title: Terminal glycosylation and disease: influence on cancer and cystic fibrosis.
abstract: Terminal glycosylation has been a recurring theme of the laboratory. In cystic fibrosis (CF), decreased sialic acid and increased fucosyl residues in alpha1,3 position to antennary N-acetyl glucosamine is the CF glycosylation phenotype. The glycosylation phenotype is reversed by transfection of CF airway cells with wtCFTR. In neuronal cells, polymers of alpha2,8sialyl residues are prominent in oligodendrocytes and human neuroblastoma. These findings are discussed in relationship to early studies in our laboratories and those of other investigators. The potential extension of these concepts to future clinical therapeutics is presented.
authors: Department of Pediatrics and The Cystic Fibrosis Center, University of Pennsylvania School of Medicine, and The Children's Hospital of Philadelphia, 19104-4318, USA.
authors: T F
authors: TF
authors: Scanlin
authors: M C
authors: MC
authors: Glick
mesh_terms: D000818:Animals; D002240:Carbohydrate Sequence; D003550:Cystic Fibrosis / Q000235:genetics / Q000266:history / Q000378:metabolism*; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000235:genetics / Q000266:history / Q000378:metabolism; D015316:Genetic Therapy; D006031:Glycosylation; D049673:History, 20th Century; D006801:Humans; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D019158:N-Acetylneuraminic Acid / Q000737:chemistry / Q000266:history / Q000378:metabolism; D009369:Neoplasms / Q000266:history / Q000378:metabolism*
chemical_list: C505032:CFTR protein, human; D008562:Membrane Glycoproteins; D019005:Cystic Fibrosis Transmembrane Conductance Regulator; D019158:N-Acetylneuraminic Acid