Mucin glycoprotein content of human pigment gallstones

J. T. LaMont, A. S. Ventola, B. W. Trotman, R. D. Soloway

Research output: Contribution to journalArticle

55 Citations (Scopus)

Abstract

Mucin glycoproteins, a secretory product of the gallbladder, are thought to contribute to the matrix or nucleus of gallstones. Human black pigment stones originate in the gallbladder and have as their major constituent calcium bilirubinate, as well as inorganic salts and small amounts of cholesterol. The object of this study was to estimate the amount of glycoprotein in black pigment stones and to isolate gallbladder mucin from dissolved stones. Black pigment stones containing 18 to 65% calcium bilirubinate were first dissolved in 12.5 mM EDTA/0.1 N NaOH and decolorized, then subjected to glycoprotein assay. The mean glycoprotein content of eight stones was 12.4%. In separate experiments, pigment stones were partially dissolved by brief exposure to EDTA/NaOH to minimize glycoprotein breakdown, and the glycoproteins isolated by gel filtration and ultracentrifugation. Pigment stones contained two glycoprotein fractions on Sepharose 4B; a high molecular weight mucin glycoprotein in the void volume and a lower molecular fraction in the included volume. Mucin was further purified by density gradient ultracentrifugation in cesium chloride. Three separate mucin fractions had an average buoyant density of 1.48 gm per ml which is typical for these glycoproteins. Bile pigment was associated with high molecular weight mucin even after extensive dialysis, gel filtration, and density gradient ultracentrifugation. The identify of mucin was further established by β-elimination of glycoproteins in alkaline borohydride which yielded galactosaminitol from cleavage of O-glycosidic bonds. Our results indicate that mucin glycoproteins are present in significant concentrations in human black pigment stones and can be purified from stones solubilized in EDTA/NaOH. The association of bile pigment with gallbladder mucin, even after extensive purification, is consistent with the hypothesis that mucin contributes to the matrix of pigment gallstones.

Original languageEnglish (US)
Pages (from-to)377-382
Number of pages6
JournalHepatology
Volume3
Issue number3
StatePublished - 1983
Externally publishedYes

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Gallstones
Mucins
Glycoproteins
Gallbladder
Ultracentrifugation
Bile Pigments
Edetic Acid
Bilirubin
Gel Chromatography
Molecular Weight
Borohydrides
Sepharose
Dialysis
Salts
Cholesterol

ASJC Scopus subject areas

  • Hepatology

Cite this

LaMont, J. T., Ventola, A. S., Trotman, B. W., & Soloway, R. D. (1983). Mucin glycoprotein content of human pigment gallstones. Hepatology, 3(3), 377-382.

Mucin glycoprotein content of human pigment gallstones. / LaMont, J. T.; Ventola, A. S.; Trotman, B. W.; Soloway, R. D.

In: Hepatology, Vol. 3, No. 3, 1983, p. 377-382.

Research output: Contribution to journalArticle

LaMont, JT, Ventola, AS, Trotman, BW & Soloway, RD 1983, 'Mucin glycoprotein content of human pigment gallstones', Hepatology, vol. 3, no. 3, pp. 377-382.
LaMont JT, Ventola AS, Trotman BW, Soloway RD. Mucin glycoprotein content of human pigment gallstones. Hepatology. 1983;3(3):377-382.
LaMont, J. T. ; Ventola, A. S. ; Trotman, B. W. ; Soloway, R. D. / Mucin glycoprotein content of human pigment gallstones. In: Hepatology. 1983 ; Vol. 3, No. 3. pp. 377-382.
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abstract = "Mucin glycoproteins, a secretory product of the gallbladder, are thought to contribute to the matrix or nucleus of gallstones. Human black pigment stones originate in the gallbladder and have as their major constituent calcium bilirubinate, as well as inorganic salts and small amounts of cholesterol. The object of this study was to estimate the amount of glycoprotein in black pigment stones and to isolate gallbladder mucin from dissolved stones. Black pigment stones containing 18 to 65{\%} calcium bilirubinate were first dissolved in 12.5 mM EDTA/0.1 N NaOH and decolorized, then subjected to glycoprotein assay. The mean glycoprotein content of eight stones was 12.4{\%}. In separate experiments, pigment stones were partially dissolved by brief exposure to EDTA/NaOH to minimize glycoprotein breakdown, and the glycoproteins isolated by gel filtration and ultracentrifugation. Pigment stones contained two glycoprotein fractions on Sepharose 4B; a high molecular weight mucin glycoprotein in the void volume and a lower molecular fraction in the included volume. Mucin was further purified by density gradient ultracentrifugation in cesium chloride. Three separate mucin fractions had an average buoyant density of 1.48 gm per ml which is typical for these glycoproteins. Bile pigment was associated with high molecular weight mucin even after extensive dialysis, gel filtration, and density gradient ultracentrifugation. The identify of mucin was further established by β-elimination of glycoproteins in alkaline borohydride which yielded galactosaminitol from cleavage of O-glycosidic bonds. Our results indicate that mucin glycoproteins are present in significant concentrations in human black pigment stones and can be purified from stones solubilized in EDTA/NaOH. The association of bile pigment with gallbladder mucin, even after extensive purification, is consistent with the hypothesis that mucin contributes to the matrix of pigment gallstones.",
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