Skip to main content
The American Journal of Pathology logoLink to The American Journal of Pathology
. 1997 Jan;150(1):67–73.

Prolactin-derived amyloid in the aging pituitary gland.

P Westermark 1, L Eriksson 1, U Engström 1, S Eneström 1, K Sletten 1
PMCID: PMC1858515  PMID: 9006323

Abstract

Small amyloid deposits occur commonly in different organs in association with aging. As in other amyloids, the fibrils in the age-associated forms are built up by specific proteins, unique to every histological type. The amyloid proteins that have been identified in localized amyloid of human endocrine organs have all been of polypeptide hormone nature, and these include calcitonin, islet amyloid polypeptide (amylin), and atrial natriuretic factor. In the present study, we add prolactin to the increasing group of known amyloid proteins and show that this hormone constitutes the amyloid fibrils of pituitary glands of aging individuals.

Full text

PDF
67

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bilbao J. M., Kovacs K., Horvath E., Higgins H. P., Horsey W. J. Pituitary melanocorticotrophinoma with amyloid deposition. Can J Neurol Sci. 1975 Aug;2(3):199–202. doi: 10.1017/s0317167100020266. [DOI] [PubMed] [Google Scholar]
  2. Blobel G., Dobberstein B. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J Cell Biol. 1975 Dec;67(3):835–851. doi: 10.1083/jcb.67.3.835. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Castaño E. M., Frangione B. Human amyloidosis, Alzheimer disease and related disorders. Lab Invest. 1988 Feb;58(2):122–132. [PubMed] [Google Scholar]
  4. Cooper G. J., Willis A. C., Clark A., Turner R. C., Sim R. B., Reid K. B. Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc Natl Acad Sci U S A. 1987 Dec;84(23):8628–8632. doi: 10.1073/pnas.84.23.8628. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dische F. E., Wernstedt C., Westermark G. T., Westermark P., Pepys M. B., Rennie J. A., Gilbey S. G., Watkins P. J. Insulin as an amyloid-fibril protein at sites of repeated insulin injections in a diabetic patient. Diabetologia. 1988 Mar;31(3):158–161. doi: 10.1007/BF00276849. [DOI] [PubMed] [Google Scholar]
  6. Gibo Y. [Comparison of the pituitary-gonadal functions in men and women]. Nihon Sanka Fujinka Gakkai Zasshi. 1982 Dec;34(12):2244–2252. [PubMed] [Google Scholar]
  7. Gilchrist P. J., Bradshaw J. P. Amyloid formation by salmon calcitonin. Biochim Biophys Acta. 1993 Aug 4;1182(1):111–114. doi: 10.1016/0925-4439(93)90160-3. [DOI] [PubMed] [Google Scholar]
  8. Glenner G. G., Murphy M. A. Amyloidosis of the nervous system. J Neurol Sci. 1989 Dec;94(1-3):1–28. doi: 10.1016/0022-510x(89)90214-1. [DOI] [PubMed] [Google Scholar]
  9. Gustavsson A., Engström U., Westermark P. Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro. Biochem Biophys Res Commun. 1991 Mar 29;175(3):1159–1164. doi: 10.1016/0006-291x(91)91687-8. [DOI] [PubMed] [Google Scholar]
  10. Johansson B., Wernstedt C., Westermark P. Atrial natriuretic peptide deposited as atrial amyloid fibrils. Biochem Biophys Res Commun. 1987 Nov 13;148(3):1087–1092. doi: 10.1016/s0006-291x(87)80243-7. [DOI] [PubMed] [Google Scholar]
