Dr. Antonio Rusinol

Dr. Antonio Rusinol Antonio Rusinol, PhD
Associate Professor

Stanton-Gerber Hall (VA 178) Room A108
Phone: 423-439-8015

 


Education
Ph.D., 1990, National University of Tucumán, Tucumán, Argentina
B.Sc., 1983, National University of Tucumán, Tucumán, Argentina


Research Interests


My research is focused on two major areas:

A) Elucidation the molecular pathways and mechanisms of the early events of atherogenesis:  The cytotoxic effects of oxLDL have been shown to proceed through apoptotic pathways. Work reported by our group (see bellow ), and others, is consistent with the hypothesis that the induction of apoptosis by oxLDL is mediated by oxysterols. A long term goal of our laboratory is to determine whether macrophage foam cell apoptosis, induced by oxysterols, plays a significant role in atherogenesis.

B) Role of protein prenylation on traffic, function and disease: Protein prenylation can be considered as a mechanism for post-translational attachment of proteins to membranes and targeting signal for intracellular localization . All known prenylated proteins in the cell are found at least under certain conditions, bound to cellular membranes. However, although prenylation clearly mediates membrane association, other factors must determine the specificity of the subcellular localization of particular prenylated proteins since they occur in many diverse subcellular compartments. In some cases this specificity is given by secondary signals in the prenylated proteins (primary structure or additional lipid modifications) whereas in other cases it is the actual interaction with prenylation-specific receptors or protein partners that directs the final localization. The existence of such prenylation-specific binding proteins has been demonstrated by work from our laboratory (1) and work published by others. The function of such proteins is however, not clearly understood. The overall goal of our research is to determine the role of prenylation-specific binding proteins on H-ras and Prelamin A trafficking and function.

 

Selected References

1.

Identification of acidic pH-dependent ligands of pentameric C-reactive protein.

 

Hammond DJ Jr, Singh SK, Thompson JA, Beeler BW, Rusiñol AE, Pangburn MK, Potempa LA, Agrawal A.

 

J Biol Chem. 2010 Nov 12;285(46):36235-44. Epub 2010 Sep 14.

 

PMID: 20843812 [PubMed - indexed for MEDLINE]

 

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2.

Binding of the monomeric form of C-reactive protein to enzymatically-modified low-density lipoprotein: effects of phosphoethanolamine.

 

Singh SK, Suresh MV, Hammond DJ Jr, Rusiñol AE, Potempa LA, Agrawal A.

 

Clin Chim Acta. 2009 Aug;406(1-2):151-5. Epub 2009 Jun 21.

 

PMID: 19545552 [PubMed - indexed for MEDLINE] Free PMC Article

 

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3.

Phosphoethanolamine-complexed C-reactive protein: a pharmacological-like macromolecule that binds to native low-density lipoprotein in human serum.

 

Singh SK, Suresh MV, Prayther DC, Moorman JP, Rusiñol AE, Agrawal A.

 

Clin Chim Acta. 2008 Aug;394(1-2):94-8. Epub 2008 Apr 27.

 

PMID: 18486609 [PubMed - indexed for MEDLINE] Free PMC Article

 

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4.

C-reactive protein-bound enzymatically modified low-density lipoprotein does not transform macrophages into foam cells.

 

Singh SK, Suresh MV, Prayther DC, Moorman JP, Rusiñol AE, Agrawal A.

 

J Immunol. 2008 Mar 15;180(6):4316-22.

 

PMID: 18322245 [PubMed - indexed for MEDLINE] Free PMC Article

 

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5.

Involvement of xeroderma pigmentosum group A (XPA) in progeria arising from defective maturation of prelamin A.

 

Liu Y, Wang Y, Rusinol AE, Sinensky MS, Liu J, Shell SM, Zou Y.

 

FASEB J. 2008 Feb;22(2):603-11. Epub 2007 Sep 11.

 

PMID: 17848622 [PubMed - indexed for MEDLINE] Free PMC Article

 

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6.

Alterations in mitosis and cell cycle progression caused by a mutant lamin A known to accelerate human aging.

 

Dechat T, Shimi T, Adam SA, Rusinol AE, Andres DA, Spielmann HP, Sinensky MS, Goldman RD.

 

Proc Natl Acad Sci U S A. 2007 Mar 20;104(12):4955-60. Epub 2007 Mar 14.

 

PMID: 17360326 [PubMed - indexed for MEDLINE] Free PMC Article

 

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