Scholars@Duke

• Background
• 

  Education, Training, & Certifications

  • D.Sc., University of Chile (Chile) 1973
  • B.S., University of Concepcion (Chile) 1969
• 

  Previous Appointments & Affiliations

  • Associate Professor of Pathology, Pathology, Clinical Science Departments 2006 - 2011
  • Associate Research Professor of Pathology, Pathology, Clinical Science Departments 2005 - 2006
  • Assistant Research Professor of Pathology, Pathology, Clinical Science Departments 1994 - 2005
• Research
• 

  Selected Grants

  • Modulation of Angiogenesis Via the Angiostatin Receptor awarded by National Institutes of Health 2001 - 2007
  • Fibrinolysis In Vitro And In Vivo awarded by National Institutes of Health 1995
  • Lipoprotein (A), Coagulation And Fibrinolysis awarded by National Institutes of Health 1993 - 1994
  • Biosynthesis And Secretion Of Plasminogen awarded by National Institutes of Health 1985 - 1986
• Publications & Artistic Works
• 

  Selected Publications

  • Academic Articles

    • Gonzalez-Gronow, Mario, and Salvatore Vincent Pizzo. “Physiological Roles of the Autoantibodies to the 78-Kilodalton Glucose-Regulated Protein (GRP78) in Cancer and Autoimmune Diseases.” Biomedicines 10, no. 6 (May 24, 2022). https://doi.org/10.3390/biomedicines10061222.
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    • Gonzalez-Gronow, Mario, Udhayakumar Gopal, Richard C. Austin, and Salvatore V. Pizzo. “Glucose-regulated protein (GRP78) is an important cell surface receptor for viral invasion, cancers, and neurological disorders.” Iubmb Life 73, no. 6 (June 2021): 843–54. https://doi.org/10.1002/iub.2502.
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    • Al-Hashimi, Ali A., Paul Lebeau, Fadwa Majeed, Enio Polena, Šárka Lhotak, Celeste A. F. Collins, Jehonathan H. Pinthus, et al. “Autoantibodies against the cell surface-associated chaperone GRP78 stimulate tumor growth via tissue factor.” J Biol Chem 292, no. 51 (December 22, 2017): 21180–92. https://doi.org/10.1074/jbc.M117.799908.
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    • Gonzalez-Gronow, Mario, Jenny L. Fiedler, Cristian Farias Gomez, Fang Wang, Rupa Ray, Paul D. Ferrell, and Salvatore V. Pizzo. “Myelin basic protein stimulates plasminogen activation via tissue plasminogen activator following binding to independent l-lysine-containing domains.” Biochem Biophys Res Commun 490, no. 3 (August 26, 2017): 855–60. https://doi.org/10.1016/j.bbrc.2017.06.131.
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    • Gopal, Udhayakumar, Mario Gonzalez-Gronow, and Salvatore Vincent Pizzo. “Activated α2-Macroglobulin Regulates Transcriptional Activation of c-MYC Target Genes through Cell Surface GRP78 Protein.” J Biol Chem 291, no. 20 (May 13, 2016): 10904–15. https://doi.org/10.1074/jbc.M115.708131.
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    • Tu, Yufei, Mario Gonzalez-Gronow, Anton M. Kolomeyer, Alice Cohen, Joanna Pruzon, Tatyana Milman, and David S. Chu. “Adult-Onset Ligneous Conjunctivitis with Detection of a Novel Plasminogen Gene Mutation and Anti-Plasminogen IgA Antibody: A Clinicopathologic Study and Review of Literature.” Semin Ophthalmol 31, no. 6 (2016): 526–31. https://doi.org/10.3109/08820538.2015.1005319.
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    • Al-Hashimi, Ali A., Jennifer Caldwell, Mario Gonzalez-Gronow, Salvatore V. Pizzo, Danya Aboumrad, Lindsay Pozza, Hiam Al-Bayati, et al. “Binding of anti-GRP78 autoantibodies to cell surface GRP78 increases tissue factor procoagulant activity via the release of calcium from endoplasmic reticulum stores.” J Biol Chem 290, no. 48 (November 27, 2015): 28725. https://doi.org/10.1074/jbc.A110.119107.
