OCCURRENCE OF POLY(ALPHA-2,8-DEAMINONEURAMINIC ACID) IN MAMMALIAN-TISSUES - WIDESPREAD AND DEVELOPMENTALLY-REGULATED BUT HIGHLY SELECTIVE EXPRESSION ON GLYCOPROTEINS
M. Ziak et al., OCCURRENCE OF POLY(ALPHA-2,8-DEAMINONEURAMINIC ACID) IN MAMMALIAN-TISSUES - WIDESPREAD AND DEVELOPMENTALLY-REGULATED BUT HIGHLY SELECTIVE EXPRESSION ON GLYCOPROTEINS, Proceedings of the National Academy of Sciences of the United Statesof America, 93(7), 1996, pp. 2759-2763
In tissues of higher organisms homopolymers of alpha 2,8-linked N-acet
ylneuraminic acid can be found as a posttranslational modification on
selected proteins, We report here the discovery of homopolymers of alp
ha 2,8-linked deaminoneuraminic acid [poly(alpha 2,8-KDN)] in various
tissues derived from all three germ layers in vertebrates including ma
mmals, The monoclonal antibody kdn8kdn in conjunction with a bacterial
KDNase permitted the detection of poly(alpha 2,8-KDN) by immunohistoc
hemistry and immunoblotting. Further evidence for the existence of pol
y(alpha 2,8-KDN) was obtained by gas/liquid chromatography. The poly(a
lpha 2,8-KDN) glycan was detectable in all tissues studied with the ex
ception of mucus-producing cells present in various organs, the extrac
ellular matrix, and basement membranes, However, in certain organs suc
h as muscle, kidney, lung, and brain its expression was developmentall
y regulated, Despite its widespread tissue distribution, the poly(alph
a 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 dis
tinctive among polysialic acids, The ubiquitous yet selective expressi
on may be indicative of a general function of the poly(alpha 2,8-KDN)-
bearing glycoproteins.