Patents Examined by Amy DeCloux
  • Patent number: 6716974
    Abstract: This invention relates to therapeutic and diagnostic methods and compositions based on Jagged/Notch proteins and nucleic acids, and on their role in the signaling pathway relating to endothelial cell migration and/or differentiation. In addition, this invention provides a substantially purified Jagged protein, as well as a substantially purified nucleic acid or segment thereof encoding Jagged protein, or a functionally equivalent derivative, or allelic or species variant thereof. Further, this invention provides a substantially purified soluble Jagged protein and a substantially purified nucleic acid encoding same as well as a recombinant cell comprising a nucleic acid encoding a soluble Jagged protein. Soluble Jagged provides further therapeutic and diagnostic methods relating to diseases, disorders, and conditions involving Jagged/Notch signaling including, inter alia, angiogenesis, differentiation, and control of gene expression.
    Type: Grant
    Filed: May 24, 2000
    Date of Patent: April 6, 2004
    Assignee: Maine Medical Center Research Institute
    Inventors: Thomas Maciag, Ann B. Zimrin, Deena J. Small, Igor A. Prudovsky
  • Patent number: 6709864
    Abstract: A composition which comprises human mesenchymal stem cells which have the potential to differentiate into cells of more than one connective tissue type and a composition which induces cells from the mesenchymal stem cell population to differentiate into the adipogenic lineage, and a process for inducing such differentiation. The composition for inducing such differentiation comprises a glucocorticoid, a compound which stimulates cAMP production or inhibits cAMP degradation (such as a phosphodiesterase inhibitor), and/or a compound which upregulates peroxisome proliferator activated receptor &ggr; (PPAR &ggr;) expression and/or increases its binding affinity to its DNA binding site. The process can further include isolating the adipocytes from remaining hMSCs.
    Type: Grant
    Filed: March 28, 2000
    Date of Patent: March 23, 2004
    Assignee: Osiris Therapeutics, Inc.
    Inventors: Mark F. Pittenger, Stephen C. Beck
  • Patent number: 6624295
    Abstract: The invention provides for the isolation, identification, synthesis, expression and purification of antibodies reactive with factor IX (FIX)/factor IXa (IXa). In particular aspects, the invention provides human antibodies reactive with the human FIX Gla domain. The invention further provides compositions especially pharmaceutical compositions, articles of manufacture, and methods of inhibiting the activation of-FIX and inhibiting FIX/IXa dependent coagulation.
    Type: Grant
    Filed: August 26, 1999
    Date of Patent: September 23, 2003
    Assignee: Genentech, Inc.
    Inventors: Camellia W. Adams, Brigitte Devaux, Dan L. Eaton, Philip E. Hass, J. Kevin Judice, Daniel Kirchhofer, Shelley Suggett
  • Patent number: 6610501
    Abstract: The present invention provides a porcine antigen that binds to human xenoreactive antibodies. The porcine antigen differs from the known porcine xenoantigens in that the antigen does not include an &agr;Gal epitope. The present invention also provides methods to purify the porcine antigen of the invention, as well as agents that bind to the antigen. The antigen may be used to generate antibodies against the antigen. The antigen is useful for detecting the presence of human xenoreactive antibodies against the antigen in blood and blood compositions, and antibodies against the antigen may be used to detect the presence of the antigen in samples. The invention also provides methods and pharmaceutical compositions for reducing a host rejection response to a porcine xenograft. Finally, a method to treat human blood or blood-derived compositions to reduce the level of human xenoantibodies is disclosed.
    Type: Grant
    Filed: January 2, 2001
    Date of Patent: August 26, 2003
    Assignee: New York Blood Center, Inc.
    Inventor: Alex Zhu
  • Patent number: 6608030
    Abstract: Methods and products for suppressing a class II MHC-restricted immune response in a mammal, or in mammalian cells, are described. The methods depend upon inhibiting invariant chain proteolysis by cathepsin S from class II MHC/invariant chain complexes, thereby reducing the competency of Class II MHC molecules for binding antigenic peptides, reducing presentation of antigenic peptides by class II MHC molecules, and suppressing immune responses. The methods may be employed in the treatment of autoimmune diseases, allergic responses, and organ or tissue graft rejection. Pharmaceutical and therapeutic compositions which are peptide-based inhibitors of cathepsin S are also described.
    Type: Grant
    Filed: May 19, 1999
    Date of Patent: August 19, 2003
    Assignee: Brigham & Women's Hospital, Inc.
    Inventors: Hidde L. Ploegh, Harold A. Chapman, Richard J. Riese, Paula R. Bryant, Matthew S. Bogyo
  • Patent number: 6605277
    Abstract: The present invention is directed to antibodies and antibody fragments that bind specifically to the active conformation of human von Willebrand factor. Most preferred are recombinantly produced single chain variable immunoglobulin fragments. Because the antibodies or antibody fragments act only at the sites of thrombus formation and do not interfere with the normal activity of circulating platelets, they are particularly well suited for use as antithrombotic agents in a wide variety of applications.