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    • Gonzalez-Gronow, Mario, Miguel Cuchacovich, Rina Francos, Stephanie Cuchacovich, Angel Blanco, Rodrigo Sandoval, Cristian Farias Gomez, Javier A. Valenzuela, Rupa Ray, and Salvatore V. Pizzo. “Catalytic autoantibodies against myelin basic protein (MBP) isolated from serum of autistic children impair in vitro models of synaptic plasticity in rat hippocampus.” J Neuroimmunol 287 (October 15, 2015): 1–8. https://doi.org/10.1016/j.jneuroim.2015.07.006.
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    • Gonzalez-Gronow, Mario, Cristian Farias Gomez, Gustaaf G. de Ridder, Rupa Ray, and Salvatore V. Pizzo. “Binding of tissue-type plasminogen activator to the glucose-regulated protein 78 (GRP78) modulates plasminogen activation and promotes human neuroblastoma cell proliferation in vitro.” J Biol Chem 289, no. 36 (September 5, 2014): 25166–76. https://doi.org/10.1074/jbc.M114.589341.
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    • Gonzalez-Gronow, Mario, Rupa Ray, Fang Wang, and Salvatore V. Pizzo. “The voltage-dependent anion channel (VDAC) binds tissue-type plasminogen activator and promotes activation of plasminogen on the cell surface.” J Biol Chem 288, no. 1 (January 4, 2013): 498–509. https://doi.org/10.1074/jbc.M112.412502.
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    • Selim, Maria A., James L. Burchette, Edith V. Bowers, Gustaaf G. de Ridder, Lihong Mo, Salvatore V. Pizzo, and Mario Gonzalez-Gronow. “Changes in oligosaccharide chains of autoantibodies to GRP78 expressed during progression of malignant melanoma stimulate melanoma cell growth and survival.” Melanoma Res 21, no. 4 (August 2011): 323–34. https://doi.org/10.1097/CMR.0b013e3283471042.
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    • Ridder, Gustaaf G. de, Mario Gonzalez-Gronow, Rupa Ray, and Salvatore V. Pizzo. “Autoantibodies against cell surface GRP78 promote tumor growth in a murine model of melanoma.” Melanoma Res 21, no. 1 (February 2011): 35–43. https://doi.org/10.1097/CMR.0b013e3283426805.
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    • Gonzalez-Gronow, Mario, Miguel Cuchacovich, Rina Francos, Stephanie Cuchacovich, Maria del Pilar Fernandez, Angel Blanco, Edith V. Bowers, Steven Kaczowka, and Salvatore V. Pizzo. “Antibodies against the voltage-dependent anion channel (VDAC) and its protective ligand hexokinase-I in children with autism.” J Neuroimmunol 227, no. 1–2 (October 8, 2010): 153–61. https://doi.org/10.1016/j.jneuroim.2010.06.001.
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    • Al-Hashimi, Ali A., Jennifer Caldwell, Mario Gonzalez-Gronow, Salvatore V. Pizzo, Danya Aboumrad, Lindsay Pozza, Hiam Al-Bayati, et al. “Binding of anti-GRP78 autoantibodies to cell surface GRP78 increases tissue factor procoagulant activity via the release of calcium from endoplasmic reticulum stores.” J Biol Chem 285, no. 37 (September 10, 2010): 28912–23. https://doi.org/10.1074/jbc.M110.119107.
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    • Papalas, John A., Robin T. Vollmer, Mario Gonzalez-Gronow, Salvatore V. Pizzo, James Burchette, Kenneth E. Youens, Krystal B. Johnson, and Maria A. Selim. “Patterns of GRP78 and MTJ1 expression in primary cutaneous malignant melanoma.” Mod Pathol 23, no. 1 (January 2010): 134–43. https://doi.org/10.1038/modpathol.2009.152.
