Advertisement
Letter to the Editor| Volume 50, ISSUE 1, P61-64, April 2008

Download started.

Ok

C-terminal peptide of IGFBP-3, KGRKR, prolongs the proliferative potential of basal keratinocytes

Published:July 12, 2010DOI:https://doi.org/10.1016/j.jdermsci.2007.10.005
C-terminal peptide of IGFBP-3, KGRKR, prolongs the proliferative potential of basal keratinocytes
Previous ArticlePPARγ is an important transcription factor in 1α,25-dihydroxyvitamin D3-induced involucrin expression
Next ArticlePutative progenitor/stem cells isolated from human oral mucosa are resistant to ionizing radiation
      The insulin-like growth factor-binding protein (IGFBP) family comprises six soluble proteins that bind to insulin-like growth factor (IGF) [
      • Firth S.M.
      • Baxter R.C.
      Cellular actions of the insulin-like growth factor binding proteins.
      Endocr Rev. 2002; 23: 824-854
      ,
      • Sitar T.
      • Popowicz G.M.
      • Siwanowicz I.
      • Huber R.
      • Holak T.A.
      Structural basis for the inhibition of insulin-like growth factors by insulin-like growth factor-binding proteins.
      Proc Natl Acad Sci USA. 2006; 103: 13028-13033
      ]. The co-localization of the IGFBP-3 and IGF-1 receptors in the basal and germinative layers of the epidermis suggest that IGFBP-3 plays a key role in the modulation of epidermal homeostasis [
      • Edmondson S.R.
      • Thumiger S.P.
      • Kaur P.
      • Loh B.
      • Koelmeyer R.
      • Li A.
      • Silha J.V.
      • Murphy L.J.
      • Wraight C.J.
      • Werther G.A.
      Insulin-like growth factor binding protein-3 (IGFBP-3) localizes to and modulates proliferative epidermal keratinocytes in vivo.
      Br J Dermatol. 2005; 152: 225-230
      ]. It was demonstrated that IGFBPs control the bio-availability, activity and distribution of IGF [
      • Firth S.M.
      • Baxter R.C.
      Cellular actions of the insulin-like growth factor binding proteins.
      Endocr Rev. 2002; 23: 824-854
      ]. The IGF-binding sites are found on the N- and C-terminal fragments of IGFBPs [
      • Sitar T.
      • Popowicz G.M.
      • Siwanowicz I.
      • Huber R.
      • Holak T.A.
      Structural basis for the inhibition of insulin-like growth factors by insulin-like growth factor-binding proteins.
      Proc Natl Acad Sci USA. 2006; 103: 13028-13033
      ]. Moreover, the proteolytic cleavage in these domains is believed to produce lower-affinity N- and C-terminal fragments which cannot compete with the IGF receptors for IGFs [
      • Bunn R.C.
      • Fowlkes J.L.
      Insulin-like growth factor binding protein proteolysis.
      Trends Endocrinol Metab. 2003; 14: 176-181
      ]. However, recent studies have indicated that the resulting N- and C-terminal fragments nonetheless inhibit IGF activity and have functional properties which differ from those of intact proteins. Thus, we investigated the effects of IGFBP-3 and the C-terminal portion of IGFBP-3 (KGRKR) using keratinocyte culture systems and tissue-engineered skin equivalents (SEs).

      Keywords

      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:

      Subscribe to Journal of Dermatological Science
      Already a print subscriber? Claim online access
      Already an online subscriber? Sign in
      Register: Create an account
      Institutional Access: Sign in to ScienceDirect

      References

        • Firth S.M.
        • Baxter R.C.
        Cellular actions of the insulin-like growth factor binding proteins.
        Endocr Rev. 2002; 23: 824-854
        View in Article
        • Sitar T.
        • Popowicz G.M.
        • Siwanowicz I.
        • Huber R.
        • Holak T.A.
        Structural basis for the inhibition of insulin-like growth factors by insulin-like growth factor-binding proteins.
        Proc Natl Acad Sci USA. 2006; 103: 13028-13033
        View in Article
        • Edmondson S.R.
        • Thumiger S.P.
        • Kaur P.
        • Loh B.
        • Koelmeyer R.
        • Li A.
        • Silha J.V.
        • Murphy L.J.
        • Wraight C.J.
        • Werther G.A.
        Insulin-like growth factor binding protein-3 (IGFBP-3) localizes to and modulates proliferative epidermal keratinocytes in vivo.
        Br J Dermatol. 2005; 152: 225-230
        View in Article
        • Bunn R.C.
        • Fowlkes J.L.
        Insulin-like growth factor binding protein proteolysis.
        Trends Endocrinol Metab. 2003; 14: 176-181
        View in Article
        • Auger F.A.
        • Lopez Valle C.A.
        • Guignard R.
        • Tremblay N.
        • Noel B.
        • Goulet F.
        • Germain L.
        Skin equivalent produced with human collagen.
        In Vitro Cell Dev Biol Anim. 1995; 31: 432-439
        View in Article
        • Kim D.S.
        • Cho H.J.
        • Choi H.R.
        • Kwon S.B.
        • Park K.C.
        Isolation of human epidermal stem cells by adherence and the reconstruction of skin equivalents.
        Cell Mol Life Sci. 2004; 61: 2774-2781
        View in Article
        • Bravo R.
        • Frank R.
        • Blundell P.A.
        • Macdonald-Bravo H.
        Cyclin/PCNA is the auxiliary protein of DNA polymerase-delta.
        Nature. 1987; 326: 515-517
        View in Article
        • Pellegrini G.
        • Dellambra E.
        • Golisano O.
        • Martinelli E.
        • Fantozzi I.
        • Bondanza S.
        • Ponzin D.
        • McKeon F.
        • De Luca M.
        P63 identifies keratinocyte stem cells.
        Proc Natl Acad Sci USA. 2001; 98: 3156-3161
        View in Article
        • Baxter R.C.
        Insulin-like growth factor (IGF)-binding proteins: interactions with IGFs and intrinsic bioactivities.
        Am J Physiol Endocrinol Metab. 2000; 278: E967-E979
        View in Article

      Article info

      Publication history

      Published online: July 12, 2010
      Received: June 27, 2007

      Identification

      DOI: https://doi.org/10.1016/j.jdermsci.2007.10.005

      Copyright

      © 2007 Japanese Society for Investigative Dermatology. Published by Elsevier Inc. All rights reserved.

      ScienceDirect

      Access this article on ScienceDirect

      The content on this site is intended for healthcare professionals.


      We use cookies to help provide and enhance our service and tailor content. To update your cookie settings, please visit the Cookie Preference Center for this site.
      Copyright © 2023 Elsevier Inc. except certain content provided by third parties.


      RELX