  11. Johansson B., Westermark P. The relation of atrial natriuretic factor to isolated atrial amyloid. Exp Mol Pathol. 1990 Jun;52(3):266–278. doi: 10.1016/0014-4800(90)90068-o. [DOI] [PubMed] [Google Scholar]
  12. Landolt A. M., Kleihues P., Heitz P. U. Amyloid deposits in pituitary adenomas. Differentiation of two types. Arch Pathol Lab Med. 1987 May;111(5):453–458. [PubMed] [Google Scholar]
  13. Linke R. P., Voigt C., Störkel F. S., Eulitz M. N-terminal amino acid sequence analysis indicates that isolated atrial amyloid is derived from atrial natriuretic peptide. Virchows Arch B Cell Pathol Incl Mol Pathol. 1988;55(2):125–127. doi: 10.1007/BF02896569. [DOI] [PubMed] [Google Scholar]
  14. Maloy A. L., Longnecker D. S., Greenberg E. R. The relation of islet amyloid to the clinical type of diabetes. Hum Pathol. 1981 Oct;12(10):917–922. doi: 10.1016/s0046-8177(81)80197-9. [DOI] [PubMed] [Google Scholar]
  15. Mandybur T. I. The incidence of cerebral amyloid angiopathy in Alzheimer's disease. Neurology. 1975 Feb;25(2):120–126. doi: 10.1212/wnl.25.2.120. [DOI] [PubMed] [Google Scholar]
  16. Paetau A., Partanen S., Mustajoki P., Valtonen S., Pelkonen R., Wahlström T. Prolactinoma of the pituitary containing amyloid. Acta Endocrinol (Copenh) 1985 Jun;109(2):176–180. doi: 10.1530/acta.0.1090176. [DOI] [PubMed] [Google Scholar]
  17. Polleri A., Masturzo P., Murialdo G., Agnoli A. Circadian rhythmicity of prolactin secretion in elderly subjects: changes during bromocriptine treatment. J Endocrinol Invest. 1981 Jul-Sep;4(3):317–321. doi: 10.1007/BF03349450. [DOI] [PubMed] [Google Scholar]
  18. Rocken Christoph, Uhlig Holger, Saeger Wolfgang, Linke Reinhold P., Fehr Susanne. Amyloid Deposits in Pituitaries and Pituitary Adenomas: Immunohistochemistry and In Situ Hybridization. Endocr Pathol. 1995 Summer;6(2):135–143. doi: 10.1007/BF02739876. [DOI] [PubMed] [Google Scholar]
  19. Rolandi E., Magnani G., Sannia A., Barreca T. Evaluation of Prl secretion in elderly subjects. Acta Endocrinol (Copenh) 1982 Jul;100(3):351–357. doi: 10.1530/acta.0.1000351. [DOI] [PubMed] [Google Scholar]
  20. Saeger W., Gerigk C., Missmahl P. H., Lüdecke D. K. Amyloidablagerungen in Hypophysenadenomen. Polarisationsoptische, immunhistologische und elektronenmikroskopische Untersuchungen. Pathologe. 1983 Jul;4(4):183–189. [PubMed] [Google Scholar]
  21. Saeger W., Warner R., Missmahl H. P. Amyloidosen der Hypophyse im Sektionsgut. Häufigkeit, Verteilung und Korrelationen zum Alter und zu Grundkrankheiten. Pathologe. 1983 Jul;4(4):177–182. [PubMed] [Google Scholar]
  22. Saitoh Y., Mori H., Matsumoto K., Ushio Y., Hayakawa T., Mori S., Arita N., Mogami H. Accumulation of amyloid in pituitary adenomas. Acta Neuropathol. 1985;68(2):87–92. doi: 10.1007/BF00688628. [DOI] [PubMed] [Google Scholar]
  23. Schober R., Nelson D. Fine structure and origin of amyloid deposits in pituitary adenoma. Arch Pathol. 1975 Aug;99(8):403–410. [PubMed] [Google Scholar]
  24. Sletten K., Westermark P., Natvig J. B. Characterization of amyloid fibril proteins from medullary carcinoma of the thyroid. J Exp Med. 1976 Apr 1;143(4):993–998. doi: 10.1084/jem.143.4.993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Stam F. C., Wigboldus J. M., Smeulders A. W. Age incidence of senile brain amyloidosis. Pathol Res Pract. 1986 Oct;181(5):558–562. doi: 10.1016/S0344-0338(86)80149-2. [DOI] [PubMed] [Google Scholar]
