ArticlePlant physiology1993
Investigation of the Calcium-Transporting ATPases at the Endoplasmic Reticulum and Plasma Membrane of Red Beet (Beta vulgaris).
Article in Plant physiology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 48 citations in OpenAlex.
- Epigenetic Regulation in Heterosis and Environmental Stress: The Challenge of Producing Hybrid Epigenomes to Face Climate Change.Epigenomes · 2023Review
- Comparison of the heat stress induced variations in DNA methylation between heat-tolerant and heat-sensitive rapeseed seedlings.Breeding science · 2014Article
- A thapsigargin-sensitive Ca(2+) pump is present in the pea Golgi apparatus membrane.Plant physiology · 2002Article
- Mobilization of Ca2+ by cyclic ADP-ribose from the endoplasmic reticulum of cauliflower florets.Plant physiology · 2001Article
- At-ACA8 encodes a plasma membrane-localized calcium-ATPase of Arabidopsis with a calmodulin-binding domain at the N terminus.Plant physiology · 2000Article
- Calcium release from the endoplasmic reticulum of higher plants elicited by the NADP metabolite nicotinic acid adenine dinucleotide phosphate.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Purification of the Plasma Membrane Ca2+-ATPase from Radish Seedlings by Calmodulin-Agarose Affinity ChromatographyPlant physiology · 1998Article
- Distinction between Endoplasmic Reticulum-Type and Plasma Membrane-Type Ca2+ Pumps (Partial Purification of a 120-Kilodalton Ca2+-ATPase from Endomembranes).Plant physiology · 1997Article
- A Single Gene May Encode Differentially Localized Ca2+-ATPases in Tomato.The Plant cell · 1996Article
- Regulation of Plant Defense Response to Fungal Pathogens: Two Types of Protein Kinases in the Reversible Phosphorylation of the Host Plasma Membrane H+-ATPase.The Plant cell · 1996Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calcium-transporting ATPases were compared in endoplasmic reticulum (ER)- and plasma membrane-enriched fractions of red beet (Beta vulgaris L.) storage tissue by measuring 45Ca uptake and calcium-dependent phosphoenzyme formation. The plasma membrane fraction was prepared by aqueous two-phase partitioning of a microsomal fraction and collecting the upper phase. The ER-enriched fraction was obtained by submitting a sucrose-gradient ER-enriched fraction to aqueous two-phase partitioning and collecting the lower phase; this reduced contaminating plasma membrane, which partitioned into the upper phase. The ATP-dependent calcium uptake observed in both fractions was released by the calcium ionophore A23187. Calcium uptake showed saturation kinetics for calcium with Km values of 0.92 mmol m-3 for the ER fraction and 1.24 mmol m-3 for the plasma membrane fraction. Uptake into both fractions was inhibited by vanadate and erythrosin B, although the plasma membrane system was slightly more sensitive to both inhibitors. Cyclopiazonic acid and thapsigargin, at low concentrations, had no marked effect on uptake. The plasma membrane system was less substrate-specific for ATP than the ER system, since it was able to use GTP and ITP to drive calcium transport at up to 50% of the level obtained with ATP. Following phosphorylation with [[gamma]-32P]ATP, two high molecular mass, calcium-dependent phosphoproteins (119 and 124 kD) and a low molecular mass, calcium-independent phosphoprotein (17 kD) were observed in the plasma membrane fraction. The ER fraction showed one high molecular mass phosphoprotein (119 kD) in the presence of calcium and two low molecular mass phosphoproteins (17 and 20 kD) that showed no calcium dependence. The low molecular mass phosphoproteins were insensitive to hydroxyl-amine, but they did show turnover. The identity of these proteins is unknown, but they do not have the properties of phosphorylated intermediates of calcium-ATPases. In contrast, the high molecular mass phosphoproteins displayed properties consistent with their representing phosphorylated intermediates of E1E2-type ATPases; they were hydroxylamine-sensitive, showed rapid turnover, and were inhibited by vanadate. Because they showed calcium-dependent phosphorylation and were sensitive to erythrosin B, the 119- and 124-kD phosphoproteins may be phosphorylated intermediates of the ER and plasma membrane calcium ATPases. These phosphoproteins were characterized further with respect to inhibitor sensitivity, responses to ions, and substrate specificity.
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Registered trials
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