Lg. Baum et al., CHARACTERIZATION OF TERMINAL SIALIC-ACID LINKAGES ON HUMAN THYMOCYTES- CORRELATION BETWEEN LECTIN-BINDING PHENOTYPE AND SIALYLTRANSFERASE EXPRESSION, The Journal of biological chemistry, 271(18), 1996, pp. 10793-10799
T cell surface sialylation changes during maturation in the thymus, We
have previously demonstrated increased expression of mRNA encoding th
e Gal beta 1, 3GalNAc alpha 2,3-sialyltransferase in mature medullary
human thymocytes, compared with immature cortical thymocytes, For this
enzyme, increased expression of transferase mRNA correlated with incr
eased sialylation of O-glycans, We have now examined the pattern of ex
pression in the human thymus of two additional sialyltransferases, the
Gal beta 1,4GlcNAc alpha 2,6-sialyltransferase (ST6N) and the Gal bet
a 1,3/4GlcNAc alpha 2,3-sialyltransferase (ST3N), The patterns of mRNA
expression were compared with the pattern of binding of two sialic ac
id-specific plant lectins, Sambucus nigra agglutinin and Maackia amure
nsis agglutinin, which preferentially recognize alpha 2,6- and alpha 2
,3-linked sialic acids, respectively, on N-glycans, By in situ hybridi
zation, mRNA encoding ST3N was detected uniformly throughout the thymu
s, All thymocytes bound M, amurensis agglutinin, demonstrating a direc
t correlation between the level of ST3N mRNA expression and cell-surfa
ce glycosylation, In contrast, mRNA encoding ST6N was also expressed u
niformly throughout the thymus; however, only mature (CD3(hi)) medulla
ry thymocytes bound S. nigra agglutinin, On mature thymocytes, S. nigr
a agglutinin appeared to bind primarily to the cell-surface glycoprote
in CD45; since only the mature thymocytes expressed the CD45RA isoform
, while both mature and immature populations expressed the CD45R0 isof
orm, CD45RA may be a preferred substrate for ST6N, These results demon
strate that glycoprotein sialylation is tightly regulated during T cel
l development and that the developmentally regulated expression of spe
cific oligosaccharide structures on the cell surface may be influenced
by expression of both the relevant glycosyltransferase and specific a
cceptor substrate.