  26. Tashima T., Kitamoto T., Tateishi J., Ogomori K., Nakagaki H. Incidence and characterization of age related amyloid deposits in the human anterior pituitary gland. Virchows Arch A Pathol Anat Histopathol. 1988;412(4):323–327. doi: 10.1007/BF00750258. [DOI] [PubMed] [Google Scholar]
  27. Touitou Y., Fèvre M., Lagoguey M., Carayon A., Bogdan A., Reinberg A., Beck H., Cesselin F., Touitou C. Age- and mental health-related circadian rhythms of plasma levels of melatonin, prolactin, luteinizing hormone and follicle-stimulating hormone in man. J Endocrinol. 1981 Dec;91(3):467–475. doi: 10.1677/joe.0.0910467. [DOI] [PubMed] [Google Scholar]
  28. Weiske W. H., Frick J. Plasmaprolactin in den verschiedenen Altersstufen. Padiatr Padol Suppl. 1977;(5):49–55. [PubMed] [Google Scholar]
  29. Westermark P., Engström U., Johnson K. H., Westermark G. T., Betsholtz C. Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation. Proc Natl Acad Sci U S A. 1990 Jul;87(13):5036–5040. doi: 10.1073/pnas.87.13.5036. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Westermark P., Grimelius L., Polak J. M., Larsson L. I., Van Noorden S., Wilander E., Pearse A. G. Amyloid in polypeptide hormone-producing tumors. Lab Invest. 1977 Aug;37(2):212–215. [PubMed] [Google Scholar]
  31. Westermark P., Johansson B., Natvig J. B. Senile cardiac amyloidosis: evidence of two different amyloid substances in the ageing heart. Scand J Immunol. 1979;10(4):303–308. doi: 10.1111/j.1365-3083.1979.tb01355.x. [DOI] [PubMed] [Google Scholar]
  32. Westermark P., Johnson K. H., O'Brien T. D., Betsholtz C. Islet amyloid polypeptide--a novel controversy in diabetes research. Diabetologia. 1992 Apr;35(4):297–303. doi: 10.1007/BF00401195. [DOI] [PubMed] [Google Scholar]
  33. Westermark P., Wernstedt C., O'Brien T. D., Hayden D. W., Johnson K. H. Islet amyloid in type 2 human diabetes mellitus and adult diabetic cats contains a novel putative polypeptide hormone. Am J Pathol. 1987 Jun;127(3):414–417. [PMC free article] [PubMed] [Google Scholar]
  34. Westermark P., Wernstedt C., Wilander E., Hayden D. W., O'Brien T. D., Johnson K. H. Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Proc Natl Acad Sci U S A. 1987 Jun;84(11):3881–3885. doi: 10.1073/pnas.84.11.3881. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Westermark P., Wernstedt C., Wilander E., Sletten K. A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas. Biochem Biophys Res Commun. 1986 Nov 14;140(3):827–831. doi: 10.1016/0006-291x(86)90708-4. [DOI] [PubMed] [Google Scholar]
  36. Westermark P., Wilander E. The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus. Diabetologia. 1978 Nov;15(5):417–421. doi: 10.1007/BF01219652. [DOI] [PubMed] [Google Scholar]
  37. Yamaji T., Shimamoto K., Ishibashi M., Kosaka K., Orimo H. Effect of age and sex on circulating and pituitary prolactin levels in human. Acta Endocrinol (Copenh) 1976 Dec;83(4):711–719. doi: 10.1530/acta.0.0830711. [DOI] [PubMed] [Google Scholar]

Articles from The American Journal of Pathology are provided here courtesy of American Society for Investigative Pathology

RESOURCES