Subscribe to RSS
DOI: 10.1055/s-0030-1265220
© Georg Thieme Verlag KG Stuttgart · New York
Glycerol-3-phosphate Dehydrogenase Expression and Oxygen Consumption in Liver Mitochondria of Female and Male Rats with Chronic Alteration of Thyroid Status
Publication History
received 01.07.2010
accepted 23.08.2010
Publication Date:
30 September 2010 (online)

Abstract
In our chronic experiments (over several months), the activity and protein amount of glycerol-3-phosphate dehydrogenase (GPDH) in mitochondria isolated from the liver of adult male and female inbred Lewis strain euthyroid (EU), hyperthyroid (TH), and hypothyroid (HY) rats were analyzed by biochemical and Western blot methods. The TH status was induced by intraperitoneal injections of 3,3′,5-triiodo-L-thyronine and the HY status with 0.05% solution of methimazole in drinking water. The TH status led to a significant increase and the HY status to a significant decrease of enzyme activity and protein amount in both male and female animals. These changes were, however, more pronounced in females. The EU and TH female rats also showed a significantly higher activity and the TH female rats showed also a significantly higher enzyme amount in comparison with males, while the HY rats showed low levels in both sexes. The glycerol-3-phosphate-dependent oxygen consumption of freshly isolated rat liver mitochondria from the TH animals was higher in comparison with the EU animals and it was activated by idebenone, a synthetic analogue of coenzyme Q, in both the EU and TH rats. Measurements of serum thyroid hormone levels and analysis of anatomical parameters (relative heart and thyroid gland weights) confirmed that our procedures inducing the TH and HY states are efficient and reliable and that determination of GPDH can serve as an additional criterion for the evaluation of the thyroid hormone status.
Key words
chronic administration - triiodothyronine - methimazole - sex difference - idebenone
References
- 1
Hulbert AJ.
Thyroid hormones and their effects: a new perspective.
Biol Rev.
2000;
75
519-631
MissingFormLabel
- 2
Harper ME, Seifert EL.
Thyroid hormones effects on mitochondrial energetics.
Thyroid.
2008;
18
145-156
MissingFormLabel
- 3
Lee YP, Takemori AE, Lardy H.
Enhanced oxidation of α-glycerophosphate by mitochondria of thyroid-fed rats.
J Biol Chem.
1959;
234
3051-3054
MissingFormLabel
- 4
Lardy HA, Lee YP, Takemori A.
Enzyme responses to thyroid hormones.
Ann NY Acad Sci.
1960;
86
506-511
MissingFormLabel
- 5
Lee YP, Lardy HA.
Influence of thyroid hormones on l-α-glycerophosphate dehydrogenases and other dehydrogenases
in various organs of the rat.
J Biol Chem.
1965;
240
1427-1436
MissingFormLabel
- 6
Sellinger OZ, Lee KL, Fesler KW.
The induction of mitochondrial α-glycerophosphate dehydrogenase by thyroid hormone:
Effects of adrenalectomy, thyroidectomy and cortisone administration.
Biochim Biophys Acta.
1966;
124
289-294
MissingFormLabel
- 7
Costante G, Crupi D, Catalfamo R, Trimarchi F.
Stimulation of liver mitochondrial α-glycerophosphate dehydrogenase activity by l-thyroxine
in thyroidectomized rats: comparison with the suppression of pituitary TSH secretion.
J Endocrinol Invest.
1990;
13
61-64
MissingFormLabel
- 8
Oliveira E, Fagundes ATS, Alves SB, Pazos-Moura CC, Moura EG, Passos MCF, Lisboa CP.
Chronic leptin treatment inhibits liver mitochondrial α-glycerol-β-phosphate dehydrogenase
in euthyroid rats.
Horm Metab Res.
2007;
39
867-870
MissingFormLabel
- 9
Moura EG, Santos RS, Lisboa CP, Alves SB, Bonomo IT, Fagundes AT, Oliveira E, Passos MC.
Thyroid function and body weight programming by neonatal hyperthyroidism in rats –
the role of leptin and deiodase activities.
Horm Metab Res.
2008;
40
1-7
MissingFormLabel
- 10
Oppenheimer JH, Silva E, Schwartz HL, Surks ML.
Stimulation of hepatic mitochondrial α-glycerophosphate dehydrogenase and malic enzyme
by l-triiodothyronine. Characteristics of the response with specific nuclear thyroid
hormone binding sites fully saturated.
J Clin Invest.
1977;
59
517-527
MissingFormLabel
- 11
Jolin T.
Response of hepatic mitochondrial α-glycerophosphate dehydrogenase and malic enzyme
to 3,5,3′-triiodothyronine in streptozotocin-diabetic rats.
Endocrinology.
