Abstract
1. Five-day-old anaesthetized rats subjected to slow, prolonged asphyxia (50–55 min) were either allowed to die or resuscitated when at the point of death. Activities of various cerebral acid hydrolases known to be associated with lysosomes were determined in these animals and in littermate controls. 2. Asphyxia to death resulted in a significant increase in the activities of acid phosphatase, cathepsin (pH5.0) and β-glucuronidase in whole-brain homogenates. 3. The effect of asphyxia on β-glucuronidase activity was not apparent when the assay was performed in the presence of Triton X-100 (0.1%, v/v). 4. In resuscitated animals whole-brain-homogenate β-glucuronidase activity showed the greatest increase (31%) 15 min after recovery. After a 60 min recovery period differences between control and asphyxiated animals were no longer apparent. 5. In animals anoxiated to death activities of acid phosphatase and β-N-acetylglucosaminidase in brain high-speed supernatants were significantly higher than in controls. Acid phosphatase activity was similarly increased in asphyxiated animals resuscitated for 5 or 60 min. 6. It is suggested that the response of the immature rat brain to asphyxia involves a disruption or increased fragility of lysosomal particles.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Adlard B. P., Dobbing J. Vulnerability of developing brain. 3. Development of four enzymes in the brains of normal and undernourished rats. Brain Res. 1971 Apr 16;28(1):97–107. doi: 10.1016/0006-8993(71)90527-0. [DOI] [PubMed] [Google Scholar]
- 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]
- DE DUVE C., WATTIAUX R. Tissue fractionation studies. VII. Release of bound hydrolases by means of triton X-100. Biochem J. 1956 Aug;63(4):606–608. doi: 10.1042/bj0630606. [DOI] [PMC free article] [PubMed] [Google Scholar]
- De Duve C., Wattiaux R. Functions of lysosomes. Annu Rev Physiol. 1966;28:435–492. doi: 10.1146/annurev.ph.28.030166.002251. [DOI] [PubMed] [Google Scholar]
- 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]
- KOENIG H., GAINES D., MCDONALD T., GRAY R., SCOTT J. STUDIES OF BRAIN LYSOSOMES. I. SUBCELLULAR DISTRIBUTION OF FIVE ACID HYDROLASES, SUCCINATE DEHYDROGENASE AND GANGLIOSIDES IN RAT BRAIN. J Neurochem. 1964 Oct;11:729–743. doi: 10.1111/j.1471-4159.1964.tb06118.x. [DOI] [PubMed] [Google Scholar]
- 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]
- SELLINGER O. Z., RUCKER D. L., DE BALBIAN VERSTER F. CEREBRAL LYSOSOMES--I. A COMPARATIVE STUDY OF LYSOSOMAL N-ACETYL-BETA-D-GLUCOSAMINIDASE AND MITOCHONDRIAL ASPARTIC TRANSAMINASE OF RAT CEREBRAL CORTEX. J Neurochem. 1964 Apr;11:271–280. doi: 10.1111/j.1471-4159.1964.tb06141.x. [DOI] [PubMed] [Google Scholar]
- Weissmann G. Lysosome. N Engl J Med. 1965 Nov 11;273(20):1084–contd. doi: 10.1056/NEJM196511112732006. [DOI] [PubMed] [Google Scholar]