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    • Gonzalez-Gronow, Mario, Maria Angelica Selim, John Papalas, and Salvatore V. Pizzo. “GRP78: a multifunctional receptor on the cell surface.” Antioxid Redox Signal 11, no. 9 (September 2009): 2299–2306. https://doi.org/10.1089/ARS.2009.2568.
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    • Gonzalez-Gronow, Mario, Steven Kaczowka, Govind Gawdi, and Salvatore V. Pizzo. “Dipeptidyl peptidase IV (DPP IV/CD26) is a cell-surface plasminogen receptor.” Front Biosci 13 (January 1, 2008): 1610–18. https://doi.org/10.2741/2785.
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    • Papalas, J., J. Turner, J. Burchette, M. Gonzalez-Gronow, and M. Selim. “GRP 78 protein expression in malignant melanoma.” Journal of Cutaneous Pathology 35, no. 1 (January 1, 2008): 135–135.
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    • Gonzalez-Gronow, Mario, Steven J. Kaczowka, Sturgis Payne, Fang Wang, Govind Gawdi, and Salvatore V. Pizzo. “Plasminogen structural domains exhibit different functions when associated with cell surface GRP78 or the voltage-dependent anion channel.” J Biol Chem 282, no. 45 (November 9, 2007): 32811–20. https://doi.org/10.1074/jbc.M703342200.
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    • Gonzalez-Gronow, Mario, Miguel Cuchacovich, Carolina Llanos, Cristian Urzua, Govind Gawdi, and Salvatore V. Pizzo. “Prostate cancer cell proliferation in vitro is modulated by antibodies against glucose-regulated protein 78 isolated from patient serum.” Cancer Res 66, no. 23 (December 1, 2006): 11424–31. https://doi.org/10.1158/0008-5472.CAN-06-1721.
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    • Mavropoulos, John C., Miguel Cuchacovich, Carolina Llanos, Juan C. Aguillón, Hector Gatica, Salvatore V. Pizzo, and Mario Gonzalez-Gronow. “Anti-tumor necrosis factor-alpha therapy augments dipeptidyl peptidase IV activity and decreases autoantibodies to GRP78/BIP and phosphoglucose isomerase in patients with rheumatoid arthritis.” J Rheumatol 32, no. 11 (November 2005): 2116–24.
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    • Wahl, Miriam L., Daniel J. Kenan, Mario Gonzalez-Gronow, and Salvatore V. Pizzo. “Angiostatin's molecular mechanism: aspects of specificity and regulation elucidated.” J Cell Biochem 96, no. 2 (October 1, 2005): 242–61. https://doi.org/10.1002/jcb.20480.
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    • Gonzalez-Gronow, Mario, Uma K. Misra, Govind Gawdi, and Salvatore V. Pizzo. “Association of plasminogen with dipeptidyl peptidase IV and Na+/H+ exchanger isoform NHE3 regulates invasion of human 1-LN prostate tumor cells.” J Biol Chem 280, no. 29 (July 22, 2005): 27173–78. https://doi.org/10.1074/jbc.M500383200.
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    • Cuchacovich, M., G. Merino, J. H. Yamamoto, F. Villarroel, T. Saavedra, S. Jofre, H. Gatica, V. Velasquez, S. V. Pizzo, and M. Gonzalez-Gronow. “Behcet's disease patients present high levels of deglycosylated anti-lipoteichoic acid IgG and high IL-8 production after lipoteichoic acid stimulation.” Clinical and Experimental Rheumatology 23, no. 4 (July 1, 2005): S27–34.
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    • Misra, Uma Kant, Mario Gonzalez-Gronow, Govind Gawdi, and Salvatore Vincent Pizzo. “The role of MTJ-1 in cell surface translocation of GRP78, a receptor for alpha 2-macroglobulin-dependent signaling.” J Immunol 174, no. 4 (February 15, 2005): 2092–97. https://doi.org/10.4049/jimmunol.174.4.2092.
