Neuroendocrinology
Original Paper
Human Pituitary Phenol Sulfotransferase: Biochemical Properties and Activities of the Thermostable and Thermolabile FormsAnderson R.J. · Yoon J.K. · Sinsheimer E.G. · Jackson B.L.Section of Endocrinology and Metabolism, Department of Medicine, Veterans Administration West Side Medical Center, University of Illinois College of Medicine at Chicago, Chicago, Ill., USA
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Article / Publication Details
Received: November 25, 1985
Accepted: April 09, 1986
Published online: April 01, 2008
Issue release date: 1986
Number of Print Pages: 8
Number of Figures: 0
Number of Tables: 0
ISSN: 0028-3835 (Print)
eISSN: 1423-0194 (Online)
For additional information: https://www.karger.com/NEN
Abstract
Pituitary tissue contains phenol sulfotransferase (PST), the enzyme that catalyzes the sulfate conjugation of monoamine neurotransmitters. We carried out these studies with pituitaries obtained 21.3 ± 3.0 h postmortem (mean ± SEM; n = 21) to determine whether the biochemical properties and variations in levels of human pituitary PST activities were similar to those of PST in platelets from control subjects. PST in the human platelet has been studied thoroughly because of the possibility that platelet PST might reflect levels of PST activity in other tissues such as the pituitary and brain. Our results demonstrated 2 forms of the pituitary enzyme that were similar to the thermostable (TS) and thermolabile (TL) forms of platelet PST with regard to assay conditions, pH optima, Km values for multiple substrates, responses to 2,6-dichloro-4-nitrophenol (DCNP), and thermal stability properties. Pituitary samples also were obtained at autopsy 6.3 ± 0.33 h (mean ± SEM; n = 3) after death to determine the effects of storage at 4 °C on PST activities. After storage for 6–18 h, 83–99.6% of the TS PST activity remained and 44–66.9% of the TL PST activity remained. Pituitary TS PST activity in samples obtained within 12.1 ± 3.25 h after death was 121.0 ± 49.1 units/mg protein (mean ± SEM; n = 7) with a range from 9.7 to 367.6. TL PST activity was 35.6 ± 11.6 units/mg protein (mean ± SEM; n = 6) with a range from 6.1 to 80.7. Wide variations of both enzyme activities were also present in 3 pituitary tumor samples. Therefore, at least 2 forms of PST were present in the human pituitary, and the pituitary enzymes were biochemically similar to platelet TS and TL PST activities. It will now be feasible to determine whether variations in the levels of platelet PST activities might be useful measures of normal and tumor pituitary PST activities.
© 1986 S. Karger AG, Basel
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Article / Publication Details
Received: November 25, 1985
Accepted: April 09, 1986
Published online: April 01, 2008
Issue release date: 1986
Number of Print Pages: 8
Number of Figures: 0
Number of Tables: 0
ISSN: 0028-3835 (Print)
eISSN: 1423-0194 (Online)
For additional information: https://www.karger.com/NEN
Copyright / Drug Dosage / Disclaimer
Copyright: All rights reserved. No part of this publication may be translated into other languages, reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording, microcopying, or by any information storage and retrieval system, without permission in writing from the publisher.Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug.
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