18 research outputs found
Eletroacupuntura aplicada nas fases precoce e tardia da cicatrização do tendĂŁo calcanear comum de coelhos apĂłs reparo tardio com peritĂ´nio bovino conservado em solução supersaturada de sal: aspectos clĂnicos
Characterization and Heterogeneity of Monoclonal Antibodies Directed to Intestinal Mucin Derived from Crohn's Disease Small Bowel
Retinoic acid-regulated cellular differentiation and mucin gene expression in isolated rabbit tracheal epithelial cells in culture
Functional protective role for mucin glycosylated repetitive domains
Mucins carry out a number of protective roles, some of which are more easily studied than others. One mucin function is believed to be the protection of the mucosal epithelium against acidic and proteolytic damage in the stomach and intestines. In the present work, a portion of stomach mucin tandem repeat sequence (Muc6) was joined to the catalytic domain of a reporter enzyme [human milk cholesterol esterase (CE)] to determine whether the former can protect the latter protein from damage. This Muc6 domain replaced a unique series of glycosylated C-terminal repeats normally present in CE. The chimeric protein (CE/Muc6) was expressed in two different cell lines and its properties compared to recombinant full-length CE and a truncated version of CE which contained only the catalytic domain (CE/trunc). Results showed that both CE and CE/Muc6 were resistant to denaturation by acid and to proteolysis by pepsin at low pH values or by pancreatic proteases compared to CE/trunc. Thus, a stomach Muc6 domain is sufficient to confer stability on the CE catalytic domain, demonstrating a protective effect by a glycosylated mucin sequence