Basic science| Volume 64, ISSUE 2, P399-404, August 2004

Comparison of gene expression profiles between Peyronie's disease and Dupuytren's contracture

  • A Qian
    Harbor-UCLA Research and Education Institute, Torrance, California, USA
    Search for articles by this author
  • R.A Meals
    Department of Orthopedics, University of California, Los Angeles, School of Medicine, Los Angeles, California, USA
    Search for articles by this author
  • J Rajfer
    Harbor-UCLA Research and Education Institute, Torrance, California, USA

    Department of Urology, University of California, Los Angeles, School of Medicine, Los Angeles, California, USA
    Search for articles by this author
  • N.F Gonzalez-Cadavid
    Reprint requests: Nestor F. Gonzalez-Cadavid, Ph.D., Department of Urology, Harbor-UCLA Research and Education Institute, Building F-6, 1124 West Carson Street, Torrance, CA 90502, USA
    Harbor-UCLA Research and Education Institute, Torrance, California, USA

    Department of Urology, University of California, Los Angeles, School of Medicine, Los Angeles, California, USA
    Search for articles by this author



      To compare the gene expression alterations in human Peyronie's disease (PD) and Dupuytren's disease (DD) to determine whether they share a common pathophysiology. Multiple mRNA expression profiles of human PD have previously shown that genes that regulate fibroblast replication, myofibroblast differentiation, collagen metabolism, tissue repair, and ossification are involved. DD, a palmar fascia fibrosis, may be associated with PD.


      Total RNA samples from PD plaques, normal tunica albuginea, Dupuytren's nodules, and normal palmar fascia (nine samples per group) were subjected to differential gene expression profile analysis (Clontech Atlas DNA microarray) comparing PD with tunica albuginea and DD with normal palmar fascia. Changes of more than 2.0 in PD and DD compared with tunica albuginea and normal palmar fascia, respectively, were recorded. Reverse transcriptase-polymerase chain reactions were performed for some genes whose expression was altered in PD.


      Some of the gene families upregulated in both PD and DD were (a) collagen degradation: matrix metalloproteinase (MMP), with MMP2 and MMP9, and thymosins (MMP activators), with TMβ10 and TMβ4; (b) ossification: osteoblast-specific factors (OSFs) OSF-1 and OSF-2 (DD only); and (c) myofibroblast differentiation: RhoGDP dissociation inhibitor 1. The genes upregulated in PD only were decorin (an inhibitor of transforming growth factor-beta1 and a part of fibroblast replication/collagen synthesis) and early growth response protein. Reverse transcriptase-polymerase chain reaction confirmed these changes.


      These data demonstrate that the pattern of alterations in the expression of certain gene families in PD and DD is similar, suggesting that they share a common pathophysiology and may be amenable to the same therapeutic regimens.
      To read this article in full you will need to make a payment

      Purchase one-time access:

      Academic & Personal: 24 hour online accessCorporate R&D Professionals: 24 hour online access
      One-time access price info
      • For academic or personal research use, select 'Academic and Personal'
      • For corporate R&D use, select 'Corporate R&D Professionals'


      Subscribe to Urology
      Already a print subscriber? Claim online access
      Already an online subscriber? Sign in
      Institutional Access: Sign in to ScienceDirect