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    • Gonzalez-Gronow, Mario, Hernan E. Grenett, Govind Gawdi, and Salvatore V. Pizzo. “Angiostatin directly inhibits human prostate tumor cell invasion by blocking plasminogen binding to its cellular receptor, CD26.” Exp Cell Res 303, no. 1 (February 1, 2005): 22–31. https://doi.org/10.1016/j.yexcr.2004.09.008.
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    • Cuchacovich, M., G. Merino, J. H. Yamamoto, F. Villarroel, T. Saavedra, S. Jofre, H. Gatica, V. Velasquez, S. V. Pizzo, and M. Gonzalez-Gronow. “Behçet's disease patients present high levels of deglycosylated anti-lipoteichoic acid IgG and high IL-8 production after lipoteichoic acid stimulation.” Clin Exp Rheumatol 23, no. 4 Suppl 38 (2005): S27–34.
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    • Misra, Uma Kant, Mario Gonzalez-Gronow, Govind Gawdi, Fang Wang, and Salvatore Vincent Pizzo. “A novel receptor function for the heat shock protein Grp78: silencing of Grp78 gene expression attenuates alpha2M*-induced signalling.” Cell Signal 16, no. 8 (August 2004): 929–38. https://doi.org/10.1016/j.cellsig.2004.01.003.
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    • Gonzalez-Gronow, Mario, Michael S. Hershfield, Francisco X. Arredondo-Vega, and Salvatore V. Pizzo. “Cell surface adenosine deaminase binds and stimulates plasminogen activation on 1-LN human prostate cancer cells.” J Biol Chem 279, no. 20 (May 14, 2004): 20993–98. https://doi.org/10.1074/jbc.M401023200.
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    • Gonzalez-Gronow, Mario, Theodosia Kalfa, Carrie E. Johnson, Govind Gawdi, and Salvatore V. Pizzo. “The voltage-dependent anion channel is a receptor for plasminogen kringle 5 on human endothelial cells.” J Biol Chem 278, no. 29 (July 18, 2003): 27312–18. https://doi.org/10.1074/jbc.M303172200.
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    • GONZALEZ-GRONOW, M. “The voltage-dependent anion channel is a receptor for plasminogen kringle 5 on human endothelial cells.” J Biol Chem 278 (2003): 27312–18.
    • Cuchacovich, Miguel, Héctor Gatica, Paula Vial, Jorge Yovanovich, Salvatore V. Pizzo, and Mario Gonzalez-Gronow. “Streptokinase promotes development of dipeptidyl peptidase IV (CD26) autoantibodies after fibrinolytic therapy in myocardial infarction patients.” Clin Diagn Lab Immunol 9, no. 6 (November 2002): 1253–59. https://doi.org/10.1128/cdli.9.6.1253-1259.2002.
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    • Misra, Uma K., Mario Gonzalez-Gronow, Govind Gawdi, Justin P. Hart, Carrie E. Johnson, and Salvatore V. Pizzo. “The role of Grp 78 in alpha 2-macroglobulin-induced signal transduction. Evidence from RNA interference that the low density lipoprotein receptor-related protein is associated with, but not necessary for, GRP 78-mediated signal transduction.” J Biol Chem 277, no. 44 (November 1, 2002): 42082–87. https://doi.org/10.1074/jbc.M206174200.
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    • Gonzalez-Gronow, Mario, Govind Gawdi, and Salvatore V. Pizzo. “Tissue factor is the receptor for plasminogen type 1 on 1-LN human prostate cancer cells.” Blood 99, no. 12 (June 15, 2002): 4562–67. https://doi.org/10.1182/blood.v99.12.4562.
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    • Gonzalez-Gronow, M., H. E. Grenett, M. R. Weber, G. Gawdi, and S. V. Pizzo. “Interaction of plasminogen with dipeptidyl peptidase IV initiates a signal transduction mechanism which regulates expression of matrix metalloproteinase-9 by prostate cancer cells.” Biochem J 355, no. Pt 2 (April 15, 2001): 397–407. https://doi.org/10.1042/0264-6021:3550397.
