Literature DB >> 2808365

Molecular cloning of a histidine-rich Ca2+-binding protein of sarcoplasmic reticulum that contains highly conserved repeated elements.

S L Hofmann1, J L Goldstein, K Orth, C R Moomaw, C A Slaughter, M S Brown.   

Abstract

We reported previously the purification of a 165-kDa muscle-specific protein identified by virtue of its ability to bind 125I-labeled low density lipoprotein with high affinity after sodium dodecyl sulfate-polyacrylamide gel electrophoresis (Hoffmann, S. L., Brown, M. S., Lee, E., Pathak, R. K., Anderson, R. G. W., and Goldstein, J. J. (1989) J. Biol. Chem. 264, 8260-8270). The protein is located in the lumen of the sarcoplasmic reticulum, where it has no access to plasma lipoproteins. It binds to 45Ca2+ on nitrocellulose blots and stains metachromatically blue with Stains-all, a cationic dye that stains Ca2+-binding proteins. In the current paper, we have isolated a full-length rabbit cDNA clone for the 165-kDa protein. The deduced amino acid sequence reveals a 852-amino acid protein with the following structural features: 1) an NH2-terminal 27-residue putative signal sequence; 2) a highly repetitive region containing nine nearly identical tandem repeats of 29 residues, each consisting of a histidine-rich sequence HRHRGH, a stretch of 10-11 acidic amino acids, and a sequence containing 2 serines and a threonine in a negatively charged context; 3) a 13-residue stretch of polyglutamic acid; and 4) a COOH-terminal cluster of 14 closely spaced cysteine residues with the repeating pattern of Cys-X-X-Cys suggestive of a heavy metal binding domain. Histidine, aspartic acid, and glutamic acid accounted, respectively, for 13, 12, and 19% of the amino acids. The protein does not share any significant sequence homology with the cell surface low density lipoprotein receptor. Stretches of acidic amino acids are a feature of two other luminal sarcoplasmic reticulum proteins, suggesting that these may be a general feature of luminal sarcoplasmic reticulum proteins. We suggest that the histidine-rich Ca2+-binding protein described in the current study be designated HCP. The role of HCP in Ca2+ homeostasis in the sarcoplasmic reticulum of skeletal and cardiac muscle remains to be determined.

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Year:  1989        PMID: 2808365

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  33 in total

1.  Histidine-rich calcium binding protein, a sarcoplasmic reticulum protein of striated muscle, is also abundant in arteriolar smooth muscle cells.

Authors:  R K Pathak; R G Anderson; S L Hofmann
Journal:  J Muscle Res Cell Motil       Date:  1992-06       Impact factor: 2.698

Review 2.  Intracellular organelles in the saga of Ca2+ homeostasis: different molecules for different purposes?

Authors:  Enrico Zampese; Paola Pizzo
Journal:  Cell Mol Life Sci       Date:  2011-10-04       Impact factor: 9.261

3.  Proteins in load-bearing junctions: the histidine-rich metal-binding protein of mussel byssus.

Authors:  Hua Zhao; J Herbert Waite
Journal:  Biochemistry       Date:  2006-11-28       Impact factor: 3.162

4.  Increased susceptibility to isoproterenol-induced cardiac hypertrophy and impaired weight gain in mice lacking the histidine-rich calcium-binding protein.

Authors:  Eric J Jaehnig; Analeah B Heidt; Stephanie B Greene; Ivo Cornelissen; Brian L Black
Journal:  Mol Cell Biol       Date:  2006-10-09       Impact factor: 4.272

5.  Molecular and functional analyses of aspolin, a fish-specific protein extremely rich in aspartic acid.

Authors:  Shigeharu Kinoshita; Eriko Katsumi; Hiroshi Yamamoto; Kazuharu Takeuchi; Shugo Watabe
Journal:  Mar Biotechnol (NY)       Date:  2010-09-29       Impact factor: 3.619

6.  Calcium signalling in muscle: a milestone for modulation studies.

Authors:  Eduardo Ríos
Journal:  J Physiol       Date:  2006-02-09       Impact factor: 5.182

Review 7.  Junctin - the quiet achiever.

Authors:  Angela Dulhunty; Lan Wei; Nicole Beard
Journal:  J Physiol       Date:  2009-07-01       Impact factor: 5.182

8.  Calcium binds to LipL32, a lipoprotein from pathogenic Leptospira, and modulates fibronectin binding.

Authors:  Jung-Yu Tung; Chih-Wei Yang; Shao-Wen Chou; Chien-Chih Lin; Yuh-Ju Sun
Journal:  J Biol Chem       Date:  2009-11-30       Impact factor: 5.157

9.  HRC is a direct transcriptional target of MEF2 during cardiac, skeletal, and arterial smooth muscle development in vivo.

Authors:  Joshua P Anderson; Evdokia Dodou; Analeah B Heidt; Sarah J De Val; Eric J Jaehnig; Stephanie B Greene; Eric N Olson; Brian L Black
Journal:  Mol Cell Biol       Date:  2004-05       Impact factor: 4.272

10.  Identification of the MAGE-1 gene product by monoclonal and polyclonal antibodies.

Authors:  Y T Chen; E Stockert; Y Chen; P Garin-Chesa; W J Rettig; P van der Bruggen; T Boon; L J Old
Journal:  Proc Natl Acad Sci U S A       Date:  1994-02-01       Impact factor: 11.205

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