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Ca2+-activated prot...
Ca2+-activated protease activity in frog sciatic nerve : Characterization and effect on rapidly transported axonal proteins
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- Kanje, Martin (author)
- Lund University,Lunds universitet,Neuronano Research Center (NRC),Forskargrupper vid Lunds universitet,Biologiska institutionen,Naturvetenskapliga fakulteten,Lund University Research Groups,Department of Biology,Faculty of Science
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- Lazarewicz, Jerzy (author)
- Institute - Center for Molecular and Macromolecular Studies of the Polish Academy of Sciences
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- Ekström, Per (author)
- Lund University,Lunds universitet,Oftalmologi, Lund,Sektion IV,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Retinal degeneration: Molekylär patologi,Forskargrupper vid Lunds universitet,Ophthalmology, Lund,Section IV,Department of Clinical Sciences, Lund,Faculty of Medicine,Retinal degeneration: Molecular Pathology,Lund University Research Groups
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- Edström, Anders (author)
- Lund University,Lunds universitet,Funktionell zoologi,Biologiska institutionen,Naturvetenskapliga fakulteten,Functional zoology,Department of Biology,Faculty of Science
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(creator_code:org_t)
- Elsevier BV, 1985
- 1985
- English 8 s.
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In: Brain Research. - : Elsevier BV. - 0006-8993. ; 327:1-2, s. 29-36
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Abstract
Subject headings
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- Protease activity was studied in the frog sciatic nerve. The activity was measured as the release of TCA-soluble radioactivity from either 3H-labelled proteins transported by rapid axonal transport (AXT) or 3H-labelled ganglionic proteins. In nerve homogenates containing transported substrates, protease activity exhibited two peaks, one around pH 5 and one around pH 8. Ca2+ at 100 μM or higher concentrations only stimulated the latter, which was inhibited by 1 mM parachloromercuric benzoate, a sulphydryl reagent, but unaffected by ATP (1 mM). The proteolytic activity was recovered in the 105 g supernatant of the homogenate. In desheathed nerves containing 3H-labelled transported proteins, the protease activity could be activated by exposing the nerve to a Ca2+-ionophore, X-537 A, or to an elevated Ca2+-concentration (50 mM). These conditions were also shown to increase the influx and efflux of 45Ca2+ in the nerves. The results indicate the presence within axons of a Ca2+-activated soluble protease, which degrades rapidly transported proteins. The finding that the protease degraded ganglionic soluble proteins to about the same extent suggests a broad substrate specificity. The present system should be useful for further characterization of protease activity during various physiological conditions.
Subject headings
- NATURVETENSKAP -- Biologi -- Cellbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Cell Biology (hsv//eng)
Keyword
- axonal transport
- Ca
- protease activity
Publication and Content Type
- art (subject category)
- ref (subject category)
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