Research Collection. Enzymology of the final steps in Aldosterone biosynthesis in the rat adrenal cortex. Doctoral Thesis.
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1 Research Collection Doctoral Thesis Enzymology of the final steps in Aldosterone biosynthesis in the rat adrenal cortex Author(s): Lauber, Markus Ernst Publication Date: 1987 Permanent Link: Rights / License: In Copyright NonCommercial Use Permitted This page was generated automatically upon download from the ETH Zurich Research Collection. For more information please consult the Terms of use. ETH Library
2 Diss. ETH No ENZYMOLOGY OF THE FINAL STEPS IN ALDOSTERONE BIOSYNTHESIS IN THE RAT ADRENAL CORTEX A dissertation submitted to the SWISS FEDERAL INSTITUTE OF TECHNOLOGY ZURICH for the degree of Doctor of natural sciences presented by MARKUS ERNST LAUBER Dip!. Natw. ETH born 3rd June 1957 citizen of Luzern, Switzerland accepted on the recommendation of Prof K.H. Winterhalter, examiner Prof. J. Miiller, coexaminer Zurich 1987
3 81 In SUMMARY Whereas cytochrome P450 11/3 was recently shown to catalyze the twostep conversion of corticosterone to aldosterone in the bovine and porcine adrenal cortex, the identity of the enzyme involved in the two final steps of aldosterone biosynthesis in the rat adrenal cortex is as yet unknown. Mitochondria from capsular adrenals of sodiumdeficient, potassiumreplete (stimulated) rats converted corticosterone to 18hydroxycorticosterone and aldosterone at markedly higher rates than mitochondria from capsular adrenals of sodiumreplete, potassiumdeficient (suppressed) rats. However, the same preparations exhibited no difference in their 11/3hydroxylase activities, i.e. the conversion of deoxycorticosterone to cortico sterone. Only mitochondria of zona glomerulosa from rats with stimulated aldosterone biosynthesis contained a 49kD protein which showed a strong crossreactivity with a monoclonal antibody raised against purified bovine cytochrome P450 11(3. contrast, a crossreactive protein with a molecular weight of 51kD was found in mitochondria of zona fasciculata and in mitochondria of zona glomerulosa from rats with a suppressed aldosterone biosynthesis. The two mitochondrial proteins of the rat adrenal cortex exhibited a considerable structural similarity as demonstrated by peptide map ping and immunostaining. However, the catalytic activities of the two proteins differed significantly. Thus, the purified 51kD protein from zona fasciculata catalyzed the conversion of 11deoxycortico sterone to corticosterone and 18OHlldeoxycorticosterone but exhibited no corticosterone methyl oxidase I and II activity. On the other hand, 11/3hydroxylation and CMO I activity could be measured in semipurified 49kD preparations. This indicated the existence of two different forms of cytochrome P450 11(3 in the rat adrenal cortex, with only one of them, i.e. the 49kD form, being capable of catalyzing the two final steps of aldo sterone biosynthesis vn situ. Thus, the enzymology of the late steps of aldosterone biosynthesis in the rat adrenal cortex can be charac terized by a "one enzyme, two forms hypothesis". The experimental
4 82 data, obtained with bovine, porcine and sheep adrenal tissue rather support a "one enzyme hypothesis" for the late steps of aldosterone biosynthesis in these animal species. Thus, even animals with stimulated aldosterone biosynthesis exhibi ted no differences in the total protein pattern of zona glomerulosa and zona fasciculata mitochondria. In addition, the mitochondrial proteins immunoreactive with MAb 258 in the two zones appeared to be identical. Purified preparations of cytochrome P450 11(3 from bovine and porcine adrenals have been shown to catalyze each of the three reactions involved in the conversion of 11deoxycorticosterone to aldosterone. These results indicate that, in contrast to rats, only one enzyme is responsible for the late steps of aldosterone biosynthesis in these animal species. The mechanism, causing the observed zone differences in aldosterone production by intact mitochondria or cells remains to be elucidated.
