Internists, Cardiologist (heart)
12 years of experience

Accepting new patients
Medical Associates Ocean Cnty
1301 Route 72 W
Ste 300
Manahawkin, NJ 08050
609-597-6513
Locations and availability (3)

Education ?

Medical School Score Rankings
Yeshiva University (1998)
  • Currently 3 of 4 apples
Top 50%

Awards & Distinctions ?

Associations
Heart Rhythm Society
American Board of Internal Medicine

Affiliations ?

Dr. Wjasow is affiliated with 7 hospitals.

Hospital Affilations

Score

Rankings

  • Virtua Memorial Hospital Of Burlington County
    Cardiology
    175 Madison Ave, Mount Holly, NJ 08060
    • Currently 4 of 4 crosses
    Top 25%
  • St. Mary Medical Center - Langhorne
    Cardiology
    1201 Langhorne Newtown Rd, Langhorne, PA 19047
    • Currently 3 of 4 crosses
    Top 50%
  • Atlanticare Regional Medical Center-City Division
    Cardiology
    1925 Pacific Ave, Atlantic City, NJ 08401
    • Currently 3 of 4 crosses
    Top 50%
  • Hahnemann University Hospital
    Cardiology
    230 N Broad St, Philadelphia, PA 19102
    • Currently 2 of 4 crosses
  • Deborah Heart & Lung Center
    Cardiology
    200 Trenton Rd, Browns Mills, NJ 08015
    • Currently 2 of 4 crosses
  • St Francis Medical Center
    Cardiology
    601 Hamilton Ave, Trenton, NJ 08629
    • Currently 1 of 4 crosses
  • Virtua Memorial Health Burlington County, Inc
  • Publications & Research

    Dr. Wjasow has contributed to 6 publications.
    Title Anaphylaxis After Low Dose Intravenous Vitamin K.
    Date June 2003
    Journal The Journal of Emergency Medicine
    Excerpt

    Over-anticoagulation from warfarin is a common occurrence, and these patients are often referred to the Emergency Department for further treatment. Unfortunately, there is little guidance in the Emergency Medicine literature for the management of such patients. The American College of Chest Physicians (ACCP) issued guidelines in 1998 that address the use of vitamin K for patients with over-anticoagulation. However, there is still debate as to the optimal dose and route of vitamin K administration. This case report describes a patient who was treated with intravenous vitamin K within the scope of these guidelines at a very low dose (1 mg) and had a fatal anaphylactic reaction. This article will further discuss this patient, the 1998 ACCP guidelines, and the data supporting the alternative of subcutaneously administered vitamin K for patients with over-anticoagulation with no active bleeding.

    Title Regulation of the P85/p110alpha Phosphatidylinositol 3'-kinase. Distinct Roles for the N-terminal and C-terminal Sh2 Domains.
    Date December 1998
    Journal The Journal of Biological Chemistry
    Excerpt

    Our previous studies on the p85/p110alpha phosphatidylinositol 3-kinase showed that the p85 regulatory subunit inhibits the p110alpha catalytic subunit, and that phosphopeptide activation of p85/p110alpha dimers reflects a disinhibition of p110alpha (Yu, J., Zhang, Y., McIlroy, J., Rordorf-Nikolic, T., Orr, G. A., and Backer, J. M. (1998) Mol. Cell. Biol. 18, 1379-1387). We now define the domains of p85 required for inhibition of p110alpha. The iSH2 domain of p85 is sufficient to bind p110alpha but does not inhibit it. Inhibition of p110alpha requires the presence of the nSH2 domain linked to the iSH2 domain. Phosphopeptides increase the activity of nSH2/iSH2-p110alpha dimers, demonstrating that the nSH2 domain mediates both inhibition of p110alpha and disinhibition by phosphopeptides. In contrast, phosphopeptides did not increase the activity of iSH2/cSH2-p110alpha dimers, or dimers composed of p110alpha and an nSH2/iSH2/cSH2 construct containing a mutant nSH2 domain. Phosphopeptide binding to the cSH2 domain increased p110alpha activity only in the context of an intact p85 containing both the nSH2 domain and residues 1-322 (the SH3, proline-rich and breakpoint cluster region-homolgy domains). These data suggest that the nSH2 domain of p85 is a direct regulator of p110alpha activity. Regulation of p110alpha by phosphopeptide binding to the cSH2 domain occurs by a mechanism that requires the additional presence of the nSH2 domain and residues 1-322 of p85.

