Effect of α-crystallin on thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase

Khanova, Helen A.; Markossian, Kira A.; Kleimenov, S. Yu.; Levitsky, Dmitrii I.; Chebotareva, Natalia A.; Golub, Nikolay V.; Asryants, R.A.; Muronetz, Vladimir I.; Saso, Luciano; Yudin, I. K.; Muranov, Konstantin O.; Оstrovsky, М. А.; Bi, Kurganov

doi:10.1016/j.bpc.2006.11.002

Cited by 53 publications

(57 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the presence of a-crystallin, the displacement of the position of the maximum on the DSC profile for GAPDH toward the lower temperatures was observed. 6 Besides, acrystallin accelerated thermal inactivation of GAPDH. 48 It is known that the elevated temperatures induce dissociation of the tetrameric form of GAPDH into oligomeric forms of lesser size.…”

Section: Discussionmentioning

confidence: 99%

Kinetics of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle: Mechanism of protective action of α‐crystallin

et al. 2007

Self Cite

View full text Add to dashboard Cite

The kinetics of thermal aggregation of glycogen phosphorylase b (Phb) from rabbit skeletal muscle have been studied by dynamic light scattering (0.08M Hepes, pH 6.8, containing 0.1M NaCl; 48 degrees C). The hydrodynamic radius of the start aggregates determined from the initial linear parts of the dependences of the hydrodynamic radius (R(h)) on time was found to be 16.7 +/- 1.0 nm. At rather high values of time, the R(h) value for the protein aggregates becomes proportional to t(1/1.8) = t(0.56) suggesting that the aggregation process proceeds in the regime of diffusion-limited cluster-cluster aggregation. In the presence of alpha-crystallin, a protein possessing the chaperone-like activity, the process of protein aggregation switches to the regime of reaction-limited cluster-cluster aggregation as indicated by the exponential dependence of the R(h) value on time. It was shown that the addition of alpha-crystallin raises the rate of thermal inactivation of Phb. These data in combination with the results of the study of interaction of Phb with alpha-crystallin by analytical ultracentrifugation suggest that alpha-crystallin interacts with the intermediates of unfolding of the Phb molecule.

show abstract

Section: Discussionmentioning

confidence: 99%

Kinetics of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle: Mechanism of protective action of α‐crystallin

et al. 2007

Self Cite

View full text Add to dashboard Cite

show abstract

“…Khanova and coworkers [40] examined the effects of a-crystallin on GAPDH. As determined by differential scanning calorimetry, thermal-induced dissociation/unfolding of GAPDH (at, approximately 3 mM) occurred at 61.6 C. In the presence of a-crystallin (at, 0.4 mg/mL), the temperature transition for GAPDH dissociation/unfolding occurred at 58.0 C, indicating that the stability of GAPDH is markedly reduced in the presence of a-crystallin.…”

Section: Folding Accessory Proteinsmentioning

confidence: 99%

Dynamic Oligomeric Properties

Seidler

2012

GAPDH: Biological Properties and Diversity

View full text Add to dashboard Cite

This chapter provides a foundation for further research into the relationship between dynamic oligomeric properties and functional diversity. The structural basis that underlies the conformational sub-states of the GAPDH oligomer is discussed. The issue of protein stability is given a thorough analysis, since it is well-established that the primary strategy for protein oligomerization is to stabilize conformation. Several factors that affect oligomerization are described, including chemical modification by synthetic reagents. The effects of native substrates and coenzymes are also discussed. The curious feature of chloride ions having a de-stabilizing effect on native GAPDH structure is described. Additionally, the role of adenine dinucleotides in tetramer-dimer equilibrium dynamics is suggested to be a major part of the physiological regulation of GAPDH structure and function. This chapter also contends that a vast amount of useful information can come from comparative analyses of diverse species, particularly regarding protein stability and subunit-subunit interaction. Lastly, the concept of domain exchange is introduced as a means of understanding the stabilization of dynamic oligomers, suggesting that inter-subunit contacts may also be a way of masking docking sites to other proteins.

show abstract

“…These molecular volumes ranged from 171,000 to 179,000 Å 3 . Khanova and coworkers [27] measured the hydrodynamic radius of GAPDH from dynamic light scattering. The diameter of GAPDH in this study was determined to be 86 Å .…”

Section: Actin Filamentsmentioning

confidence: 99%

Functional Diversity

Seidler

2012

GAPDH: Biological Properties and Diversity

View full text Add to dashboard Cite

There is increasing evidence to support a gene economy model that is fully based on the principles of evolution in which a limited number of proteins does not necessarily reflect a finite number of biochemical processes. The concept of 'gene sharing' proposes that a single protein can have alternate functions that are typically attributed to other proteins. GAPDH appears to play this role quite well in that it exhibits more than one function. GAPDH represents the prototype for this new paradigm of protein multi-functionality. The chapter discusses the diverse functions of GAPDH among three broad categories: cell structure, gene expression and signal transduction. Protein function is curiously re-specified given the cell's unique needs. GAPDH provides the cell with the means of linking metabolic activity to various cellular processes. While interpretations may often lead to GAPDH's role in meeting focal energy demands, this chapter discusses several other very distinct GAPDH functions (i.e. membrane fusogenic properties) that are quite different from its ability to catalyze oxidative phosphorylation of the triose, glyceraldehyde 3-phosphate. It is suggested that a single protein participates in multiple processes in the structural organization of the cell, controls the transmission of genetic information (i.e. GAPDH's involvement may not be finite) and mediates intracellular signaling.

show abstract

Effect of α-crystallin on thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase

Cited by 53 publications

References 35 publications

Kinetics of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle: Mechanism of protective action of α‐crystallin

Kinetics of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle: Mechanism of protective action of α‐crystallin

Dynamic Oligomeric Properties

Functional Diversity

Contact Info

Product

Resources

About