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. 1965 Nov;97(2):518–522. doi: 10.1042/bj0970518

Lysosomal enzyme changes in enforced mammary-gland involution

A L Greenbaum 1,2,3, T F Slater 1,2,3, D Y Wang 1,2,3
PMCID: PMC1264669  PMID: 16749158

Abstract

1. Changes occurring in the activities and latency of acid ribonuclease and β-glucuronidase have been studied in rat mammary gland during the early phases of mammary involution. 2. It was found that there were rapid increases in the proportions of both enzymes in the `free' (i.e. unsedimentable) form. The total activities of both enzymes did not show the rapid decrease characteristic of most other enzymes studied during mammary-gland involution. 3. The effects of pretreating the rats with reserpine or the antihistamine drug Phenergan on these lysosomal changes was studied. Neither treatment affected the enzymic redistribution that occurs during early involution. 4. It was concluded that lysosomal rupture occurs as an early manifestation of mammary-gland involution. Although reserpine treatment preserves the histological appearance of the gland and, apparently, inhibits involution, this drug did not prevent the lysosomal changes normally found in suspensions.

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Selected References

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

  1. BENSON G. K. Effect of reserpine on mammary gland involution and on other organs in the rat. Proc Soc Exp Biol Med. 1958 Dec;99(3):550–553. doi: 10.3181/00379727-99-24416. [DOI] [PubMed] [Google Scholar]
  2. BENSON G. K., FOLLEY S. J. Oxytocin as stimulator for the release of prolactin from the anterior pituitary. Nature. 1956 Apr 14;177(4511):700–700. doi: 10.1038/177700a0. [DOI] [PubMed] [Google Scholar]
  3. BENSON G. K. Further studies on effects of tranquilizing drugs on mammary involution in the rat. Proc Soc Exp Biol Med. 1960 Jan;103:132–137. doi: 10.3181/00379727-103-25436. [DOI] [PubMed] [Google Scholar]
  4. BINGHAM E. W., ZITTLE C. A. Purification and properties of acid phosphatase in bovine milk. Arch Biochem Biophys. 1963 Jun;101:471–477. doi: 10.1016/0003-9861(63)90505-8. [DOI] [PubMed] [Google Scholar]
  5. BINGHAM E. W., ZITTLE C. A. Ribonuclease in bovine milk. Biochem Biophys Res Commun. 1962 May 11;7:408–413. doi: 10.1016/0006-291x(62)90325-x. [DOI] [PubMed] [Google Scholar]
  6. DARBY F. J., WANG D. Y., GREENBAUM A. L. THE INFLUENCE OF RESERPINE ON THE NUCLEIC ACID AND ACID-SOLUBLE RIBONUCLEOTIDE CONTENTS OF INVOLUTING MAMMARY TISSUE OF RATS. J Endocrinol. 1964 Feb;28:329–337. doi: 10.1677/joe.0.0280329. [DOI] [PubMed] [Google Scholar]
  7. DE DUVE C., BEAUFAY H. Tissue fractionation studies. 10. Influence of ischaemia on the state of some bound enzymes in rat liver. Biochem J. 1959 Dec;73:610–616. doi: 10.1042/bj0730610. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. DE DUVE C., PRESSMAN B. C., GIANETTO R., WATTIAUX R., APPELMANS F. Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue. Biochem J. 1955 Aug;60(4):604–617. doi: 10.1042/bj0600604. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. EMANUEL C. F., CHAIKOFF I. L. An hydraulic homogenizer for the controlled release of cellular components from various tissues. Biochim Biophys Acta. 1957 May;24(2):254–261. doi: 10.1016/0006-3002(57)90191-9. [DOI] [PubMed] [Google Scholar]
