Response of recombinant calcineurin to metal ions, reduction-oxidation agents, and enzymatic modification.

  title={Response of recombinant calcineurin to metal ions, reduction-oxidation agents, and enzymatic modification.},
  author={David J. Rhode and Jennifer Imparl-Radosevich and Cheryl J Bartleson and Donna J. Spannaus-Martin and Bruce L. Martin},
  journal={Protein expression and purification},
  volume={26 2},
Recombinant calcineurin heterodimer with the full length delta-isoform of the catalytic subunit (CaN(500)) was expressed in insect cells using the baculovirus system and compared to native bovine brain enzyme in its response to divalent metal ions, redox reagents, and enzymatic modification of arginine residues. The response to various metal ions showed essentially the same profile as bovine brain calcineurin, although Co2+ and Zn2+ did not support recombinant activity as well. Kinetic analysis… Expand
La3+ stimulate the activity of calcineurin in two different ways
The effects of La3+ on CaN activity are unique among metal ions and may provide clues to understand the biological effects ofLa3+. Expand
Expression of chitinase A (chiA) gene from a local isolate of Serratia marcescens in Coleoptera‐specific Bacillus thuringiensis
Aims:  The present study focused on cloning and expression of chiA gene from a highly chitinolytic local isolate of Serratia marcescens in an anti‐Coleopteran Bacillus thuringiensis and comparison ofExpand


Redox Control of Calcineurin by Targeting the Binuclear Fe2+-Zn2+ Center at the Enzyme Active Site*
The interaction of protein serine/threonine phosphatase calcineurin (CaN) with superoxide and hydrogen peroxide was investigated. Superoxide specifically inhibited phosphatase activity of CaN towardExpand
Modification of the calmodulin-stimulated phosphatase, calcineurin, by sulfhydryl reagents.
  • M. King
  • Chemistry, Medicine
  • The Journal of biological chemistry
  • 1986
Results suggest that activation of calcineurin by Ni2+ is synergistic with Ca2+ and indicates an important role for the Ca2-binding subunit in the activation process, and 1 cysteine residue on the catalytic subunit appears to be important in establishing the Ni2-activated conformation of calcinesurin. Expand
Studies of calcineurin-calmodulin interaction: probing the role of arginine residues using peptidylarginine deiminase.
Fluorescence titrations indicate that at least one arginine is important for calmodulin binding and is likely located at the cal modulin binding site of the CaN A subunit. Expand
Chemical modification of the calmodulin-stimulated phosphatase, calcineurin, by phenylglyoxal.
  • M. King, L. Heiny
  • Medicine, Chemistry
  • The Journal of biological chemistry
  • 1987
The results of this modification study indicate that at least 1 arginine residue is essential for the expression of catalytic activity of the calmodulin-regulated phosphatase. Expand
Calcium Regulation of Calcineurin Phosphatase Activity by Its B Subunit and Calmodulin
Kinetic analysis showed that although the purified mutants had no activity in the absence of calcium, they were less dependent than the wild-type enzyme on calcium and calmodulin for activity, consistent with synergistic activation of calcineurin by Ca acting through both CaM and the B subunit. Expand
Superoxide dismutase protects calcineurin from inactivation
The protection of calcineurin against inactivation by superoxide dismutase constitutes a new physiological role for this enzyme which enables the Ca2+-dependent regulation of cellular processes to be modulated by the redox potential. Expand
Selective activation of calcineurin by dipicolinic acid.
  • B. Martin
  • Chemistry, Medicine
  • Archives of biochemistry and biophysics
  • 1997
Atomic absorption spectrometry analysis showed no loss of iron or zinc from calcineurin after activation (2 h) by dipicolinic acid, and incubated with 1.0 mM Mn2+ (saturating levels) also did not show any loss of intrinsic metal by atomic absorption analysis. Expand
Characterization of the phosphatase activity of a baculovirus-expressed calcineurin A isoform.
The reconstitution of the phosphatase activity of an expressed isoform of calcineurin A by purified B subunit and calmodulin may facilitate comparative studies of the regulation of calcinesurin C activity by the B sub unit and cal modulin. Expand
Modulation of the phosphatase activity of calcineurin by oxidants and antioxidants in vitro.
The hypothesis that redox factors modulate the phosphatase activity of calcineurin and suggest that further in vivo studies are warranted is extended. Expand
Activation of Calcineurin by the Trivalent Metal Terbium
The hypothesis that activating, exogenous divalent metal participates directly in catalysis supported, Tb3+ was binding directly at the active site of calcineurin, with the corollary that exogenous activating metal (Mn2+) binds at theactive site of the enzyme. Expand