ArticleMolecular biotechnology2009
Molecular cloning of OSP94: A significant biomarker protein of hypertensive human heart and a member of HSP110 family.
Article in Molecular biotechnology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed, 2 citations in OpenAlex.
- Phosphokinome Analysis of Barth Syndrome Lymphoblasts Identify Novel Targets in the Pathophysiology of the Disease.International journal of molecular sciences · 2018Article
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2 authors at 1 institution in 1 country.
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Abstract
Heat shock proteins (HSPs) are upregulated in response to stress and play a protective function in refolding of cellular proteins. In hypertension, the heart is a vital organ that requires examination and investigation, and primary induction of HSPs is predominantly effected. Hypertension results from osmotic imbalance during renin-angiotensin cycle inefficiency. Osmotic stress protein 94 (OSP94) is a stress protein induced upon osmotic imbalance. It is therefore necessary to analyze its precise role in the hypertensive heart. We have first reported the cloning and expression of human heart OSP94 followed by an analysis of gene sequence and protein homology. Directional cloning of OSP94 by PCR amplification yielded a 2.5 kb amplicon and was cloned into pET-15b. Site-directed mutagenesis was essentially followed. mRNA expression levels were evaluated in correlation with HSPs. Gene analysis indicated a 2520 bp sequence with an 838-amino acid protein complement. Protein homology revealed highly conserved sequence similarity among mammalian sequences. Structural predictions of OSP94 protein were also investigated. OSP94 is therefore recognized as a significant stress protein for investigations in hypertensive heart tissues and is a highly conserved protein in the HSP110 subfamily.
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