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    • Cuchacovich, M., H. Gatica, S. V. Pizzo, and M. Gonzalez-Gronow. “Characterization of human serum dipeptidyl peptidase IV (CD26) and analysis of its autoantibodies in patients with rheumatoid arthritis and other autoimmune diseases.” Clin Exp Rheumatol 19, no. 6 (2001): 673–80.
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    • Asplin, I. R., U. K. Misra, G. Gawdi, M. Gonzalez-Gronow, and S. V. Pizzo. “Selective upregulated expression of the alpha2-macroglobulin signaling receptor in highly metastatic 1-LN prostate carcinoma cells.” Arch Biochem Biophys 383, no. 1 (November 1, 2000): 135–41. https://doi.org/10.1006/abbi.2000.2052.
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    • Misra, U. K., G. Gawdi, M. Gonzalez-Gronow, and S. V. Pizzo. “Coordinate regulation of the alpha(2)-macroglobulin signaling receptor and the low density lipoprotein receptor-related protein/alpha(2)-macroglobulin receptor by insulin.” J Biol Chem 274, no. 36 (September 3, 1999): 25785–91. https://doi.org/10.1074/jbc.274.36.25785.
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    • Gonzalez-Gronow, M., M. R. Weber, and S. V. Pizzo. “Secretion of MMP-9 by 1-LN human prostate tumor cells is modulated via a signaling mechanism initiated by interaction between plasminogen carbohydrate chains and DPP IV (CD26) on the cell surface.” Faseb Journal 12, no. 8 (December 1, 1998).
    • Pizzo, S. V., U. K. Misra, M. Gonzalez-Gronow, and G. Gawdi. “Upregulation of a2m signalling receptor by insulin in macrophages.” Faseb Journal 12, no. 8 (December 1, 1998).
    • Gonzalez-Gronow, M., M. R. Weber, G. Gawdi, and S. V. Pizzo. “Dipeptidyl peptidase IV (CD26) is a receptor for streptokinase on rheumatoid synovial fibroblasts.” Fibrinolysis and Proteolysis 12, no. 3 (January 1, 1998): 129–35. https://doi.org/10.1016/S0268-9499(98)80294-4.
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    • Gonzalez-Gronow, M., M. R. Weber, T. V. Shearin, G. Gawdi, S. R. Pirie-Shepherd, and S. V. Pizzo. “Plasmin(ogen) carbohydrate chains mediate binding to dipeptidyl peptidase IV (CD 26) in rheumatoid arthritis human synovial fibroblasts.” Fibrinolysis and Proteolysis 12, no. 6 (January 1, 1998): 366–74. https://doi.org/10.1016/S0268-9499(98)80395-0.
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    • Shearin, T. V., S. V. Pizzo, and M. Gonzalez-Gronow. “Molecular abnormalities of human plasminogen isolated from synovial fluid of rheumatoid arthritis patients.” J Mol Med (Berl) 75, no. 5 (May 1997): 378–85.
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    • Misra, U. K., M. Gonzalez-Gronow, G. Gawdi, and S. V. Pizzo. “Up-regulation of the alpha2-macroglobulin signaling receptor on rheumatoid synovial fibroblasts.” J Biol Chem 272, no. 1 (January 3, 1997): 497–502. https://doi.org/10.1074/jbc.272.1.497.
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    • Gonzalez-Gronow, M., M. Cuchacovich, D. M. Grigg, and S. V. Pizzo. “Analysis of autoantibodies to plasminogen in the serum of patients with rheumatoid arthritis.” J Mol Med (Berl) 74, no. 8 (August 1996): 463–69. https://doi.org/10.1007/BF00217522.