  10. GIANETTO R., DE DUVE C. Tissue fractionation studies. 4. Comparative study of the binding of acid phosphatase, beta-glucuronidase and cathepsin by rat-liver particles. Biochem J. 1955 Mar;59(3):433–438. doi: 10.1042/bj0590433. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. GLOCK G. E., McLEAN P. Pathways of glucose utilization in mammary tissue. Proc R Soc Lond B Biol Sci. 1958 Dec 17;149(936):354–362. doi: 10.1098/rspb.1958.0075. [DOI] [PubMed] [Google Scholar]
  12. GREENBAUM A. L., GREENWOOD F. C. Some enzymic changes in the mammary gland of rats during pregnancy, lactation and mammary involution. Biochem J. 1954 Apr;56(4):625–631. doi: 10.1042/bj0560625. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. GREENBAUM A. L., SLATER T. F. Studies on the particulate components of rat mammary gland. II. Changes in the levels of the nucleic acids of the mammary glands of rats during pregnancy, lactation and mammary involution. Biochem J. 1957 May;66(1):155–161. doi: 10.1042/bj0660155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. GREENBAUM A. L., SLATER T. F., WANG D. Y. Lysosomal-like particles in the rat mammary gland. Nature. 1960 Oct 22;188:318–320. doi: 10.1038/188318a0. [DOI] [PubMed] [Google Scholar]
  15. Greenbaum A. L., Darby F. J. The effect of adrenalectomy on the metabolism of the mammary glands of lactating rats. Biochem J. 1964 May;91(2):307–317. doi: 10.1042/bj0910307. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  17. McLEAN P. Carbohydrate metabolism of mammary tissue. I. Pathways of glucose catabolism in the mammary gland. Biochim Biophys Acta. 1958 Nov;30(2):303–315. doi: 10.1016/0006-3002(58)90055-6. [DOI] [PubMed] [Google Scholar]
  18. REES K. R., SHOTLANDER V. L., SINHA K. P. Blood enzymes in liver injury following dimethylnitrosamine poisoning. J Pathol Bacteriol. 1962 Apr;83:483–490. [PubMed] [Google Scholar]
  19. REYNOLDS E. S. LIVER PARENCHYMAL CELL INJURY. I. INITIAL ALTERATIONS OF THE CELL FOLLOWING POISONING WITH CARBON TETRACHLORIDE. J Cell Biol. 1963 Oct;19:139–157. doi: 10.1083/jcb.19.1.139. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. SLATER T. F. Studies on mammary involution. I. Chemical changes. Arch Int Physiol Biochim. 1962 Mar;70:167–178. doi: 10.3109/13813456209092850. [DOI] [PubMed] [Google Scholar]
  21. SMUCKLER E. A., BENDITT E. P. Carbon tetrachloride poisoning in rats: alteration in ribosomes of the liver. Science. 1963 Apr 19;140(3564):308–310. doi: 10.1126/science.140.3564.308. [DOI] [PubMed] [Google Scholar]
  22. Slater T. F., Greenbaum A. L. Changes in lysosomal enzymes in acute experimental liver injury. Biochem J. 1965 Aug;96(2):484–491. doi: 10.1042/bj0960484. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Slater T. F. Ribonuclease activity in the rat mammary gland during pregnancy, lactation and mammary involution. Biochem J. 1961 Mar;78(3):500–504. doi: 10.1042/bj0780500. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Slater T. F., Sträuli U. D., Sawyer B. C. Changes in liver nucleotide concentrations in experimental liver injury. 1. Carbon tetrachloride poisoning. Biochem J. 1964 Nov;93(2):260–266. doi: 10.1042/bj0930260. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. VANLANCKER J. L. LYSOSOMES. CONCLUDING REMARKS. Fed Proc. 1964 Sep-Oct;23:1050–1052. [PubMed] [Google Scholar]
  26. WANG D. Y. Effects of short-term weaning on the acid-soluble ribonucleotides of rat mammary gland. Nature. 1960 Dec 24;188:1109–1110. doi: 10.1038/1881109a0. [DOI] [PubMed] [Google Scholar]
  27. ZALKIN H., TAPPEL A. L., CALDWELL K. A., SHIBKO S., DESAI I. D., HOLLIDAY T. A. Increased lysosomal enzymes in muscular dystrophy of vitamin E-deficient rabbits. J Biol Chem. 1962 Aug;237:2678–2682. [PubMed] [Google Scholar]

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