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(Circulation Research. 2005;97:961.)
© 2005 American Heart Association, Inc.

Editorials

New Function of Calreticulin

Calreticulin-Dependent mRNA Destabilization

Mitsuhiro Yokoyama, Ken-ichi Hirata

From the Division of Cardiovascular and Respiratory Medicine, Department of Internal Medicine, Kobe University Graduate School of Medicine, Japan.

Correspondence to Dr Mitsuhiro Yokoyama, MD, PhD, the Division of Cardiovascular and Respiratory Medicine, The Department of Internal Medicine, Kobe University Graduate School of Medicine, 7-5-1, Kusunoki-cho, Chuo-ku, Kobe, 650-0017 Japan. E-mail yokoyama@med.kobe-u.ac.jp

See related article, pages 1001–1008

Key Words: calreticulin • mRNA • GLUTs

An extract of the first 250 words of the full text is provided, because this article has no abstract.

	Introduction

 
Calreticulin was first identified as a Ca²⁺-binding protein of the muscle sarcoplasmic reticulum in 1974, and the DNA encoding this protein was isolated in 1989.¹ Calreticulin is a ubiquitous protein, found in a wide range of species and in all nucleated cell types, and has a variety of important biological functions. The human gene for calreticulin contains 9 exons and 8 introns. The deduced amino acid sequence indicates that calreticulin has a 17 amino acid hydrophobic signal sequence at its N terminus and that mature calreticulin contains 400 amino acids. The structure of calreticulin has been well characterized.² It has at least 3 structural and functional domains (Figure).

View larger version (7K): [in this window] [in a new window]   Structure of calreticulin protein. The Figure shows a schematic representation of the genomic configuration of domain structure of calreticulin protein. Structural predictions for calreticulin suggest that the protein has at least 3 structural and functional domains. Exons encoding the N domain (including the N-terminal signal sequence), the P domain, and the C domain of calreticulin are in blue, red, and green respectively. The N, P, and C domains are also presented in blue, red, and green. The protein contains an N-terminal amino acid signal sequence (black box) and a C-terminal KDEL ER retrieval signal. The locations of 3 cysteine residues and the disulphide bridge in the N domain of calreticulin are indicated. The arrowheads indicate the location of potential glycosylation sites (residues 162 and 327). Repeats A (amino acid sequence PXXIXDPDAXKPEDWDE) and B (amino acid sequence GXWXPPXIXNPXYX) are indicated . . . [Full Text of this Article]

Related Article:

Calreticulin Destabilizes Glucose Transporter-1 mRNA in Vascular Endothelial and Smooth Muscle Cells Under High-Glucose Conditions

Hana Totary-Jain, Tally Naveh-Many, Yael Riahi, Nurit Kaiser, Jürgen Eckel, and Shlomo Sasson
Circ. Res. 2005 97: 1001-1008. [Abstract] [Full Text] [PDF]

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