Protease ‘Clipsin’ extract activity reflects demographic characteristics of human brain
| Autor: | G. C. Stratmann, Andrew W. Procter, Paul T. Francis, Marie-Therese Webster, David M. Bowen |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
medicine.medical_treatment
Molecular Sequence Data Nerve Tissue Proteins Peptide Biology Sex Factors Alzheimer Disease Cause of Death Casein Hydrolase medicine Humans Peptide bond Amino Acid Sequence Aged Aged 80 and over chemistry.chemical_classification Protease General Neuroscience Serine Endopeptidases Brain Caseins Membrane Proteins Human brain Middle Aged medicine.anatomical_structure Chromogenic Compounds Biochemistry Membrane protein chemistry Ionic strength Postmortem Changes Biomarkers |
| Zdroj: | Neuroscience Letters. 143:43-47 |
| ISSN: | 0304-3940 |
| DOI: | 10.1016/0304-3940(92)90229-z |
| Popis: | ‘Clipsin’ and other peptide bond hydrolase activities that appear to be integral membrane proteins, including two implicated in the formation of the histological hallmarks of Alzheimer's disease, were assayed in the frontal and parietal cortex from a large ( n = 45) series of postmortem human brains. Tissues were extracted sequentially with detergent-containing and low ionic strength buffers. The final extracts obtained with detergent-high ionic strength buffer were assayed for peptide-bond hydrolase activity using radiolabelled casein and four chromophore-linked peptide substrates. Hydrolysis of N -succinyl-Ala-Ala-Pro-Phe- p -nitroanilide and α-casein showed evidence of sensitivity to the presence of Alzheimer's disease ( n = 22) and some of the seven other demographic features (postmortem delay; mode of death in the case of one substrate) of the brain samples considered. By contrast, activity towards carbobenzoxy( Z )-Leu-Leu-Glu-2-napthylamide, Z -Val-Lys-Met-4-methyl-coumaryl-7-amide and Z -Val-Lys-Lys-Arg-4-methoxy-2-napthylamide were independent of all factors. The results are discussed in terms of damage to a sub-population of protease-containing membranes. |
| Databáze: | OpenAIRE |
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