5 83 ZUSAMMENFASSUNG Obwohl man seit kurzer Zeit weiss, dass gereinigtes Cytochrom P450 11(3 aus Rinder und Schweinenebennieren 11Deoxycorticosterone in Aldosteron umwandeln kann, ist uber das entsprechende Enzym aus Rattennebennieren noch sehr wenig bekannt. Versuche mit verschiedenen Rattendiaten (in Bezug auf Mineralgehalt) haben gezeigt, dass natriumverarmte und kaliumgesattigte Tiere eine stimulierte Aldosteronbiosynthese aufweisen. Im Gegensatz dazu, fuhrt eine natriumreiche und kaliumarme Diat zur vollstandigen Unterdriickung der endogenen Aldosteronproduktion. Der regulatorische Einfluss von Natrium und Kalium beschrankt sich auf die letzten beiden Biosyntheseschritte des Mineralocorticoides und lasst die 11Hydroxylation von 11Deoxycorticosteron praktisch unverandert. Untersuchungen des Proteinmusters von Mitochondrien aus der Zona Glomerulosa von Ratten mit stimulierter Aldosteronbiosynthese zeigten die Anwesenheit eines zusatzlichen 49 kd Proteins. Dieses Protein verfugte uber eine starke Kreuzreaktivitat mit einem monoklonalen Antikorper, gegen gereinigte, bovine 11/3 Hydroxylase. Mitochondrien aus der Zona Fasciculata (unabhangig von der Diat) und aus der Zona Glomerulosa von Ratten mit supprimierter Aldosterobiosynthese enthielten ein immunokreuzreaktives Protein mit einem Molekulargewicht von 51kD. Die beiden mitochondrialen Proteine aus Rattennebennieren sind sich strukturell sehr ahnlich. Das konnte einerseits immunologisch gezeigt werden und wurde durch Experimente mit partieller, proteolytischer Verdauung bestatigt. Trotz dieser strukturellen Aehnlichkeit waren die enzymatischen Eigenschaften der beide Proteine aber verschieden. So katalysierte eine gereinigte Fraktion des 51 kd Proteins nur gerade die 11(3 und 18Hydroxylierung von 11Deoxycorticosteron, wahrend eine angereicherte 49 kd Preparation zusatzlich noch 180H Corticosteron produzierte. Diese experimentellen Befunde ermoglichten die Formulierung einer "Ein Enzym, zwei Formen Hypothese".
6 84 In Anpassung an das Natrium und Kaliumangebot produziert die Ratte jeweils die benotigte Enzymform. Es bleibt jedoch noch abzuklaren, ob das 49 kd Protein ein separates Genprodukt ist oder ob es durch posttranslationelle Modifikation des 51 kd Proteins entsteht. Im Gegensatz zu den Ratten, scheinen andere Saugetiere wie zum Beispiel Rind, Schwein oder Schaf ihre Aldosteronbiosynthese auf eine andere Art und Weise zu organisieren. Die experimentellen Befunde mit diesen Tierspezies deuten auf eine "Ein Enzym Hypothese" der Aldosteronproduktion hin. So konnten auch in "stimulierten" Tieren keine Unterschiede im Proteinmuster zwischen Zona Fasiculata und Zona Glomerulosa gefunden werden. Zusatzlich verhielten sich Mitochondrien von den beiden Zonen identisch in den immunologischen Versuchen mit dem oben erwahnten Antikorper. Ein weiteres Indiz fur die EinEnzymHypothese ist die Tatsache, dass gereinigte 11/3 Hydroxylase als homogene Proteinfraktion (SDSPAGE und IEF) erscheint und 11Deoxycorticosteron in Aldosteron umwandeln kann. Es darf aber nicht vergessen werden, dass auch bei diesen Spezies frisches Gewebe, Zellen oder Mitochondrien den Zonenunterschied in Bezug auf Aldosteronproduktion noch aufweisen. Der Mechanismus des Zonenunterschiedes sowie der physiologischen Regulation dieser Enzymaktivitaten ist bis heute noch nicht bekannt.
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