17 -Hydroxysteroid Dehydrogenase Type 1, 2, 3, and 4 Expression and Enzyme Activity in Human Anterior Pituitary Adenomas

1999 ◽  
Vol 84 (4) ◽  
pp. 1340-1345 ◽  
Author(s):  
V. L. Green
Keyword(s):  
Enzyme Activity ◽  
Pituitary Adenomas ◽  
Anterior Pituitary ◽  
Hydroxysteroid Dehydrogenase ◽  
Human Anterior Pituitary

scholarly journals 17β-Hydroxysteroid Dehydrogenase Type 1, 2, 3, and 4 Expression and Enzyme Activity in Human Anterior Pituitary Adenomas

1999 ◽  
Vol 84 (4) ◽  
pp. 1340-1345
Author(s):  
V. L. Green ◽  
V. Speirs ◽  
A. M. Landolt ◽  
P. M. Foy ◽  
S. L. Atkin
Keyword(s):  
Gene Expression ◽  
Enzyme Activity ◽  
Pituitary Adenomas ◽  
Anterior Pituitary ◽  
Estrogenic Activity ◽  
Hydroxysteroid Dehydrogenase ◽  
Messenger Ribonucleic Acid ◽  
Human Anterior Pituitary

17β-Hydroxysteroid dehydrogenase (17βHSD) isoforms reversibly catalyze the final step in the formation of estradiol (E2) from estrone (E1) and the formation of testosterone from androstenedione. We have investigated 17βHSD type 1, 2, 3, and 4 gene expression and 17βHSD estrogenic activity in human anterior pituitary adenomas. 17βHSD messenger ribonucleic acid (mRNA) expression was studied by RT-PCR in 42 pituitary tumors and 3 normal pituitaries, 17βHSD activity was studied in 11 tumors and 17βHSD type 1 was immunolocalized in vitro in 6 tumors. 17βHSD type 1 gene expression was detected in 34 of 42 adenomas in all tumor subtypes; 17βHSD type 2 mRNA was detected in 18 of 42 adenomas, but not in prolactinomas; 17βHSD type 3 mRNA was detected in 12 of 42 adenomas, but not in corticotropinomas; 17βHSD type 4 was expressed in 20 of 42 adenomas by all adenoma subtypes. Reversible 17βHSD activity was found in 9 of 11 adenomas, and 17βHSD type 1 immunopositivity was cytoplasmically distributed in all 6 adenomas in vitro. All 4 17βHSD isoforms are variably expressed in human anterior pituitary adenomas, which also show 17βHSD enzyme activity, suggesting that 17βHSD may play an important role in regulating the local cellular levels of estradiol.

Dispersed Human Anterior Pituitary Adenomas Preferentially Attach to Poly-L-Lysine Coated Wells

1991 ◽  
Vol 81 (s25) ◽  
pp. 29P-30P
Author(s):  
SL Atkin ◽  
AM Landolt ◽  
RV Jeffreys ◽  
White MC
Keyword(s):  
Pituitary Adenomas ◽  
Anterior Pituitary ◽  
Human Anterior Pituitary

An in vitro microdialysis methodology to study 11β-hydroxysteroid dehydrogenase type 1 enzyme activity in liver microsomes

2007 ◽  
Vol 370 (1) ◽  
pp. 26-37 ◽  
Author(s):  
Li Sun ◽  
Julie A. Stenken ◽  
Amy Y. Yang ◽  
Jamie J. Zhao ◽  
Donald G. Musson
Keyword(s):  
Enzyme Activity ◽  
Liver Microsomes ◽  
Hydroxysteroid Dehydrogenase

Interactions between normal and tumoral tissues at the boundary of human anterior pituitary adenomas

1994 ◽  
Vol 424 (1) ◽  
Author(s):  
M.R. Farnoud ◽  
F. Peillon ◽  
J.Y. Li ◽  
M. Kujas ◽  
J. Racadot ◽  
...  
Keyword(s):  
Pituitary Adenomas ◽  
Anterior Pituitary ◽  
Human Anterior Pituitary

scholarly journals Importance of the 11β-hydroxysteroid dehydrogenase enzyme in clinical disorders

2013 ◽  
Vol 154 (8) ◽  
pp. 283-293 ◽  
Author(s):  
Karolina Feldman ◽  
István Likó ◽  
Zsolt Nagy ◽  
Ágnes Szappanos ◽  
Vince Kornél Grolmusz ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Hydroxysteroid Dehydrogenase ◽  
Chromosome 1 ◽  
Gene Encoding ◽  
Local Synthesis ◽  
Dehydrogenase Enzyme ◽  
Clinical Disorders ◽  
Polymorphic Variants

