineral compartment of bovine fetal enamel share common antigenic determinants with serum proteins

et al. 1990

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Two fractions were separated from the proteins of the mineral compartment of bovine developing enamel on the basis of their affinity for the lectin concanavalin-A. A monoclonal antibody was prepared by the hybridoma technique against the Con-A-binding fraction. This antibody and a commercial polyclonal antibody against bovine serum albumin were used to examine the relationship between those proteins, serum albumin and alpha-2HS glycoprotein, two proteins concentrated within dentin and bone matrices. The Con-A-unbound fraction reacted with the anti-albumin antibody and the antibody against the Con-A-binding fraction recognized the alpha-2HS glycoprotein. These data fully support the presence of significant levels of proteins related to serum components in the mineral compartment of developing enamel matrix.

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Synthesis and secretion of an albumin-like protein by cultured bovine tracheal gland serous cells

Cited by 16 publications

References 9 publications

The buffer capacity of airway epithelial secretions

The buffer capacity of airway epithelial secretions

Modulation of albumin‐like protein and lysozyme production by bovine tracheal gland serous cells

Proteins of the mineral compartment of bovine fetal enamel share common antigenic determinants with serum proteins

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