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  • Allan R. Sinning, PhD

    Sinning, AllanProfessor
    Office: 710A
    Phone: (601) 984-1651 or 984-1649
    Lab: N727: Phone: (601) 984-1661
    Fax: (601) 984-1655
    E-mail: asinning@umc.edu 


    • BS - University of Wisconsin-Platteville, 1979
    • MS - University of North Dakota, 1983
    • PhD - University of North Dakota, 1985
    • Postdoctorall fellow - Medical College of Wisconsin

    Research Interests

    The role of extracellular matrix proteins in early development


    Medical Gross Anatomy
    Fall quarter: M, T, Th, F: 1:00-5:00 PM

    Research Statement

    A critical step in early heart development is the elaboration of cardiac mesenchyme within the endocardial cushions. These cushions are located in the atrioventricular canal and proximal outflow tract and provide a framework for the elaboration of valves and for partitioning of the heart into its representative chambers. Mesenchyme formation is controlled by the secretion of a particulate form of extracellular matrix from the myocardium underlying these cushions. The particulate matrix consists of a multicomponent complex of proteins that includes fibronectin and at least 5-6 other components. The focus of my laboratory is in the isolation, purification and functional identification of these components.

    In pursuit of these proteins we have utilized lectin histochemistry and lectin affinity chromatography to isolate a group of proteins responsible for mesenchyme formation. While the molecular weight of these proteins is known, little information has been obtained as to the identity or functional role of these proteins in this process. To further characterize these proteins we have produced a series of monoclonal antibodies directed against the bound fraction from the lectin affinity column. We are currently using one of these antibodies to characterize a 283-kDa extracellular protein that is involved in this process.

    This antibody was also used to screen two cDNA expression libraries in an attempt to identify a clone for this protein. We have isolated a 500-bp fragment using this strategy. Sequence analysis of this probe revealed a unique sequence not found in the database. This probe was also used to isolate two 1-Kb fragments that are now being sequenced.

    In addition we are separating the media into components using size exclusion chromatography utilizing both low and high pressure systems so that we can test individual proteins or groups of proteins for biological activity in a bioassay of mesenchyme formation. Finally we are examining the affect of retinoic acid, a known teratogen of heart development, on the expression of this protein to determine if the defects associated with this teratogen are manifested by changes in the extracellular matrix.

    Selected Publications

    • Yan, M., Nick, T.G., and Sinning, A.R. (2000) Retinoic acid inhibition of cardiac mesenchyme formation in vitro correlates with changes in the secretion of particulate matrix from the myocardium. Anat. Rec. 258:186-197.
    • Sinning, A.R. (1998) The role of vitamin A in the formation of congenital heart defects. Anat. Rec. (New Anat.) 253:147-153
    • Smith, S.M., Dickman, E.D., Thompson, R., Sinning, A.R., Wunsch, A.M. and Markwald R.R. (1997) Retinoic acid directs cardiac laterality and the expression of early markers of precardiac asymmetry. Dev. Biol. 182:162-171
    • Sinning, A.R. (1997) Partial purification of hLAMP-1 provides direct evidence for the multi-component nature of the particulate matrix associated with cardiac mesenchyme formation. Jour. Cell. Biochem. 66:112-122.
    • Sinning, A.R. and Hewitt, C.C. (1996) Identification of a 283 kDa protein component of the particulate matrix associated with cardiac mesenchyme formation. Acta Anat., 155:219-230.
    • Sinning, A.R., Hewitt, C.C., and Markwald, R.R. (1995) A subset of SBA lectin binding proteins isolated from myocardial conditioned media transforms cardiac endothelium into mesenchyme. Acta Anat., 154:111-119.
    • Sinning, A.R., Krug, E.L. and Markwald, R.R. (1992) Multiple glycoproteins occur within a unique, particulate form of extracellular matrix expressed in regions of the embryonic heart where endothelial cells are induced to form mesenchyme. Anat. Rec., 232:285-292.
    • Markwald, R.R., Mjaatvedt, C.H., Krug, E.L., and Sinning, A.R. (1990) Endothelial formation of mesenchyme: Induction by an in vivo adheron like complex. In: Molecular Biology of the Cardiovascular System. Cetus-Upjohn UCLA symposium, Alan R. Liss. Eds. Sambrok, J. and Roberts, R. pp 311-319.
    • Markwald, R.R., Mjaatvedt, C.H., Krug, E.L., and Sinning, A.R. (1990) Inductive interactions in heart development: Role of adherons in cushion tissue formation. In: Embryonic Origins and Defective Heart Development. An. NY Acad. Sci. Vol. 588. Eds. Bockman, D.E. and Kirby, M.L. pp 13-35.
    • Sai Majji, S. LaPratra, SM Long, R. Smaple, L. Bryan, A. Sinning, VG Chinchar (2006) Rana catesbeiana virus Z (RCV-Z): A novel pathogenic rana virus. Diseases of Aquatic Organisms, 73:1-11
    • Sample RL, Bryan SL, G. Hoskins, A. Sinning, J. Olivier, and VG Chinchar (2007) Inhibition of iridovirus protein synthesis and virus replication by antisense morpholino oligonucleotides targeted to the major capsid protein the 18 kDa immediate-early protein, and a viral homolog of RNA polymerase II. Virology 358: 311-320