Occurrence of Poly(α 2,8-Deaminoneuraminic Acid) in Mammalian Tissues: Widespread and Developmentally Regulated but Highly Selective Expression on Glycoproteins

• Published in: Proceedings of the National Academy of Sciences - PNAS 1996-04, Vol.93 (7), p.2759-2763
• Main Authors: Ziak, Martin, Qu, Baoxi, Zuo, Xulei, Zuber, Christian, Kanamori, Akiko, Kitajima, Ken, Inoue, Sadako, Inuoe, Yasuo, Roth, Jürgen
• Format: Article
• Language: English
• Subjects: Amino acids; Animals; Antibodies, Monoclonal; Brain - metabolism; Cells; Cellular biology; Chickens; Chromatography, Gas; Cricetinae; Electrophoresis, Polyacrylamide Gel; Gene Expression Regulation; Glycoproteins; Glycoproteins - biosynthesis; Glycoproteins - chemistry; Glycoside Hydrolases; Immunoblotting; Immunohistochemistry; Kidneys; Lung - metabolism; Male; Mammals; Mesocricetus; Monoclonal antibodies; Muscle, Skeletal - metabolism; Muscles; Neural cell adhesion molecules; Organ Specificity; Physiological regulation; Polymers; Polysaccharides; Polysaccharides - analysis; Polysaccharides - biosynthesis; Protein Processing, Post-Translational; Proteins; Rats; Swine; Testis - metabolism; Thymus Gland - metabolism
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.93.7.2759

In tissues of higher organisms homopolymers of α 2,8-linked N-acetylneuraminic acid can be found as a posttranslational modification on selected proteins. We report here the discovery of homopolymers of α 2,8-linked deaminoneuraminic acid [poly(α 2,8-KDN)] in various tissues derived from all three germ layers in vertebrates including mammals. The monoclonal antibody kdn8kdn in conjunction with a bacterial KDNase permitted the detection of poly (α 2,8-KDN) KDN) by immunohistochemistry and immunoblotting. Further evidence for the existence of poly (α 2,8-KDN) was obtained by gas/liquid chromatography. The poly (α 2,8-KDN) glycan was detectable in all tissues studied with the exception of mucus-producing cells present in various organs, the extracellular matrix, and basement membranes. However, in certain organs such as muscle, kidney, lung, and brain its expression was developmentally regulated. Despite its widespread tissue distribution, the poly (α 2,8-KDN) glycan was detected on a single 150-kDa glycoprotein except for a single >350-kDa glycoprotein in kidney, which makes it most distinctive among polysialic acids. The ubiquitous yet selective expression may be indicative of a general function of the poly (α 2,8-KDN)-bearing glycoproteins.