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TSH-induced galactose incorporation at the NH2terminus of thyroglobulin secreted by FRTL-5 cells

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
189
Issue
3
Identifiers
DOI: 10.1016/0006-291x(92)90263-k

Abstract

Abstract FRTL-5 cells were cultured in media containing standard growth factors with or without TSH, plus labeled precursors of N-linked oligosaccharide chains. The thyroglobulin secreted in the medium was purified and fragmented with CNBr. Three peptides were identified by NH 2-terminal sequencing, that were labeled mainly with D-[2- 3H]mannose, independent of TSH. One of them, corresponding to the NH 2-terminus of thyroglobulin, incorporated both more D-[2- 3H]mannose and more D-[1- 3H] galactose upon TSH addition. These data likely reflect a TSH-induced increment of N-linked glycosylation at the NH 2-terminus of thyroglobulin, mostly with the maturation of high-mannose to complex chains.

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