Light and electron microscopy localization of the 11β-hydroxysteroid dehydrogenase type I enzyme in the rat

P. S. Brereton, R. R. Van Driel, Farihah Suhaimi, K. Koyama, R. Dilley, Z. Krozowski

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

The 11β-hydroxysteroid dehydrogenase type I enzyme (11βHSD1) converts cortisone to cortisol in humans, and 11-dehydrocorticosterone to corticosterone in rodents. In the present study we used a new immunopurified polyclonal antibody, RAH113, to localize 11βHSD1 at the light and electron microscopy levels in a wide range of rat tissues, 11βHSD1 staining in the liver was of highest intensity around the central vein and decreased radially. In the lung, 11βHSD1 was found at highest levels in the interstitial fibroblast, with levels in the type II pneumocyte an order of magnitude lower. RAH113 stained proximal tubules of the renal cortex and interstitial cells of the medulla and papilla. Adrenal 11βHSD1 was confined to the glomerulosa and medulla, whereas the glucocorticoid-inactivating hydroxysteroid dehydrogenase isoform 11βHSD2 was present in fascilulata/reticularis, 11βHSD1 was found in parietal cells of the fundic region of the stomach, but not in the antrum. In the heart, 11βHSD1 was detected in cells resembling interstitial fibroblasts of the endocardium and in the adventitial fibroblasts of blood vessels. Western blot analysis confirmed the presence of an antigen of the correct size (34 kDa) and intensity consistent with levels of enzyme activity previously reported in these tissues. Brain and testis also displayed the 34-kDa protein, confirming the expression of authentic 11βHSD1 in these tissues. Electron microscopy of lung and kidney interstitial cells showed that 11βHSD1 was localized both to the endoplasmic reticulum and the nuclear membrane. These results show that 11βHSD1 is present in discrete cell populations where it may facilitate intracrine and paracrine glucocorticoid action in addition to its classical role of maintaining circulating glucocorticoids via activity in the liver.

Original languageEnglish
Pages (from-to)1644-1651
Number of pages8
JournalEndocrinology
Volume142
Issue number4
DOIs
Publication statusPublished - 2001
Externally publishedYes

Fingerprint

11-beta-Hydroxysteroid Dehydrogenases
Electron Microscopy
Light
Glucocorticoids
Enzymes
Fibroblasts
Alveolar Epithelial Cells
Endocardium
Adventitia
Lung
Proximal Kidney Tubule
Hydroxysteroid Dehydrogenases
Liver
Cortisone
Nuclear Envelope
Corticosterone
Endoplasmic Reticulum
Blood Vessels
Hydrocortisone
Testis

ASJC Scopus subject areas

  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

Cite this

Light and electron microscopy localization of the 11β-hydroxysteroid dehydrogenase type I enzyme in the rat. / Brereton, P. S.; Van Driel, R. R.; Suhaimi, Farihah; Koyama, K.; Dilley, R.; Krozowski, Z.

In: Endocrinology, Vol. 142, No. 4, 2001, p. 1644-1651.

Research output: Contribution to journalArticle

Brereton, P. S. ; Van Driel, R. R. ; Suhaimi, Farihah ; Koyama, K. ; Dilley, R. ; Krozowski, Z. / Light and electron microscopy localization of the 11β-hydroxysteroid dehydrogenase type I enzyme in the rat. In: Endocrinology. 2001 ; Vol. 142, No. 4. pp. 1644-1651.
@article{4cf38159ef744c5589bf96c7f50ba0de,
title = "Light and electron microscopy localization of the 11β-hydroxysteroid dehydrogenase type I enzyme in the rat",
abstract = "The 11β-hydroxysteroid dehydrogenase type I enzyme (11βHSD1) converts cortisone to cortisol in humans, and 11-dehydrocorticosterone to corticosterone in rodents. In the present study we used a new immunopurified polyclonal antibody, RAH113, to localize 11βHSD1 at the light and electron microscopy levels in a wide range of rat tissues, 11βHSD1 staining in the liver was of highest intensity around the central vein and decreased radially. In the lung, 11βHSD1 was found at highest levels in the interstitial fibroblast, with levels in the type II pneumocyte an order of magnitude lower. RAH113 stained proximal tubules of the renal cortex and interstitial cells of the medulla and papilla. Adrenal 11βHSD1 was confined to the glomerulosa and medulla, whereas the glucocorticoid-inactivating hydroxysteroid dehydrogenase isoform 11βHSD2 was present in fascilulata/reticularis, 11βHSD1 was found in parietal cells of the fundic region of the stomach, but not in the antrum. In the heart, 11βHSD1 was detected in cells resembling interstitial fibroblasts of the endocardium and in the adventitial fibroblasts of blood vessels. Western blot analysis confirmed the presence of an antigen of the correct size (34 kDa) and intensity consistent with levels of enzyme activity previously reported in these tissues. Brain and testis also displayed the 34-kDa protein, confirming the expression of authentic 11βHSD1 in these tissues. Electron microscopy of lung and kidney interstitial cells showed that 11βHSD1 was localized both to the endoplasmic reticulum and the nuclear membrane. These results show that 11βHSD1 is present in discrete cell populations where it may facilitate intracrine and paracrine glucocorticoid action in addition to its classical role of maintaining circulating glucocorticoids via activity in the liver.",
author = "Brereton, {P. S.} and {Van Driel}, {R. R.} and Farihah Suhaimi and K. Koyama and R. Dilley and Z. Krozowski",
year = "2001",
doi = "10.1210/en.142.4.1644",
language = "English",
volume = "142",
pages = "1644--1651",
journal = "Endocrinology",
issn = "0013-7227",
publisher = "The Endocrine Society",
number = "4",

