Changes in the sialylation and sulfation of secreted thyrotropin in congenital hypothyroidism

Journal Article · Tue May 01 00:00:00 EDT 1990 · Proceedings of the National Academy of Sciences of the United States of America; (United States)

DOI:https://doi.org/10.1073/pnas.87.10.3792· OSTI ID:5463669

Gyves, P W; Gesundheit, N; Thotakura, N R; Stannard, B S; DeCherney, G S; Weintraub, B D ^[1]

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1. National Institutes of Health, Bethesda, MD (USA)

The authors have examined the oligosaccharide structure of secreted thyrotropin (TSH) in perinatal and mature rats with congenital primary hypothyroidism. Rat pituitaries from euthyroid control animals and those rendered hypothyroid by methimazole treatment were incubated with ({sup 3}H)glucosamine in vitro. Secreted TSH was purified, and oligosaccharides were enzymatically released and characterized by anion-exchange HPLC. In perinatal hypothyroid animals compared with control animals, oligosaccharides from TSH {alpha} and {beta} subunits contained more species with three or more negative charges. Moreover, perinatal hypothyroid animals demonstrated a dramatic increase in the ratio of sialylated to sulfated species within oligosaccharides of the same negative charge. In mature hypothyroid 9-week-old animals compared with control animals, changes were less pronounced, suggesting that endocrine regulation of oligosaccharide structure is dependent upon the maturational state of the animal. Together, these data provide direct evidence and characterization of specific changes in the structure of a secreted pituitary glycoprotein hormone occurring as a result of in vivo endocrine alterations during early development. Moreover, they provide a potential structural basis to explain the delayed clearance of both TSH and the gonadotropins with end-organ deficiency, which may have important implications for the in vivo biological activities of these hormones.

• OSTI ID: 5463669
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 87:10; ISSN 0027-8424
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
HYPOTHYROIDISM
PATHOGENESIS
OLIGOSACCHARIDES
MOLECULAR STRUCTURE
TRITIUM COMPOUNDS
UPTAKE
TSH
RADIOIMMUNOASSAY
ASPARAGINE
CONGENITAL DISEASES
GLUCOSAMINE
GLYCOPROTEINS
GLYCOSYL HYDROLASES
GONADOTROPINS
ION EXCHANGE CHROMATOGRAPHY
PITUITARY GLAND
AMIDES
AMINES
AMINO ACIDS
BIOASSAY
BODY
CARBOHYDRATES
CARBOXYLIC ACIDS
CHROMATOGRAPHY
DIAGNOSTIC TECHNIQUES
DISEASES
ENDOCRINE DISEASES
ENDOCRINE GLANDS
ENZYMES
GLANDS
HEXOSAMINES
HEXOSES
HORMONES
HYDROGEN COMPOUNDS
HYDROLASES
IMMUNOASSAY
IMMUNOLOGY
ISOTOPE APPLICATIONS
MONOSACCHARIDES
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
ORGANS
PEPTIDE HORMONES
PITUITARY HORMONES
PROTEINS
RADIOASSAY
RADIOIMMUNODETECTION
RADIOIMMUNOLOGY
SACCHARIDES
SEPARATION PROCESSES
TRACER TECHNIQUES
550201* - Biochemistry- Tracer Techniques