A Purified Serum Glycopeptide from Controls and Cystic Fibrosis Patients. I. Comparison of their Mucociliary Activity on Rabbit Tracheal Explants

Blitzer, Miriam G.; Shapira, Emmanuel

doi:10.1203/00006450-198203000-00008

Cited by 17 publications

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“…In the present study, we used the hybridoma technique (9, 10) in an attempt to obtain specific monoclonal antibodies toward the purified glycopeptide with ciliary dyskinetic activity from CF patients and toward its normal counterpart (2). The advantage of having a continuous, unlimited supply of monoclonal antibody with a defined specificity toward an antigenic determinant will avoid the methodologic problems encountered by antisera adsorption.…”

Section: Discussionmentioning

confidence: 99%

“…In both the CF Eshhar, Weizmann Institute. The following purified glycoprotein and control glycopeptides, the protein components revealed the preparations were obtained: fetuin, ovalbumin, and bovine subabsence of aromatic amino acids, and the carbohydrate component maxillary mucin from Sigma Chemical Company, ribonuclease-B was shown to be deficient in sialic acid (2). and rabbit seromucoid from Worthington Biochemical CorporaAttempts to develop a quantitative, specific immunoassay to tion (Freehold, NJ), bovine transferrin from Miles Biochemicals detect Spock's ciliary dyskinetic factor in order to detect CF (Elkhart, IN), and lXI-acid glycoprotein from the American Red patients and heterozygotes have not been afforded much success.…”

Section: Speculationmentioning

confidence: 99%

“…The purified glycopeptide preparations from controls and CF patients were obtained as previously described (2). The samples were compared in a double-blind manner for ciliary dyskinetic activity on rabbit tracheal ex plants (2). All glycopeptide preparations from CF patients revealed ciliary dyskinetic activity, whereas the preparations from controls showed no biological activity on the explants.…”

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confidence: 99%

“…Monoclonal antibodies from these media were either used directly for experiments or were isolated by precipitation with ammonium sulfate at 45% saturation. Mouse IgG antibodies in these fractions were characterized by immunoelectrophoresis against goat antisera to mouse IgG, as previously described (2).…”

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confidence: 99%

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A Purified Serum Glycopeptide from Controls and Cystic Fibrosis Patients. II. Comparison of their Immunologic Properties Using Monoclonal Antibodies

Blitzer

Shapira

1982

Pediatr Res

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Section: Discussionmentioning

confidence: 99%

Section: Speculationmentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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A Purified Serum Glycopeptide from Controls and Cystic Fibrosis Patients. II. Comparison of their Immunologic Properties Using Monoclonal Antibodies

Blitzer

Shapira

1982

Pediatr Res

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Increased Binding of Limulin to α₂‐Macroglobulin and Immunoglobulin M from Cystic Fibrosis Patients

Owens‐Williams,

Shapira

1982

J. pediatr. gastroenterol. nutr.

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SummaryIn the present study the binding of limulin, a lectin with sialic acid specificity, to three serum glycoproteins from controls and cystic fibrosis patients was compared. α2‐Macroglobulin from patients with cystic fibrosis was shown to have significantly increased binding to the lectin limulin when compared to that from healthy controls (t = 3.6, p < 0.01). The binding of limulin to immunoglobulin M (IgM) from cystic fibrosis patients was also shown to be significantly higher than the binding to IgM from controls (t = 3.6, p < 0.01). whereas no detectable binding of fluorescein‐conjugated limulin to immunoglobulin G from either cystic fibrosis patients or controls was observed. These findings support the hypothesis that the underlying inherited defect in cystic fibrosis might be an abnormal synthesis or degradation of glycoproteins and glycopeptides.

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Secretory activity of hamster tracheal explants and isolated tracheal epithelial cells and the effects of cystic fibrosis serum

Rudick

Wooten

Rudick

1984

Journal Cellular Physiology

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Serum from cystic fibrosis patients has been shown by scanning electron microscopy to cause release of large quantities of mucus from the cultured tracheal rings of 3-4-month-old male Golden Syrian hamsters. In order to study this phenomenon on single cells, an epithelial (HTE) cell culture has been established from the hamster tracheal rings using the cell rescue method of Goldman and Baseman (1980a, In Vitro, 16:313). The cells were demonstrated to be epithelial by histochemical staining and immunofluorescent detection of laminin. Proteins secreted by HTE cells were partially characterized and shown to consist, at least in part, of acidic glycoproteins. The proteins were precipitated by addition of buffered alcian blue (AB) to the cell-free medium under conditions in which all of a polyanionic protein [3H]-labeled mucin, was precipitated without carrier. [14C] galactosamine-labeled AB precipitate was beta-eliminated and, after neutralization and centrifugation, the material in the supernatant was sized by chromatography on a calibrated Bio-Gel P2 column. The label eluted with a molecular weight close to a disaccharide. HTE cells pulse-labeled for 1.0 hr with [3H] leucine or [14C] galactosamine secreted increasing amounts of labeled glycoprotein during the chase. Sodium dodecylsulfate-polyacrylamide gel electrophoresis and fluorography of labeled AB precipitates revealed three major bands, two with molecular weights greater than 100 kd. Secretion was stimulated by retinoate (50% increase), but not by retinol. Exposure of HTE cells to whole sera from cystic fibrosis patients resulted in heightened secretion rates as compared to results obtained with normal sera. Heterozygote sera produced secretion rates intermediate between the two extremes.

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A Purified Serum Glycopeptide from Controls and Cystic Fibrosis Patients. I. Comparison of their Mucociliary Activity on Rabbit Tracheal Explants

Cited by 17 publications

References 13 publications

A Purified Serum Glycopeptide from Controls and Cystic Fibrosis Patients. II. Comparison of their Immunologic Properties Using Monoclonal Antibodies

A Purified Serum Glycopeptide from Controls and Cystic Fibrosis Patients. II. Comparison of their Immunologic Properties Using Monoclonal Antibodies

Increased Binding of Limulin to α₂‐Macroglobulin and Immunoglobulin M from Cystic Fibrosis Patients

Secretory activity of hamster tracheal explants and isolated tracheal epithelial cells and the effects of cystic fibrosis serum

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A Purified Serum Glycopeptide from Controls and Cystic Fibrosis Patients. I. Comparison of their Mucociliary Activity on Rabbit Tracheal Explants

Cited by 17 publications

References 13 publications

A Purified Serum Glycopeptide from Controls and Cystic Fibrosis Patients. II. Comparison of their Immunologic Properties Using Monoclonal Antibodies

A Purified Serum Glycopeptide from Controls and Cystic Fibrosis Patients. II. Comparison of their Immunologic Properties Using Monoclonal Antibodies

Increased Binding of Limulin to α2‐Macroglobulin and Immunoglobulin M from Cystic Fibrosis Patients

Secretory activity of hamster tracheal explants and isolated tracheal epithelial cells and the effects of cystic fibrosis serum

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Increased Binding of Limulin to α₂‐Macroglobulin and Immunoglobulin M from Cystic Fibrosis Patients