Glucocorticoids play an important role in the regulation of carbohydrate and amino acid metabolism, they modulate the function of the immune system, and contribute to stress response. Increased and decreased production of glucocorticoids causes specific diseases. In addition to systemic hypo- or hypercortisolism, alteration of local synthesis and metabolism of cortisol may result in tissue-specific hypo- or hypercortisolism. One of the key enzymes participating in the local synthesis and metabolism of cortisol is the 11β-hydroxysteroid dehydrogenase enzyme. Two isoforms, type 1 and type 2 enzymes are located in the endoplasmic reticulum and catalyze the interconversion of hormonally active cortisol and inactive cortisone. The type 1 enzyme mainly works as an activator, and it is responsible for the generation of cortisol from cortisone in liver, adipose tissue, brain and bone. The gene encoding this enzyme is located on chromosome 1. The authors review the physiological and pathophysiological processes related to the function of the type 1 11β-hydroxysteroid dehydrogenase enzyme. They summarize the potential significance of polymorphic variants of the enzyme in clinical diseases as well as knowledge related to inhibitors of enzyme activity. Although further studies are still needed, inhibition of the enzyme activity may prove to be an effective tool for the treatment of several diseases such as obesity, osteoporosis and type 2 diabetes. Orv. Hetil., 2013, 154, 283–293.

Expression of the transferrin receptor in human anterior pituitary adenomas is confined to gonadotrophinomas

1996 ◽  
Vol 44 (4) ◽  
pp. 467-471 ◽  
Author(s):  
S. L. Atkin ◽  
H. E. Burnett ◽  
V. L. Green ◽  
M. C. White ◽  
M. Lombard
Keyword(s):  
Transferrin Receptor ◽  
Pituitary Adenomas ◽  
Anterior Pituitary ◽  
Human Anterior Pituitary

mRNA and enzyme activity of hepatic 11β-hydroxysteroid dehydrogenase type 1 are elevated in C57BL/KsJ-db/db mice

Life Sciences ◽  
2001 ◽  
Vol 69 (21) ◽  
pp. 2543-2549 ◽  
Author(s):  
Kazutaka Aoki ◽  
Masato Homma ◽  
Toshihiko Hirano ◽  
Kitaro Oka ◽  
Shinobu Satoh ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Hydroxysteroid Dehydrogenase

Cytokine expression in human anterior pituitary adenomas

1996 ◽  
Vol 45 (2) ◽  
pp. 179-185 ◽  
Author(s):  
V. L. Green ◽  
S. L. Atkin ◽  
V. Speirs ◽  
R. V. Jeffreys ◽  
A. M. Landolt ◽  
...  
Keyword(s):  
Pituitary Adenomas ◽  
Anterior Pituitary ◽  
Cytokine Expression ◽  
Human Anterior Pituitary

scholarly journals Expression of 5'-deiodinase enzymes in normal pituitaries and in various human pituitary adenomas

2002 ◽  
pp. 263-268 ◽  
Author(s):  
A Baur ◽  
M Buchfelder ◽  
J Kohrle
Keyword(s):  
Thyroid Hormone ◽  
Pituitary Adenomas ◽  
Anterior Pituitary ◽  
Potent Inhibitor ◽  
Feedback Regulation ◽  
Cellular Distribution ◽  
Limited Information ◽  
Human Pituitary ◽  
Normal Tissues ◽  
Human Anterior Pituitary

OBJECTIVE: Local 5'-deiodination of l-thyroxine (T(4)) to active thyroid hormone 3,3',5-tri-iodothyronine (T(3)) catalyzed by the two 5'-deiodinase enzymes (D1 and D2) regulates various T(3)-dependent functions in the anterior pituitary and has been well studied in rodents. Only limited information about deiodinase expression and its cellular distribution in human anterior pituitaries is available. DESIGN: We examined 5'-deiodinase enzyme activities in pituitary adenomas (18 non-functioning, seven TSH-producing, one GH- and TSH-producing, five GH-producing, eight prolactin (PRL)-producing, two adenomas each from patients with Cushing's disease and Nelson's syndrome) and three normal anterior pituitaries. METHODS: Activities were measured as release of (125)I(-) from tyrosyl-ring labeled reverse T(3) with or without propylthiouracil, a potent inhibitor of D1 which does not influence D2 activities. RESULTS: Most of the adenomas and normal tissues expressed both isoenzymes, with D2 activity higher than D1. In a few tissues D1 activity was higher than D2 and some tissues did not express D1 activity at all. Highest activities of both enzymes were found in TSH- and PRL-producing adenomas but absolute activities and the D1/D2 ratio were variable in the same kind of tumor in different patients. CONCLUSION: The finding that all examined tissues expressed 5'-deiodinase activity, most of them expressing both isoenzymes, implies that both enzymes are still active in tumors and that local deiodination is important for the function and feedback regulation of human anterior pituitary.

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