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

K. Duus; N. Sandhu; C. S. Jørgensen; P. R. Hansen; A. Steinø; M. Thaysen-Andersen; P. Højrup; G. Houen

doi:10.2174/092986609789353772

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

K. Duus, N. Sandhu, C. S. Jørgensen, P. R. Hansen, A. Steinø, M. Thaysen-Andersen, P. Højrup, G. Houen^*

^*Corresponding author for this work

8 Citations (Scopus)

Abstract

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.

Original language	English
Journal	Protein and Peptide Letters
Volume	16
Issue number	11
Pages (from-to)	1414-1423
Number of pages	10
ISSN	0929-8665
DOIs	https://doi.org/10.2174/092986609789353772
Publication status	Published - 1 Nov 2009

Keywords

Calreticulin
Chaperone
Helix, ß-
Peptide specificity
Sheet
Structural class, α-

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10.2174/092986609789353772

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title = "Interaction of the chaperone calreticulin with proteins and peptides of different structural classes",

abstract = "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.",

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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.

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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.

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KW - Chaperone

KW - Helix, ß-

KW - Peptide specificity

KW - Sheet

KW - Structural class, α-

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

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