}

TY - JOUR

T1 - Light and electron microscopy localization of the 11β-hydroxysteroid dehydrogenase type I enzyme in the rat

AU - Brereton, P. S.

AU - Van Driel, R. R.

AU - Suhaimi, Farihah

AU - Koyama, K.

AU - Dilley, R.

AU - Krozowski, Z.

PY - 2001

Y1 - 2001

N2 - The 11β-hydroxysteroid dehydrogenase type I enzyme (11βHSD1) converts cortisone to cortisol in humans, and 11-dehydrocorticosterone to corticosterone in rodents. In the present study we used a new immunopurified polyclonal antibody, RAH113, to localize 11βHSD1 at the light and electron microscopy levels in a wide range of rat tissues, 11βHSD1 staining in the liver was of highest intensity around the central vein and decreased radially. In the lung, 11βHSD1 was found at highest levels in the interstitial fibroblast, with levels in the type II pneumocyte an order of magnitude lower. RAH113 stained proximal tubules of the renal cortex and interstitial cells of the medulla and papilla. Adrenal 11βHSD1 was confined to the glomerulosa and medulla, whereas the glucocorticoid-inactivating hydroxysteroid dehydrogenase isoform 11βHSD2 was present in fascilulata/reticularis, 11βHSD1 was found in parietal cells of the fundic region of the stomach, but not in the antrum. In the heart, 11βHSD1 was detected in cells resembling interstitial fibroblasts of the endocardium and in the adventitial fibroblasts of blood vessels. Western blot analysis confirmed the presence of an antigen of the correct size (34 kDa) and intensity consistent with levels of enzyme activity previously reported in these tissues. Brain and testis also displayed the 34-kDa protein, confirming the expression of authentic 11βHSD1 in these tissues. Electron microscopy of lung and kidney interstitial cells showed that 11βHSD1 was localized both to the endoplasmic reticulum and the nuclear membrane. These results show that 11βHSD1 is present in discrete cell populations where it may facilitate intracrine and paracrine glucocorticoid action in addition to its classical role of maintaining circulating glucocorticoids via activity in the liver.

AB - The 11β-hydroxysteroid dehydrogenase type I enzyme (11βHSD1) converts cortisone to cortisol in humans, and 11-dehydrocorticosterone to corticosterone in rodents. In the present study we used a new immunopurified polyclonal antibody, RAH113, to localize 11βHSD1 at the light and electron microscopy levels in a wide range of rat tissues, 11βHSD1 staining in the liver was of highest intensity around the central vein and decreased radially. In the lung, 11βHSD1 was found at highest levels in the interstitial fibroblast, with levels in the type II pneumocyte an order of magnitude lower. RAH113 stained proximal tubules of the renal cortex and interstitial cells of the medulla and papilla. Adrenal 11βHSD1 was confined to the glomerulosa and medulla, whereas the glucocorticoid-inactivating hydroxysteroid dehydrogenase isoform 11βHSD2 was present in fascilulata/reticularis, 11βHSD1 was found in parietal cells of the fundic region of the stomach, but not in the antrum. In the heart, 11βHSD1 was detected in cells resembling interstitial fibroblasts of the endocardium and in the adventitial fibroblasts of blood vessels. Western blot analysis confirmed the presence of an antigen of the correct size (34 kDa) and intensity consistent with levels of enzyme activity previously reported in these tissues. Brain and testis also displayed the 34-kDa protein, confirming the expression of authentic 11βHSD1 in these tissues. Electron microscopy of lung and kidney interstitial cells showed that 11βHSD1 was localized both to the endoplasmic reticulum and the nuclear membrane. These results show that 11βHSD1 is present in discrete cell populations where it may facilitate intracrine and paracrine glucocorticoid action in addition to its classical role of maintaining circulating glucocorticoids via activity in the liver.

UR - http://www.scopus.com/inward/record.url?scp=0035054184&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035054184&partnerID=8YFLogxK

U2 - 10.1210/en.142.4.1644

DO - 10.1210/en.142.4.1644

M3 - Article

VL - 142

SP - 1644

EP - 1651

JO - Endocrinology

JF - Endocrinology

SN - 0013-7227

IS - 4

ER -