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Modulation of an Intracellular Calmodulin-Stimulated Ca2+-Pumping ATPase in Cauliflower by Trypsin (The Use of Calcium Green-5N to Measure Ca2+ Transport in Membrane Vesicles)
Jönköping University, School of Education and Communication, HLK, Disciplinary Research. Department of Plant Biochemistry, Lund University, Lund, Sweden.ORCID iD: 0000-0003-0117-2974
1996 (English)In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 110, no 3, p. 913-922Article in journal (Refereed) Published
Abstract [en]

The effect of controlled trypsin digestion of a calmodulin-stimulated Ca2+-ATPase in low-density intracellular membranes from cauliflower (Brassica oleracea L.) inflorescences was investigated. Ca2+ uptake into vesicles was measured either continuously with the fluorescent Ca2+ indicator Calcium Green-5N or with a radio-active filter technique. Trypsin treatment of vesicles resulted in a 3-fold activation of Ca2+ uptake and loss of calmodulin sensitivity. Immunoblotting experiments with an antiserum raised against the Ca2+-ATPase showed that the trypsin activation was accompanied by a decrease in the amount of intact Ca2+-ATPase (111 kD) and by successive appearances of polypeptides of 102 and 99 to 84 kD. 125I-Calmodulin overlays showed that only the intact Ca2+-ATPase bound calmodulin. Removal of the calmodulin-binding domain (about 9 kD) was not enough to obtain full activation. Trypsin proteolysis resulted in a Ca2+ concentration necessary for half-maximal activity of 0.5 [mu]M, whereas a value of about 2 [mu]M was obtained with untreated membranes in the presence of calmodulin. Without trypsin treatment or calmodulin the activity was not saturated even at 57 [mu]M free Ca2+. The data suggest that trypsin digestion and calmodulin activate the cauliflower Ca2+-ATPase by at least partly different mechanisms.

Place, publisher, year, edition, pages
1996. Vol. 110, no 3, p. 913-922
National Category
Biochemistry and Molecular Biology
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URN: urn:nbn:se:hj:diva-2175PubMedID: 12226230OAI: oai:DiVA.org:hj-2175DiVA, id: diva2:32995
Available from: 2007-10-17 Created: 2007-10-17 Last updated: 2017-12-12Bibliographically approved

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