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    • Gonzalez-Gronow, M., G. Gawdi, T. V. Shearin, S. R. Pirie-Shepherd, and S. V. Pizzo. “Plasmin(ogen) carbohydrate chains mediate binding to dipeptidyl peptidase iv (cd 26) on rheumatoid artrhitis human synovial fibroblasts.” Fibrinolysis 10, no. SUPPL. 3 (January 1, 1996): 25. https://doi.org/10.1016/s0268-9499(96)80163-9.
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    • Gonzalez-Gronow, M., T. V. Shearin, and S. V. Pizzo. “Dipeptidyl Peptidase IV(CD 26) is a Receptor for Streptokinase and Fibronectin on Rheumatoid Arthritis Human Synovial Fibroblasts.” Fibrinolysis 10, no. SUPPL. 3 (January 1, 1996): 32. https://doi.org/10.1016/s0268-9499(96)80184-6.
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    • Moser, T. L., M. S. Stack, M. Gonzalez-Gronow, and S. V. Pizzo. “Interaction of human plasminogen kringles 1-3 (angiostatin) with human umbilical vein endothelial cells (huvec): binding properties and effects on cell proliferation.” Fibrinolysis 10, no. SUPPL. 3 (January 1, 1996): 73. https://doi.org/10.1016/s0268-9499(96)80336-5.
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    • Pirie-Shepherd, S. R., R. L. Serrano, N. L. Andon, M. Gonzalez-Gronow, and S. V. Pizzo. “The role of carbohydrate in the activation of plasminogen 2 glycoforms by streptokinase.” Fibrinolysis 10, no. 1 (January 1, 1996): 49–53. https://doi.org/10.1016/S0268-9499(05)80076-1.
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    • Cuchacovich, M., H. Gatica, D. M. Grigg, S. V. Pizzo, and M. Gonzalez-Gronow. “Potential pathogenicity of deglycosylated IgG cross reactive with streptokinase and fibronectin in the serum of patients with rheumatoid arthritis.” J Rheumatol 23, no. 1 (January 1996): 44–51.
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    • Serrano, R. L., P. Rodriguez, S. V. Pizzo, and M. Gonzalez-Gronow. “ATP-regulated activity of the plasmin-streptokinase complex: a novel mechanism involving phosphorylation of streptokinase.” Biochem J 313 ( Pt 1), no. Pt 1 (January 1, 1996): 171–77. https://doi.org/10.1042/bj3130171.
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    • Gonzalez-Gronow, M., G. Gawdi, and S. V. Pizzo. “Characterization of the plasminogen receptors of normal and rheumatoid arthritis human synovial fibroblasts.” J Biol Chem 269, no. 6 (February 11, 1994): 4360–66.
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    • Gonzalez-Gronow, M., G. Gawdi, and S. V. Pizzo. “Plasminogen activation stimulates an increase in intracellular calcium in human synovial fibroblasts.” J Biol Chem 268, no. 28 (October 5, 1993): 20791–95.
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    • Gonzalez-Gronow, M., J. J. Enghild, and S. V. Pizzo. “Streptokinase and human fibronectin share a common epitope: implications for regulation of fibrinolysis and rheumatoid arthritis.” Biochim Biophys Acta 1180, no. 3 (January 22, 1993): 283–88. https://doi.org/10.1016/0925-4439(93)90051-2.
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    • Stack, M. S., S. V. Pizzo, and M. Gonzalez-Gronow. “Effect of desialylation on the biological properties of human plasminogen.” Biochem J 284 ( Pt 1), no. Pt 1 (May 15, 1992): 81–86. https://doi.org/10.1042/bj2840081.
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    • Gonzalez-Gronow, M., S. Stack, and S. V. Pizzo. “Plasmin binding to the plasminogen receptor enhances catalytic efficiency and activates the receptor for subsequent ligand binding.” Arch Biochem Biophys 286, no. 2 (May 1, 1991): 625–28. https://doi.org/10.1016/0003-9861(91)90090-6.
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    • Stack, S., M. Gonzalez-Gronow, and S. V. Pizzo. “The effect of divalent cations on the conformation and function of human plasminogen.” Arch Biochem Biophys 284, no. 1 (January 1991): 58–62. https://doi.org/10.1016/0003-9861(91)90263-i.