1988;
123
248-257
MissingFormLabel
- 12
Mráček T, Ješina P, Křiváková P, Bolehovská R, červinková Z, Drahota Z, Houštěk J.
Time-course of hormone induction of mitochondrial glycerophosphate dehydrogenase biogenesis
in rat liver.
Biochim Biophys Acta.
2005;
1726
217-223
MissingFormLabel
- 13
Rauchová H, Zachařová G, Soukup T.
Influence of chronically altered thyroid status on the activity of liver mitochondrial
glycerol-3-phosphate dehydrogenase in female inbred Lewis rats.
Horm Metab Res.
2004;
36
286-290
MissingFormLabel
- 14
Ruegamer WR, Westerfeld WW, Richert DA.
α-Glycerophosphate dehydrogenase response to thyroxine in thyroidectomized, thiouracil-fed
and temperature-adapted rats.
Endocrinology.
1964;
75
908-916
MissingFormLabel
- 15
Okamura K, Taurog A, Krulich L.
Hypothyroidism in severely iodine deficient rats.
Endocrinology.
1981;
109
464-468
MissingFormLabel
- 16
Dümmler K, Müller S, Seitz HJ.
Regulation of adenine nucleotide translocase and glycerol-3-phosphate dehydrogenase
expression by thyroid hormones in different rat tissues.
Biochem J.
1996;
317
913-918
MissingFormLabel
- 17
Soukup T, Jirmanová I.
Regulation of myosin expression in developing and regenerating extrafusal and intrafusal
muscle fibres with special emphasis on the role of thyroid hormones.
Physiol Res.
2000;
49
617-633
MissingFormLabel
- 18 Johnson D, Lardy H. Isolation of liver and kidney mitochondria. In: Estabrook RW, Pullman ME, (eds) Methods in Enzymology 10, Oxidation and Phosphorylation. New York, London: Academic Press; 1967: 94-96
MissingFormLabel
- 19
Lowry OH, Rosebrough JN, Farr AL, Randall RJ.
Protein measurement with the Folin-phenol reagent.
J Biol Chem.
1951;
193
265-275
MissingFormLabel
- 20
Schagger H, von Jagow G.
Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation
of proteins in the range from 1 to 100 kDa.
Anal Biochem.
1987;
166
368-379
MissingFormLabel
- 21
Ueda K, Tanizawa Y, Ishihara H, Kizuki N, Ohta Y, Matsutani A, Oka Y.
Overexpression of mitochondrial FAD-linked glycerol-3-phosphate dehydrogenase does
not correct glucose-stimulated insulin secretion from diabetic GK rat pancreatic islets.
Diabetologia.
1998;
41
649-653
MissingFormLabel
- 22
Coleoni AH, Cherubini O.
Sex-related differences in the activity of liver mitochondrial α-glycerophosphate
dehydrogenase in the rat.
Acta Physiol Pharmacol Latinoam.
1989;
39
245-253
MissingFormLabel
- 23
Alfadda A, DosSantos RA, Stepanyan Z, Marrif H, Silva JE.
Mice with deletion of the mitochondrial glycerol-3-phosphate dehydrogenase gene exhibit
a thrifty phenotype: effect of gender.
Am J Physiol Regul Integr Comp Physiol.
2004;
287
R147-R156
MissingFormLabel
- 24
Límanová Z.
The thyroid gland-running the show behind the scenes (In Czech).
Cas Lek Ces.
2009;
148
83-85
MissingFormLabel
- 25
Sellinger OZ, Lee KL.
The induction of mitochondrial α-glycerophosphate dehydrogenase by thyroid hormone:
Evidence for enzyme synthesis.
Biochim Biophys Acta.
1964;
91
183-186
MissingFormLabel
- 26
Müller S, Seitz HJ.
Cloning of cDNA for the FAD-linked glycerol-3-phosphate dehydrogenase from rat liver
and its regulation by thyroid hormones.
Proc Natl Acad Sci USA.
1994;
91
10581-10585
MissingFormLabel
- 27
Rauchová H, Drahota Z, Bergamini C, Fato R, Lenaz G.
Modification of respiratory-chain activities in brown adipose tissue mitochondria
by idebenone (hydroxydecyl-ubiquinone).
J Bioenerg Biomembr.
2008;
40
85-83
MissingFormLabel
- 28
Soukup T, Zachařová G, Smerdu V, Jirmanová I.
Body, heart, thyroid gland and skeletal muscle weight changes in rats with altered
thyroid status.
Physiol Res.
2001;
50
619-626
MissingFormLabel
Correspondence
H. Rauchová
Institute of Physiology, v.v.i.
Academy of Sciences of the
Czech Republic
Vídeňská 1083
42220 Prague 4
Czech Republic
Phone: +420/2/4106 2432
Fax: +420/2/4106 2488
Email: rauchova@biomed.cas.cz