        • Gholami S.S.
        • Gonzalez-Cadavid N.F.
        • Lin C.-S.
        • et al.
        Peyronie's disease.
        J Urol. 2002; 169: 1234-1241
        • Somers K.D.
        • Dawson D.M.
        Fibrin deposition in Peyronie's disease plaque.
        J Urol. 1997; 157: 311-315
        • Davila H.
        • Ferrini M.
        • Rajfer J.
        • et al.
        Fibrin induction of a Peyronie's-like plaque in the rat penile tunica albuginea.
        Br J Urol. 2003; 91: 830-838
        • Ferrini M.G.
        • Vernet D.
        • Magee T.R.
        • et al.
        Antifibrotic role of inducible nitric oxide synthase (iNOS).
        Nitric Oxide. 2002; 6: 1-12
        • Vernet D.
        • Ferrini M.G.
        • Valente E.
        • et al.
        Effect of nitric oxide on fibroblast differentiation into myofibroblasts in cell cultures from the Peyronie's fibrotic plaque and in its rat model in vivo.
        Nitric Oxide. 2002; 7: 262-276
        • Mulhall J.P.
        Expanding the paradigm for plaque development in Peyronie's disease.
        Int J Impot Res. 2003; 15: S93-S102
        • Powell D.W.
        • Mifflin R.C.
        • Valentich J.D.
        • et al.
        Myofibroblasts. I. Paracrine cells important in health and disease.
        Am J Physiol. 1999; 277: C1-C9
        • Valente E.G.
        • Ferrini M.G.
        • Vernet D.
        • et al.
        PDE l-arginine and PDE inhibitors counteract fibrosis in the Peyronie's fibrotic plaque and related fibroblast cultures.
        Nitric Oxide. 2003; 9: 229-244
        • Fitzgerald A.M.
        • Kirkpatrick J.J.
        • Naylor I.L.
        Dupuytren's disease.
        J Hand Surg [Br]. 1999; 24: 395-399
        • Carrieri M.P.
        • Serraino D.
        • Palmiotto F.
        • et al.
        A case-control study on risk factors for Peyronie's disease.
        J Clin Epidemiol. 1998; 51: 511-515
        • Tomasek J.J.
        • Vaughan M.B.
        • Haaksma C.J.
        Cellular structure and biology of Dupuytren's disease.
        Hand Clin. 1999; 15: 21-34
        • Forster T.
        • Roy D.
        • Ghazal P.
        Experiments using microarray technology.
        J Endocrinol. 2003; 178: 195-204
        • Magee T.R.
        • Qian A.
        • Rajfer J.
        • et al.
        Gene expression profiles in the Peyronie's disease plaque.
        Urology. 2002; 59: 451-457
        • Ravanti L.
        • Kahari V.M.
        Matrix metalloproteinases in wound repair.
        Int J Mol Med. 2000; 6: 391-407
        • Huff T.
        • Muller C.S.
        • Otto A.M.
        • et al.
        Beta-thymosins, small acidic peptides with multiple functions.
        Int J Biochem Cell Biol. 2001; 33: 205-220
        • Philp D.
        • Badamchian M.
        • Scheremeta B.
        • et al.
        Thymosin beta 4 and a synthetic peptide containing its actin-binding domain promote dermal wound repair in db/db diabetic mice and in aged mice.
        Wound Repair Regen. 2003; 11: 19-24
        • May R.C.
        The Arp2/3 complex.
        Cell Mol Life Sci. 2001; 58: 1607-1626
        • Olofsson B.
        Rho guanine dissociation inhibitors.
        Cell Signal. 1999; 11: 545-554
        • Tare R.S.
        • Oreffo R.O.
        • Clarke N.M.
        • et al.
        Pleiotrophin/osteoblast-stimulating factor 1.
        J Bone Miner Res. 2002; 17: 2009-2020
        • Gordeladze J.O.
        • Drevon C.A.
        • Syversen U.
        • et al.
        Leptin stimulates human osteoblastic cell proliferation, de novo collagen synthesis, and mineralization.
        J Cell Biochem. 2002; 85: 825-836
        • Hashimoto Y.
        • Niikura T.
        • Chiba T.
        • et al.
        The cytoplasmic domain of Alzheimer's amyloid-beta protein precursor causes sustained apoptosis signal-regulating kinase 1/c-Jun NH2-terminal kinase-mediated neurotoxic signal via dimerization.
        J Pharmacol Exp Ther. 2003; 306: 889-902
        • Nishimura I.
        • Takazaki R.
        • Kuwako K.
        • et al.
        Upregulation and antiapoptotic role of endogenous Alzheimer amyloid precursor protein in dorsal root ganglion neurons.
        Exp Cell Res. 2003; 286: 241-251
        • Teruyama K.
        • Abe M.
        • Nakano T.
        • et al.
        Role of transcription factor Ets-1 in the apoptosis of human vascular endothelial cells.
        J Cell Physiol. 2001; 188: 243-252
        • Lee J.C.
        • Peter M.E.
        Regulation of apoptosis by ubiquitination.
        Immunol Rev. 2003; 193: 39-47
        • Lenda D.M.
        • Kikawada E.
        • Stanley E.R.
        • et al.
        Reduced macrophage recruitment, proliferation, and activation in colony-stimulating factor-1-deficient mice results in decreased tubular apoptosis during renal inflammation.
        J Immunol. 2003; 170: 3254-3262
        • Angel P.
        • Szabowski A.
        Function of AP-1 target genes in mesenchymal-epithelial cross-talk in skin.
        Biochem Pharmacol. 2002; 64: 949-956
        • Reed C.C.
        • Iozzo R.V.
        The role of decorin in collagen fibrillogenesis and skin homeostasis.
        Glycoconj J. 2002; 19: 249-255
        • Kaufmann A.
        • Salentin R.
        • Meyer R.G.
        • et al.
        Defense against influenza A virus infection.
        Immunobiology. 2001; 204: 603-613
        • Forbes J.M.
        • Thallas V.
        • Thomas M.C.
        • et al.
        The breakdown of preexisting advanced glycation end products is associated with reduced renal fibrosis in experimental diabetes.
        FASEB J. 2003; 17: 1762-1764
        • Gabbiani G.
        The myofibroblast in wound healing and fibrocontractive diseases.
        J Pathol. 2003; 200: 500-503
        • Mills T.M.
        • Chitaley K.
        • Lewis R.W.
        • et al.
        Nitric oxide inhibits RhoA/Rho-kinase signaling to cause penile erection.
        Eur J Pharmacol. 2002; 439: 173-174
        • Barnham K.J.
        • McKinstry W.J.
        • Multhaup G.
        • et al.
        Structure of the Alzheimer's disease amyloid precursor protein copper binding domain.
        J Biol Chem. 2003; 278: 17401-17407