    Title In Vitro Binding and Phosphorylation of Insulin Receptor Substrate 1 by the Insulin Receptor. Role of Interactions Mediated by the Phosphotyrosine-binding Domain and the Pleckstrin-homology Domain.
    Date May 1997
    Journal European Journal of Biochemistry / Febs
    Excerpt

    Insulin receptor substrate 1 (IRS-1) is a major substrate of the insulin receptor in most cells. The N terminus of IRS-1 contains a phosphotyrosine binding (PTB) domain and a pleckstrin homology (PH) domain, both of which have been identified as important for insulin-stimulated phosphorylation in intact cells. The PTB domain binds to a phosphorylated motif, NPEY(P)960, that is present in the juxtamembrane region of the insulin receptor. A direct interaction between the PH domain of IRS-1 and the receptor has not been demonstrated. In this study, we examine the role of the IRS-1 PTB and PH domains during IRS-1 receptor binding and IRS-1 phosphorylation in intact cells and in vitro. Abrogation of binding of the PTB domain to NPXY(P) by mutation of Tyr960 of the insulin receptor did not reduce the binding of phosphorylated IRS-1 to insulin receptors in intact cells, and had no effect on binding of insulin receptors to IRS-1 or on IRS-1 phosphorylation in vitro. We examined the phosphorylation and receptor binding of a mutant recombinant IRS-1 that lacks the N-terminal PH domain (delta PH-IRS-1). Although phosphorylation of delta PH-IRS-1 by wild-type or [Ala960]insulin receptors was similar to that of IRS-1, binding of insulin receptor to delta PH-IRS-1 was markedly reduced relative to that to IRS-1. We conclude that stable association of IRS-1 with the insulin receptor is unaffected by disruption of PTB-domain-Tyr960 interactions but requires the IRS-1 PH domain, and that efficient phosphorylation of IRS-1 in intact cells correlates with the formation of stable receptor IRS complexes.

    Title Specific Activation of P85-p110 Phosphatidylinositol 3'-kinase Stimulates Dna Synthesis by Ras- and P70 S6 Kinase-dependent Pathways.
    Date January 1997
    Journal Molecular and Cellular Biology
    Excerpt

    We have developed a polyclonal antibody that activates the heterodimeric p85-p110 phosphatidylinositol (PI) 3'-kinase in vitro and in microinjected cells. Affinity purification revealed that the activating antibody recognized the N-terminal SH2 (NSH2) domain of p85, and the antibody increased the catalytic activity of recombinant p85-p110 dimers threefold in vitro. To study the role of endogenous PI 3'-kinase in intact cells, the activating anti-NSH2 antibody was microinjected into GRC + LR73 cells, a CHO cell derivative selected for tight quiescence during serum withdrawal. Microinjection of anti-NSH2 antibodies increased bromodeoxyuridine (BrdU) incorporation fivefold in quiescent cells and enhanced the response to serum. These data reflect a specific activation of PI 3'-kinase, as the effect was blocked by coinjection of the appropriate antigen (glutathione S-transferase-NSH2 domains from p85 alpha), coinjection of inhibitory anti-p110 antibodies, or treatment of cells with wortmannin. We used the activating antibodies to study signals downstream from PI 3'-kinase. Although treatment of cells with 50 nM rapamycin only partially decreased anti-NSH2-stimulated BrdU incorporation, coinjection with an anti-p70 S6 kinase antibody effectively blocked anti-NSH2-stimulated DNA synthesis. We also found that coinjection of inhibitory anti-ras antibodies blocked both serum- and anti-NSH2-stimulated BrdU incorporation by approximately 60%, and treatment of cells with a specific inhibitor of MEK abolished antibody-stimulated BrdU incorporation. We conclude that selective activation of physiological levels of PI 3'-kinase is sufficient to stimulate DNA synthesis in quiescent cells. PI 3'-kinase-mediated DNA synthesis requires both p70 S6 kinase and the P21ras/MEK pathway.

