TY - JOUR
T1 - Interaction of human gallbladder mucin with calcium hydroxyapatite
T2 - Binding studies and the effect on hydroxyapatite formation
AU - Qiu, Sui Min
AU - Wen, Gary
AU - Wen, Julie
AU - Soloway, Roger D.
AU - Crowther, Roger S.
N1 - Funding Information:
Abbreviation: HAP, hydroxyapatite. From the 1Division of Gastroenterology, Department of Internal Medicine, and the 2Department of Pathology, University of Texas Medical Branch, Galveston, TX. Received July 12, 1994; accepted December 29, 1994. Supported by grant AM-16549 from the National Institutes of Health and by grants from the Scaly and Smith and M. D. Anderson Foundations. Address reprint requests to: Roger S. Crowther, PhD, Division of Gastroenterology, 301 University Blvd, University of Texas Medical Branch, Galveston, TX 77555-0764. Copyright © 1995 by the American Association for the Study of Liver Diseases. 0270-9139/95/2106-002053.00/0
PY - 1995/6
Y1 - 1995/6
N2 - Calcium hydroxyapatite (HAP) crystals formed in vitro in the presence of polymeric human gallbladder mucin (1.0 mg/mL) were smaller (0.75 ± 0.39 μm) than control crystals (7.86 ± 2.76 μm), but the mucin did not affect the kinetics of crystal formation or alter the amount of mineral phase present at equilibrium. In contrast, glycopeptide subunits produced by proteolysis of the native mucin had no effect on HAP crystal size. Both native mucin and glycopeptides bound to mature HAP crystals, but the glycopeptides were much more readily displaced by phosphate ions. Therefore, in experiments where HAP was being formed, the phosphate ions inhibited the interaction of glycopeptides with the nascent HAP. These results indicate that gallbladder mucin may modulate HAP formation in vivo, and that this ability may be altered during pathological states, such as neutrophil infiltration or bacterial colonization, that may cause the release of proteinases capable of digesting mucin.
AB - Calcium hydroxyapatite (HAP) crystals formed in vitro in the presence of polymeric human gallbladder mucin (1.0 mg/mL) were smaller (0.75 ± 0.39 μm) than control crystals (7.86 ± 2.76 μm), but the mucin did not affect the kinetics of crystal formation or alter the amount of mineral phase present at equilibrium. In contrast, glycopeptide subunits produced by proteolysis of the native mucin had no effect on HAP crystal size. Both native mucin and glycopeptides bound to mature HAP crystals, but the glycopeptides were much more readily displaced by phosphate ions. Therefore, in experiments where HAP was being formed, the phosphate ions inhibited the interaction of glycopeptides with the nascent HAP. These results indicate that gallbladder mucin may modulate HAP formation in vivo, and that this ability may be altered during pathological states, such as neutrophil infiltration or bacterial colonization, that may cause the release of proteinases capable of digesting mucin.
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U2 - 10.1016/0270-9139(95)90467-0
DO - 10.1016/0270-9139(95)90467-0
M3 - Article
C2 - 7768507
AN - SCOPUS:0029013645
SN - 0270-9139
VL - 21
SP - 1618
EP - 1624
JO - Hepatology
JF - Hepatology
IS - 6
ER -