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    • Gonzalez-Gronow, M., H. E. Grenett, G. M. Fuller, and S. V. Pizzo. “The role of carbohydrate in the function of human plasminogen: comparison of the protein obtained from molecular cloning and expression in Escherichia coli and COS cells.” Biochim Biophys Acta 1039, no. 3 (July 6, 1990): 269–76. https://doi.org/10.1016/0167-4838(90)90259-i.
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    • Edelberg, J. M., J. J. Enghild, S. V. Pizzo, and M. Gonzalez-Gronow. “Neonatal plasminogen displays altered cell surface binding and activation kinetics. Correlation with increased glycosylation of the protein.” J Clin Invest 86, no. 1 (July 1990): 107–12. https://doi.org/10.1172/JCI114671.
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    • Stack, S., M. Gonzalez-Gronow, and S. V. Pizzo. “Regulation of plasminogen activation by components of the extracellular matrix.” Biochemistry 29, no. 20 (May 22, 1990): 4966–70. https://doi.org/10.1021/bi00472a029.
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    • Edelberg, J. M., M. Gonzalez-Gronow, and S. V. Pizzo. “Lipoprotein(a) inhibition of plasminogen activation by tissue-type plasminogen activator.” Thromb Res 57, no. 1 (January 1, 1990): 155–62. https://doi.org/10.1016/0049-3848(90)90203-o.
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    • Edelberg, J. M., M. Gonzalez-Gronow, and S. V. Pizzo. “Lipoprotein a inhibits streptokinase-mediated activation of human plasminogen.” Biochemistry 28, no. 6 (March 21, 1989): 2370–74. https://doi.org/10.1021/bi00432a004.
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    • Gonzalez-Gronow, M., J. M. Edelberg, and S. V. Pizzo. “Further characterization of the cellular plasminogen binding site: evidence that plasminogen 2 and lipoprotein a compete for the same site.” Biochemistry 28, no. 6 (March 21, 1989): 2374–77. https://doi.org/10.1021/bi00432a005.
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    • Gonzalez-Gronow, M., and K. C. Robbins. “In vitro biosynthesis of plasminogen in a cell-free system directed by mRNA fractions isolated from monkey liver.” Biochemistry 23, no. 2 (January 17, 1984): 190–96. https://doi.org/10.1021/bi00297a003.
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    • Gonzalez-Gronow, M., G. E. Siefring, and F. J. Castellino. “Mechanism of activation of human plasminogen by the activator complex, streptokinase-plasmin.” J Biol Chem 253, no. 4 (February 25, 1978): 1090–94.
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    • Gonzalez-Gronow, M., B. N. Violand, and F. J. Castellino. “Purification and some properties of the Glu- and Lys-human plasmin heavy chains.” J Biol Chem 252, no. 7 (April 10, 1977): 2175–77.
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  • Book Sections

    • Gonzalez-Gronow, Mario, and Salvatore V. Pizzo. “Interaction Between Heat Shock Proteins and Components of the Plasminogen Activator System in the Central Nervous System.” In Heat Shock Proteins in Neuroscience, 43–52. Springer International Publishing, 2019. https://doi.org/10.1007/978-3-030-24285-5_4.
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    • Gonzalez-Gronow, M., and S. V. Pizzo. “Novel Cell Surface Targets for the Plasminogen Activating System in the Brain: Implications for Human Disease.” In Cell Surface GRP78, a New Paradigm in Signal Transduction Biology, 87–98, 2018. https://doi.org/10.1016/B978-0-12-812351-5.00005-2.
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  • Conference Papers

    • Gonzalez-Aguilar, A., F. Villarroel-Espindola, J. Asenjo, R. Francos, M. Cuchacovich, I. I. Concha, M. Gonzalez-Gronow, and J. C. Slebe. “Identification of autoantibodies against fructose-1,6-bisphosphatase isolated from serum of autistic children.” In Febs Journal, 284:146–146. WILEY, 2017.