    Title Wortmannin-sensitive Trafficking Pathways in Chinese Hamster Ovary Cells. Differential Effects on Endocytosis and Lysosomal Sorting.
    Date June 1996
    Journal The Journal of Biological Chemistry
    Excerpt

    Phosphatidylinositol (PI) 3'-kinases are a family of lipid kinases implicated in the regulation of cell growth by oncogene products and tyrosine kinase growth factor receptors. The catalytic subunit of the p85/p110 PI 3'-kinase is homologous to VPS-34, a phosphatidylinositol-specific lipid kinase involved in the sorting of newly synthesized hydrolases to the yeast vacuole. This suggests that PI 3'-kinases may play analogous roles in mammalian cells. We have measured a number of secretory and endocytic trafficking events in Chinese hamster ovary cells in the presence of wortmannin, a potent inhibitor of PI 3'-kinase. Wortmannin caused a 40-50% down-regulation of surface transferrin receptors, with a dose dependence identical to that required for maximal inhibition of the p85/p110 PI 3'-kinase in intact cells. The redistribution of transferrin receptors reflected a 60% increase in the internalization rate and a 35% decrease in the recycling rate. Experiments with fluorescent transferrin showed that entry of transferrin receptors into the recycling compartment and efflux of receptors out of the compartment were slowed by wortmannin. Wortmannin altered the morphology of the recycling compartment, which was more vesiculated than in untreated cells. Using Semliki Forest virus as a probe, we also found that delivery of the endocytosed virus to its lysosomal site of degradation was slowed by wortmannin, whereas endosomal acidification was unaffected. In contrast to these effects on endocytosis and recycling, wortmannin did not affect intracellular processing of newly synthesized viral spike proteins. Wortmannin did induce missorting of the lysosomal enzyme cathepsin D to the secretory pathway, but only at a dose 20-fold greater than that required to inhibit p85/p110 PI 3'-kinase activity or to redistribute transferrin receptors. Our data demonstrate the presence of wortmannin-sensitive enzymes at three distinct steps of the endocytic cycle in Chinese hamster ovary cells: internalization, transit from early endosomes to the recycling and degradative compartments, and transit from the recycling compartment back to the cell surface. The wortmannin-sensitive enzymes critical for endocytosis and recycling are distinct from those involved in sorting newly synthesized lysosomal enzymes.

    Title Heterotrimeric G Proteins, Vesicle Trafficking, and Cftr Cl- Channels.
    Date August 1994
    Journal The American Journal of Physiology
    Excerpt

    Previously (E.M. Schwiebert, N. Kizer, D. C. Gruenert, and B. A. Stanton, Proc. Natl. Acad. Sci. USA 89: 10623-10627, 1992), we showed that heterotrimeric G proteins regulate adenosine 3',5'-cyclic monophosphate (cAMP)-activated cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channels in human airway epithelial cells. The goal of the present study was to test the hypothesis that heterotrimeric G proteins regulate vesicle trafficking and exocytosis and that these events are critical for cAMP activation of CFTR-mediated Cl- secretion. We report that cAMP stimulates exocytosis and CFTR Cl- conductance (GCl) in normal but not in CF cells. Stimulation of the heterotrimeric G protein G alpha i-2 inhibited cAMP-activated CFTR GCl and exocytosis in normal cells. In contrast, inhibition of G alpha i-2 stimulated exocytosis and allowed cAMP to stimulate CFTR GCl in cells isolated from patients with cystic fibrosis (CF). Brefeldin A and nocodazol prevented cAMP-induced exocytosis and also blocked cAMP stimulation of CFTR GCl in normal airway epithelial cells. Our studies suggest that the heterotrimeric G protein G alpha i-2 regulates CFTR GCl in human airway epithelial cells by modulating vesicle trafficking and the delivery of CFTR Cl- channels from an intracellular vesicular pool to the plasma membrane. Inhibition of G alpha i-2 may be a useful therapeutic approach to target mutant delta F508 CFTR Cl- channels from an intracellular vesicular pool to the plasma membrane and thereby correct defective Cl- secretion in CF airway epithelial cells.


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