Geodesic
Study of interactions of different forms of glyceraldehyde-3-phosphate dehydrogenase with the chaperonin Hsp 70
Vestnik Samarskogo universiteta. Estestvennonaučnaâ seriâ, no. 6 (2009), pp. 213-221 Cet article a éte moissonné depuis la source Math-Net.Ru

Voir la notice de l'article

Interaction of different forms of glyceraldehyde-3-phosphate dehydrogenase (GAPD) with the chaperonin Hsp 70 was investigated using enzyme-linked immunosorbent assay (ELISA). The developed approach is convenient for investigation of the interaction between Hsp 70 and GAPD (and presumably with other target proteins) and the influence of different effectors on this interaction. The assay is automatic and does not require large amounts of the proteins and their ligands. Both methods did not detect any interactions between native GAPD and Hsp 70. The addition of the substrate or cofactor or acylation of the enzyme did not induce its binding to Hsp 70. Denatured forms of GAPD obtained by the dissociation of the enzyme into subunits in a water solution or by the sorption of the enzyme on an ELISA plate efficiently bound to the chaperonin Hsp 70. It was demonstrated that denatured GAPD immobilized on Sepharose also interacted with soluble Hsp 70. Thus, we showed that the chaperonin Hsp 70 binds denatured forms of GAPD, which must prevent its participation in decomposition of amyloid structures (for example, aggregates of the huntingtin protein).
Keywords: glyceraldehyde-3-phosphate dehydrogenase, chaperonin Hsp 70, immobilization, amyloid structures. 
@article{VSGU_2009_6_a21,
     author = {M. Yu. Yazykova and E. V. Shmal'gauzen and I. N. Naletova and A. P. Pleten' and V. I. Muronets},
     title = {Study of interactions of different forms of glyceraldehyde-3-phosphate dehydrogenase with the chaperonin {Hsp~70}},
     journal = {Vestnik Samarskogo universiteta. Estestvennonau\v{c}na\^a seri\^a},
     pages = {213--221},
     year = {2009},
     number = {6},
     language = {ru},
     url = {http://geodesic.mathdoc.fr/item/VSGU_2009_6_a21/}
}
TY  - JOUR
AU  - M. Yu. Yazykova
AU  - E. V. Shmal'gauzen
AU  - I. N. Naletova
AU  - A. P. Pleten'
AU  - V. I. Muronets
TI  - Study of interactions of different forms of glyceraldehyde-3-phosphate dehydrogenase with the chaperonin Hsp 70
JO  - Vestnik Samarskogo universiteta. Estestvennonaučnaâ seriâ
PY  - 2009
SP  - 213
EP  - 221
IS  - 6
UR  - http://geodesic.mathdoc.fr/item/VSGU_2009_6_a21/
LA  - ru
ID  - VSGU_2009_6_a21
ER  - 
%0 Journal Article
%A M. Yu. Yazykova
%A E. V. Shmal'gauzen
%A I. N. Naletova
%A A. P. Pleten'
%A V. I. Muronets
%T Study of interactions of different forms of glyceraldehyde-3-phosphate dehydrogenase with the chaperonin Hsp 70
%J Vestnik Samarskogo universiteta. Estestvennonaučnaâ seriâ
%D 2009
%P 213-221
%N 6
%U http://geodesic.mathdoc.fr/item/VSGU_2009_6_a21/
%G ru
%F VSGU_2009_6_a21
M. Yu. Yazykova; E. V. Shmal'gauzen; I. N. Naletova; A. P. Pleten'; V. I. Muronets. Study of interactions of different forms of glyceraldehyde-3-phosphate dehydrogenase with the chaperonin Hsp 70. Vestnik Samarskogo universiteta. Estestvennonaučnaâ seriâ, no. 6 (2009), pp. 213-221. http://geodesic.mathdoc.fr/item/VSGU_2009_6_a21/

[1] Asryants R., Duszenkova I., Nagradova N. K., “Determination of Sepharose-bound protein with Coomassie brilliant blue G-250”, Analyt. Biochem., 151 (1985), 571–574 | DOI

[2] Bradford M. M., “A rapid and sensitive method of quantitation of microgram quantities of protein utilizing the principle of protein-due binding using BSA solution as the standart”, Analyt. Biochem., 72 (1976), 248–254 | DOI

[3] J. R. Burke et al., “Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH”, Nat. Med., 2(3) (1996), 347–350 | DOI

[4] Cherednikova T., Muronetz V., Nagradova N., “Study of subunit interactions in immobilized D-glyceraldehyde-3-phosphate dehydrogenase”, Biochim. Biophys. Acta, 613 (1980), 292–308 | DOI

[5] A. J. Cooper et al., “Transglutaminase-catalyzed inactivation of glyceraldehyde 3-phosphate dehydrogenase and alpha-ketoglutarate dehydrogenase complex by polyglutamine domains of pathological length”, Proc. Natl. Acad. Sci. USA, 94(23) (1997), 12604–12609 | DOI

[6] Chuang De-Maw, Hough Christopher, Senatorov Vladimir, “Glyceraldehyde-3-Phosphate Dehydrogenase Apoptosis and Neurodegenerative Diseases”, Annu. Rev. Pharmacol. Toxicol., 45 (2005), 269–290 | DOI

[7] I. V. Guzhova et al., “In vitro studies show that Hsp 70 can be released by glia and that exogenous Hsp 70 can enchance neuronal stress tolerance”, Brain Res., 914 (2001), 66–73 | DOI

[8] Naletova I. N., Muronetz V. I., Schmalhausen E. V., “Unfolded, oxidized and thermoinactivated forms of glyceraldehyde-3-phosphate dehydrogenase interact with the chaperonin GroEL in different ways”, Biochim. Biophys. Acta, 1764 (2006), 831–838 | DOI