    Type: Grant
    Filed: April 6, 2001
    Date of Patent: August 12, 2003
    Assignee: The Brigham and Women's Hospital, Inc.
    Inventors: Robert I. Handin, Huabing Yuan, Anne McLeod
  • Patent number: 6605711
    Abstract: The invention relates to variant peptides which bind to HLA molecules, leading to lysis of cells via cytolytic T cell lines. The variants are based upon NY-ESO-1 peptides. The peptides can be incorporated into immune tetramers, which are useful as T cell sorters.
    Type: Grant
    Filed: September 29, 2000
    Date of Patent: August 12, 2003
    Assignee: Ludwig Institute for Cancer Research
    Inventors: Danila Valmori, Jean-Charles Cerottini, Pedro Romero
  • Patent number: 6565848
    Abstract: The present invention relates to molecules involved in cell-cell interactions in the immune system. In particular, the invention relates to a cell surface protein which contains certain classical cadherin characteristics, but it exhibits an apical distribution pattern on the surface of lymphocytes. The membrane location of this molecule correlates with the contact interface between T and B cells, and antibodies against an extracellular domain of this protein disrupt T cell/B cell interactions.
    Type: Grant
    Filed: April 11, 2000
    Date of Patent: May 20, 2003
    Assignee: The Board of Trustees of the Leland Stanford Junior University
    Inventors: Peter S. Lu, Mark M. Davis
  • Patent number: 6562943
    Abstract: The invention provides methods for identifying peptide epitopes that activate CD4+ T cells involved in the pathogenesis of diseases, e.g., autoimmune diseases, susceptibility to which is determined by expression of particular class II MHC genes. The invention includes peptides derived from the IA-2 polypeptide by such a method, altered peptide ligands, and methods of therapy involving the use of altered peptide ligands.
    Type: Grant
    Filed: April 20, 2000
    Date of Patent: May 13, 2003
    Assignees: Zycos, Inc., King's College London
    Inventors: Mark Peakman, Roman M. Chicz
  • Patent number: 6562950
    Abstract: A monoclonal antibody elicited by a heparanase protein or an immunogenical portion thereof, the monoclonal antibody specifically inhibits heparanase activity.
    Type: Grant
    Filed: November 4, 1998
    Date of Patent: May 13, 2003
    Assignees: Insight Strategy & Marketing Ltd., Hadasit Medical Research Services and Development Ltd.
    Inventors: Tuvia Peretz, Daphna Miron, Yinon Shlomi, Iris Pecker, Maty Ayal-Hershkovitz, Israel Vlodavsky, Yael Friedmann
  • Patent number: 6537551
    Abstract: The present invention relates to an anti-tumor agent comprising Salmosin which is a novel disintegrin containing Arg-Gly-Asp (RGD) sequence and derived from venom of Korean snake, Agkistrodon halys brevicaudus, as an active ingredient. Salmosin is a disintegrin which blocks the function of &agr;v&bgr;3 integrin and strongly inhibits tumor angiogenesis, tumor metastasis as well as growth of solid tumor. Salmosin does not exhibit cytotoxicity within an effective dose range where tumor growth is efficiently suppressed without any untoward effect on preexisting blood vessels and normal angiogenesis. Accordingly, Salmosin can be applied for the development of potent anti-tumor drugs which are effective for various types of cancers.
    Type: Grant
    Filed: February 2, 2001
    Date of Patent: March 25, 2003
    Inventors: Doo-Sik Kim, Kwang Hoe Chung, In-Cheol Kang
  • Patent number: 6531129
    Abstract: A variety of heparanase specific molecular probes which can be used for research and medical applications including diagnosis and therapy are disclosed. Specific applications include the use of a heparanase specific molecular probe for detection of the presence, absence or level of heparanase expression; the use of a heparanase specific molecular probe for therapy of a condition associated with expression of heparanase; the use of a heparanase specific molecular probe for quantification of heparanase in a body fluid; the use of a heparanase specific molecular probe for targeted drug delivery; and, the use of a heparanase specific molecular probe as a therapeutic agent.
    Type: Grant
    Filed: June 1, 1999
    Date of Patent: March 11, 2003
    Assignees: Insight Strategy & Marketing Ltd., Hadasit Medical Research Services and Development Ltd.
    Inventors: Iris Pecker, Israel Vlodavsky, Yael Friedman, Tuvia Perets
  • Patent number: 6514938
    Abstract: The present invention provides molecular weight markers for accurate determination of the molecular weight of glatiramer acetate and other copolymers. The present invention further provides a plurality of molecular weight markers for determining the molecular weight of glatiramer acetate and other copolymers which display linear relationships between molar ellipticity and molecular weight, and between retention time and the log of the molecular weight. The molecular weight markers also optimally demonstrate biological activity similar to glatiramer acetate or corresponding copolymers and can be used for treating or preventing various immune diseases. In addition, the subject invention provides pharmaceutical compositions for the treatment of immune diseases comprising a polypeptide having an identified molecular weight and an amino acid composition corresponding to glatiramer acetate or a terpolymer.
