TY - JOUR

T1 - Interaction of the chaperone calreticulin with proteins and peptides of different structural classes

AU - Duus, K.

AU - Sandhu, N.

AU - Jørgensen, C. S.

AU - Hansen, P. R.

AU - Steinø, A.

AU - Thaysen-Andersen, M.

AU - Højrup, P.

AU - Houen, G.

PY - 2009/11/1

Y1 - 2009/11/1

N2 - The interaction of calreticulin with native and denatured forms and polypeptides in proteolytic digests of proteins representing structural classes of all-a-helix (hemoglobin, serum albumin), all-ß-sheet (IgG) and α-helix + ß-sheets (lysozyme, ovalbumin) was investigated. The binding of calreticulin to denatured proteins was found to depend on conformation and structural class of the protein. No interaction was observed with the native proteins, whereas binding was seen for the denatured proteins, the order of interaction, being lysozyme = IgG > ovalbumin » hemoglobin = serum albumin. Moreover, the interaction between calreticulin and the heat-denatured proteins depended on the temperature and time used for denaturation and the degree of proteolytic fragmentation. Calreticulin bound well, to peptides in proteolytic digests from protease K or chymotrypsin treatment of lysozyme, IgG and ovalbumin but weakly or not at all. to peptides in proteolytic digests of hemoglobin, and serum albumin. Synthetic peptides from lysozyme and ovalbumin confirmed binding to hydrophobic peptides from these proteins. These results show that calreticulin has the ability to interact with denatured and fragmented forms of proteins with a preference for ß-strand structure and hydrophobicity.

AB - The interaction of calreticulin with native and denatured forms and polypeptides in proteolytic digests of proteins representing structural classes of all-a-helix (hemoglobin, serum albumin), all-ß-sheet (IgG) and α-helix + ß-sheets (lysozyme, ovalbumin) was investigated. The binding of calreticulin to denatured proteins was found to depend on conformation and structural class of the protein. No interaction was observed with the native proteins, whereas binding was seen for the denatured proteins, the order of interaction, being lysozyme = IgG > ovalbumin » hemoglobin = serum albumin. Moreover, the interaction between calreticulin and the heat-denatured proteins depended on the temperature and time used for denaturation and the degree of proteolytic fragmentation. Calreticulin bound well, to peptides in proteolytic digests from protease K or chymotrypsin treatment of lysozyme, IgG and ovalbumin but weakly or not at all. to peptides in proteolytic digests of hemoglobin, and serum albumin. Synthetic peptides from lysozyme and ovalbumin confirmed binding to hydrophobic peptides from these proteins. These results show that calreticulin has the ability to interact with denatured and fragmented forms of proteins with a preference for ß-strand structure and hydrophobicity.

KW - Calreticulin

KW - Chaperone

KW - Helix, ß-

KW - Peptide specificity

KW - Sheet

KW - Structural class, α-

UR - http://www.scopus.com/inward/record.url?scp=70349937881&partnerID=8YFLogxK

U2 - 10.2174/092986609789353772

DO - 10.2174/092986609789353772

M3 - Journal article

C2 - 19594432

AN - SCOPUS:70349937881

VL - 16

SP - 1414

EP - 1423

JO - Protein and Peptide Letters

JF - Protein and Peptide Letters

SN - 0929-8665

IS - 11

ER -