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    • Al-Hashimi, A., B. Shayegan, F. Majeed, P. F. Lebeau, J. Hoogenes, E. Polena, M. Gonzalez-Gronow, S. Pizzo, and R. C. Austin. “Contribution of Anti-GRP78 autoantibodies to prostate cancer progression through tissue factor procoagulant activity.” In Bju International, 115:85–86. WILEY-BLACKWELL, 2015.
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    • Al-Hashimi, A. A., F. Majeed, M. Gonzalez-Gronow, and R. C. Austin. “Binding of anti-GRP78 autoantibodies to cell surface GRP78 promotes cancer progression by activating tissue factor procoagulant activity.” In Thrombosis Research, 129:S158–S158. Elsevier BV, 2012. https://doi.org/10.1016/s0049-3848(12)70042-7.
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    • Austin, Richard, Mario Gonzalez-Gronow, Sarka Lhotak, Ali Al-Hashimi, Liz Crane, Anil Kapoor, and Jehonathan Pinthus. “396 PRESENCE OF GRP78 ON THE CELL SURFACE OF KIDNEY CANCER CELLS CORRELATES WITH INCREASED ANTI-GRP78 AUTOANTIBODY TITRES IN KIDNEY CANCER PATIENTS- A POTENTIAL NOVEL DIAGNOSTIC MARKER.” In Journal of Urology, Vol. 185. Ovid Technologies (Wolters Kluwer Health), 2011. https://doi.org/10.1016/j.juro.2011.02.484.
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    • Al-Hashimi, A., M. Gonzalez-Gronow, and R. C. Austin. “BINDING OF ANTI-GRP78 AUTOANTIBODIES TO CELL SURFACE GRP78 INCREASES TISSUE FACTOR PROCOAGULANT ACTIVITY VIA THE RELEASE OF CALCIUM FROM ENDOPLASMIC RETICULUM STORES.” In Canadian Journal of Cardiology, 26:99D-100D. PULSUS GROUP INC, 2010.
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    • Gonzalez-Gronow, M., S. Kaczowka, S. Payne, F. Wang, G. Gawdi, and S. Pizzo. “Plasminogen structural domains exhibit different functions when associated with cell surface GRP78 or VDAC.” In Febs Journal, 274:144–144. BLACKWELL PUBLISHING, 2007.
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    • Cuchacovich, M., J. Mavropoulos, L. Carolina, A. J. Carlos, H. Gatica, S. Pizzo, F. Sabugo, and M. Gonzalez-Gronow. “Anti-TNF-alpha therapy augments DPP IV activity and decreases autoantibodies to GRP78/BIP and phosphoglucose isomerase in the circulation of rheumatoid arthritis patients.” In Annals of the Rheumatic Diseases, 64:173–173. BMJ PUBLISHING GROUP, 2005.
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    • Pruzon, J., M. Gonzalez-Gronow, H. Mohtaseb, and D. S. Chu. “Ligneous conjunctivitis in an adult patient: A study of molecular pathophysiology and treatment options.” In Investigative Ophthalmology & Visual Science, Vol. 46. ASSOC RESEARCH VISION OPHTHALMOLOGY INC, 2005.
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    • Cuchacovich, M. T., G. Merino, T. Saavedra, J. Yamamoto, and M. Gonzalez-Gronow. “High levels of deglycosilated anti-lipoteichoic acid-IgG, and IL-8 production in Behcet's disease.” In Annals of the Rheumatic Diseases, 62:205–205. B M J PUBLISHING GROUP, 2003.
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    • Gonzalez-Gronow, M., M. R. Weber, and S. V. Pizzo. “Secretion of MMP-9 by 1-LN human prostate tumor cells is modulated via a signaling mechanism initiated by interaction between plasminogen carbohydrate chains and DPP IV (CD26) on the cell surface.” In Faseb Journal, 12:A1460–A1460. FEDERATION AMER SOC EXP BIOL, 1998.
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