    Type: Grant
    Filed: September 24, 1999
    Date of Patent: February 4, 2003
    Assignee: Yeda Research and Development Co. Ltd. at the Weizmann Institute of Science
    Inventors: Alexander Gad, Dora Lis
  • Patent number: 6479245
    Abstract: A monoclonal antibody has been developed which only specifically binds activated factor VII, and not factor VII, and which does not bind to an activated factor VII which is complexed with antithrombin III. This monoclonal antibody is isolated from the hybridoma cell line DSM ACC 2332. It can be used for qualitatively and quantitatively detecting factor VIIa in body fluids, blood coagulation preparations or the intermediate stages in the production of these preparations, on cell surfaces or in tissues, and can also be used as a humanized monoclonal antibody in therapeutic preparations.
    Type: Grant
    Filed: January 21, 1999
    Date of Patent: November 12, 2002
    Assignee: Aventis Behring GmbH
    Inventors: Jürgen Römisch, Wiegand Lang, Annette Feussner, Joachim Röder
  • Patent number: 6476211
    Abstract: The invention provides polynucleotides isolated from cDNA libraries of human fetal liver-spleen and macrophage as well as polypeptides encoded by these polynucleotides and mutants or variants thereof. The polypeptides correspond to a human CD39-like protein. Other aspects of the invention include vectors containing polynucleotides of the invention and related host cells as well a processes for producing CD39-like polypeptides, and antibodies specific for such polypeptides.
    Type: Grant
    Filed: April 25, 2000
    Date of Patent: November 5, 2002
    Assignee: Hyseq, Inc.
    Inventors: John Ford, Julio J. Mulero, George Yeung
  • Patent number: 6475749
    Abstract: Rh antibody hybrids for use in testing red blood cells for the presence of one or more Rh factors. The Rh hybrid antibody may also be used in therapeutic procedures which require the use of Rh antisera. The hybrid antibody includes an IgG anti-Rh antibody which has a polymeric tailpiece attached to the carboxy terminal end of each of the IgG antibody heavy chains. A hemagglutinin method is provided for Rh phenotyping in which agglutination of Rh-positive red blood cells is achieved in a one-step process involving addition of the hybrid Rh antisera to the red blood cells being tested.
    Type: Grant
    Filed: August 11, 1999
    Date of Patent: November 5, 2002
    Assignee: The Regents of the University of California
    Inventors: Sherie L. Morrison, Ramon Montaño
  • Patent number: 6461865
    Abstract: The invention relates to calreticulin-deficient cells. The cells can be either homozygous or heterozygous for the calreticulin mutation.
    Type: Grant
    Filed: April 23, 1998
    Date of Patent: October 8, 2002
    Inventors: Shoukat Dedhar, Rene St-Arnaud
  • Patent number: 6458767
    Abstract: The present invention provides a method of treating kidney or renal diseases/conditions in a subject by administering to the subject a pharmaceutically effective amount of a purified LAP peptide, a TSP-1 type 1 repeat peptide, or a fragment thereof to interfere with the activation process of TGF-&bgr; by thrombospondin-1 to reduce and/or prevent renal damage. The present invention further provides a method of improving renal function in a subject having impaired renal function by administering to the subject a pharmaceutically effective amount of a purified LAP peptide, a TSP-1 type 1 repeat peptide, or a fragment thereof.
    Type: Grant
    Filed: May 28, 1999
    Date of Patent: October 1, 2002
    Assignee: The UAB Research Foundation
    Inventors: Joanne E. Murphy-Ullrich, Solange M. F. Ribeiro, Christian Hugo, David D. Roberts, Henry C. Krutzsch
  • Patent number: 6455046
    Abstract: The invention provides a method of enhancing an immune response to an immunogen in an animal. The method comprises administering to the animal an effective amount of the immunogen and an effective amount of a modified C-reactive protein (mCRP) or a mutant-mCRP. The invention also provides a vaccine and a method of producing this vaccine. The vaccine comprises an immunogen and an mCRP or a mutant-mCRP in a pharmaceutically-acceptable vehicle. The invention further provides a kit for immunizing an animal to an immunogen comprising (1) a container holding the immunogen and a container holding an mCRP or a mutant-mCRP or (2) a container holding the immunogen and an mCRP or a mutant-mCRP. The invention also provides a method of elicing an immune response to a hapten in an animal. The method comprises administering to the animal an effective amount of the hapten in association with an an effective amount of an mCRP or a mutant-mCRP. The invention further provides a vaccine and a method of producing this vaccine.
    Type: Grant
    Filed: May 9, 2000
    Date of Patent: September 24, 2002
    Assignee: Immtech International, Inc.
    Inventors: Lawrence A. Potempa, James A. Radosevich
  • Patent number: 6451314
    Abstract: The present invention is directed to complexes consisting essentially of an isolated MHC component and an autoantigenic peptide associated with the antigen binding site of the MHC component. These complexes are useful in treating autoimmune disease.
    Type: Grant
    Filed: June 23, 2000
    Date of Patent: September 17, 2002
    Assignee: Anergen, Inc.
    Inventors: Brian R. Clark, Somesh D. Sharma, Bernard L. Lerch