Literature DB >> 2925646

Plant cells contain calsequestrin.

K H Krause1, M Chou, M A Thomas, R D Sjolund, K P Campbell.   

Abstract

Calsequestrin is a high capacity low affinity Ca2+-binding protein thought to be essential for the function of the intracellular rapid releasable Ca2+ pool of a variety of animal cells. Here we show that two types of plant tissues, cultured Streptanthus tortuosus cells and spinach leaves, contain a form of calsequestrin. In subcellular fractions of S. tortuosus cells, Stains-all staining reveals a metachromatically blue-staining 56,000-Da protein enriched in the microsomal fraction. This protein shares several biochemical characteristics with animal calsequestrin: 1) it changes its apparent molecular weight with the pH; 2) it is able to bind 45Ca2+ on nitrocellulose transfers; and 3) it is recognized by antibodies against canine cardiac calsequestrin. Calsequestrin was also identified in spinach leaves using a direct extraction procedure that was developed for muscle calsequestrin. Thus, our results demonstrate that plant cells contain calsequestrin within a subcellular membrane fraction. These results also suggest that calsequestrin is an ubiquitous protein rather than being limited only to animal cells.

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Year:  1989        PMID: 2925646

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  11 in total

1.  The calcium-binding activity of a vacuole-associated, dehydrin-like protein is regulated by phosphorylation.

Authors:  Bruce J Heyen; Muath K Alsheikh; Elizabeth A Smith; Carl F Torvik; Darren F Seals; Stephen K Randall
Journal:  Plant Physiol       Date:  2002-10       Impact factor: 8.340

Review 2.  The plant phosphoinositide system.

Authors:  B K Drøbak
Journal:  Biochem J       Date:  1992-12-15       Impact factor: 3.857

3.  Antibodies against the Calcium-Binding Protein: Calsequestrin from Streptanthus tortuosus (Brassicaceae).

Authors:  M Chou; K H Krause; K P Campbell; K G Jensen; R D Sjolund
Journal:  Plant Physiol       Date:  1989-12       Impact factor: 8.340

4.  Identification and characterization of cDNA clones encoding plant calreticulin in barley.

Authors:  F Chen; P M Hayes; D M Mulrooney; A Pan
Journal:  Plant Cell       Date:  1994-06       Impact factor: 11.277

5.  Calreticulin is a candidate for a calsequestrin-like function in Ca2(+)-storage compartments (calciosomes) of liver and brain.

Authors:  S Treves; M De Mattei; M Landfredi; A Villa; N M Green; D H MacLennan; J Meldolesi; T Pozzan
Journal:  Biochem J       Date:  1990-10-15       Impact factor: 3.857

6.  Calcium Fluxes across the Plasma Membrane of Commelina communis L. Assayed in a Cell-Free System.

Authors:  B Siebers; P Gräf; E W Weiler
Journal:  Plant Physiol       Date:  1990-07       Impact factor: 8.340

7.  Calsequestrinlike calcium-binding protein is expressed in calcium-accumulating cells of Pistia stratiotes.

Authors:  V R Franceschi; X Li; D Zhang; T W Okita
Journal:  Proc Natl Acad Sci U S A       Date:  1993-08-01       Impact factor: 11.205

8.  Widespread tissue distribution of rabbit calreticulin, a non-muscle functional analogue of calsequestrin.

Authors:  S Tharin; E Dziak; M Michalak; M Opas
Journal:  Cell Tissue Res       Date:  1992-07       Impact factor: 5.249

9.  Evidence that spinach leaves express calreticulin but not calsequestrin.

Authors:  L Navazio; B Baldan; P Dainese; P James; E Damiani; A Margreth; P Mariani
Journal:  Plant Physiol       Date:  1995-11       Impact factor: 8.340

10.  Characterization of a calsequestrin-like protein from sea-urchin eggs.

Authors:  D Lebeche; B Kaminer
Journal:  Biochem J       Date:  1992-11-01       Impact factor: 3.857

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