SIALYLTRANSFERASE MESSENGER-RIBONUCLEIC-ACID INCREASES IN THYROTROPHS OF HYPOTHYROID MICE - AN IN-SITU HYBRIDIZATION STUDY

被引:34
作者
HELTON, TE [1 ]
MAGNER, JA [1 ]
机构
[1] E CAROLINA UNIV,SCH MED,DEPT MED,ENDOCRINOL SECT,GREENVILLE,NC 27858
关键词
D O I
10.1210/en.134.6.2347
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
Hypothyroid patients and mice have been shown to have circulating TSH that is more highly sialylated than their euthyroid counterparts. To learn about the underlying cellular mechanisms responsible for this increased sialylation of TSH, we used in situ hybridization to examine the beta-galactoside alpha-2,6-sialyltransferase (STase) mRNA content in thyrotrophs and corticotrophs of euthyroid and hypothyroid mice. Mice were treated with or without 0.05% propylthiouracil for 1, 2, 3, 4, or 6 weeks, then pituitaries were removed, and 5-mu m slices were immunocytochemically stained for TSH and ACTH. Adjacent sections were used for in situ hybridization. A 48-mer deoxynucleotide probe to rat STase and two control probes were labeled with S-35, and autoradiography was performed. There was an approximately 140% increase in STase mRNA in hypothyroid thyrotrophs compared to euthyroid thyrotrophs by the first week, with a mean increase of 170% in weeks 1-6, whereas corticotrophs exhibited no change in STase mRNA. The increase in hybridization of the STase probe in hypothyroid thyrotrophs may be due to an increased transcription of the STase gene, stabilization of the STase mRNA, or both. Thus, modulation of the STase mRNA levels occurs in thyrotrophs and represents one important mechanism by which the oligosaccharides of TSH are altered under different physiological conditions.
引用
收藏
页码:2347 / 2353
页数:7
相关论文
共 47 条
[1]   DIRECT INTERACTION OF THE SIALIC-ACID RESIDUE OF HUMAN LUTROPIN AND CHORIONIC-GONADOTROPIN WITH TARGET-CELL IS NECESSARY FOR THE FULL EXPRESSION OF THEIR HORMONAL ACTION [J].
AMANO, J ;
KOBATA, A .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1993, 305 (02) :618-621
[2]   THE CARBOHYDRATE MOIETY OF BOVINE THYROTROPIN IS ESSENTIAL FOR FULL BIOACTIVITY BUT NOT FOR RECEPTOR RECOGNITION [J].
AMIR, SM ;
KUBOTA, K ;
TRAMONTANO, D ;
INGBAR, SH ;
KEUTMANN, HT .
ENDOCRINOLOGY, 1987, 120 (01) :345-352
[3]   ACTIVITIES OF DEGLYCOSYLATED THYROTROPIN AT THE THYROID MEMBRANE RECEPTOR-ADENYLATE CYCLASE SYSTEM [J].
AMR, S ;
MENEZEZFERREIRA, M ;
SHIMOHIGASHI, Y ;
CHEN, HC ;
NISULA, B ;
WEINTRAUB, BD .
JOURNAL OF ENDOCRINOLOGICAL INVESTIGATION, 1985, 8 (06) :537-541
[4]   THE ROLE OF THE CARBOHYDRATE MOIETY IN THYROTROPIN ACTION [J].
BERMAN, MI ;
THOMAS, CG ;
MANJUNATH, P ;
SAIRAM, MR ;
NAYFEH, SN .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1985, 133 (02) :680-687
[5]  
CHIN WW, 1978, J BIOL CHEM, V253, P7985
[6]   DIFFERENCES IN THE METABOLIC-CLEARANCE OF PITUITARY AND SERUM THYROTROPIN (TSH) DERIVED FROM EUTHYROID AND HYPOTHYROID RATS - EFFECTS OF CHEMICAL DEGLYCOSYLATION OF PITUITARY TSH [J].
CONSTANT, RB ;
WEINTRAUB, BD .
ENDOCRINOLOGY, 1986, 119 (06) :2720-2727
[7]   ALTERATIONS IN THE SIALYLATION AND SULFATION OF SECRETED MOUSE THYROTROPIN IN PRIMARY HYPOTHYROIDISM [J].
DECHERNEY, GS ;
GESUNDHEIT, N ;
GYVES, PW ;
SHOWALTER, CR ;
WEINTRAUB, BD .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1989, 159 (02) :755-762
[8]   ESTROGEN MODULATES EXPRESSION OF THE GLYCOSYLTRANSFERASES THAT SYNTHESIZE SULFATED OLIGOSACCHARIDES ON LUTROPIN [J].
DHARMESH, SM ;
BAENZIGER, JU .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (23) :11127-11131
[9]   CLEARING UP GLYCOPROTEIN HORMONES [J].
DRICKAMER, K .
CELL, 1991, 67 (06) :1029-1032
[10]   THE DISTINCT ROLES OF ALPHA-SUBUNITS AND BETA-SUBUNITS OF HUMAN THYROTROPIN IN THE RECEPTOR-BINDING AND POSTRECEPTOR EVENTS [J].
ENDO, Y ;
TETSUMOTO, T ;
NAGASAKI, H ;
KASHIWAI, T ;
TAMAKI, H ;
AMINO, N ;
MIYAI, K .
ENDOCRINOLOGY, 1990, 127 (01) :149-154