Conformational Stability of Calreticulin

Charlotte S. Jorgensen; Christa Trandum; Nanna Larsen; L. R. Ryder; Michael Gajhede; Lars K. Skov; Peter Hojrup; Vibeke Barkholt; Gunnar Houen

doi:10.2174/0929866054696082

ISSN: 0929-8665
E-ISSN: 1875-5305

Conformational Stability of Calreticulin
Authors: Charlotte S. Jorgensen¹, Christa Trandum², Nanna Larsen³, L. R. Ryder⁴, Michael Gajhede⁵, Lars K. Skov⁶, Peter Hojrup⁷, Vibeke Barkholt⁸ and Gunnar Houen⁹
View Affiliations Hide Affiliations

¹ Department of Research and Development, Statens Serum Institut, Artillerivej 5, 2300 Copenhagen S, Denmark; ² Department of Research and Development, Statens Serum Institut, Artillerivej 5, 2300 Copenhagen S, Denmark; ³ Department of Research and Development, Statens Serum Institut, Artillerivej 5, 2300 Copenhagen S, Denmark; ⁴ Department of Research and Development, Statens Serum Institut, Artillerivej 5, 2300 Copenhagen S, Denmark; ⁵ Department of Research and Development, Statens Serum Institut, Artillerivej 5, 2300 Copenhagen S, Denmark; ⁶ Department of Research and Development, Statens Serum Institut, Artillerivej 5, 2300 Copenhagen S, Denmark; ⁷ Department of Research and Development, Statens Serum Institut, Artillerivej 5, 2300 Copenhagen S, Denmark; ⁸ Department of Research and Development, Statens Serum Institut, Artillerivej 5, 2300 Copenhagen S, Denmark; ⁹ Department of Research and Development, Statens Serum Institut, Artillerivej 5, 2300 Copenhagen S, Denmark;
Source: Protein and Peptide Letters, Volume 12, Issue 7, Oct 2005, p. 687 - 693
DOI: https://doi.org/10.2174/0929866054696082
- Available online: 01 Oct 2005

Abstract

The conformational stability of calreticulin was investigated. Apparent unfolding temperatures (Tm) increased from 31°C at pH 5 to 51°C at pH 9, but electrophoretic analysis revealed that calreticulin oligomerized instead of unfolding. Structural analyses showed that the single C-terminal α-helix was of major importance to the conformational stability of calreticulin.

Article metrics loading...

/content/journals/ppl/10.2174/0929866054696082

2005-10-01

2025-05-18

From This Site

/content/journals/ppl/10.2174/0929866054696082

dcterms_title,dcterms_subject,pub_keyword

-contentType:Contributor -contentType:Concept -contentType:Institution

10

5

Full text loading...

/content/journals/ppl/10.2174/0929866054696082

Article Type: Review Article

Keyword(s): calreticulin; conformation; heat shock protein; oligomerization; stability

Conformational Stability of Calreticulin

Abstract

From This Site

Most Read This Month

Most Cited Most Cited RSS feed

The LL-37 Antimicrobial Peptide as a Treatment for Systematic Infection of Acinetobacter baumannii in a Mouse Model

FN1 Promotes Thyroid Carcinoma Cell Proliferation and Metastasis by Activating the NF-b Pathway

Wogonin Restrains the Malignant Progression of Lung Cancer Through Modulating MMP1 and PI3K/AKT Signaling Pathway

A Temporin Derived Peptide Showing Antibacterial and Antibiofilm Activities against Staphylococcus aureus

Upregulation of Connexins in the Rat Hippocampal and Cortical Neurons Following Blockade of NMDA Receptors During Postnatal Development

Long Non-coding RNA LINC00473 Promotes Breast Cancer Progression via miR-424-5p/CCNE1 Pathway

Protease Inhibitors (PIs): Candidate Molecules for Crop Protection Formulations against Necrotrophs

Preparation of IgE Antibody and Distribution of IgE⁺ Secretory Cells in the Palatine Tonsil of Bactrian Camel

Different VH3-binding Protein A Resins Show Comparable VH3-binding Mediated Byproduct Separation Capabilities Despite Having Varied Dynamic Binding Capacities Towards A VH3 Fab

Immunogenicity and Neutralization Potential of Recombinant Chimeric Protein Comprising the Catalytic Region of Gp63 of Leishmania and LTB against Leishmania donovani