The effect of heparin on structural and functional properties of low density lipoproteins

KRISKO A., Piantanida I., KVEDER M., PIFAT G., LEE A., GREILBERGER J., ...Daha Fazla

BIOPHYSICAL CHEMISTRY, cilt.119, sa.3, ss.234-239, 2006 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 119 Sayı: 3
  • Basım Tarihi: 2006
  • Doi Numarası: 10.1016/j.bpc.2005.09.011
  • Dergi Adı: BIOPHYSICAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.234-239
  • Anahtar Kelimeler: LDL, heparin, fluorescence, LDL receptor, binding, APOLIPOPROTEIN B100, RECEPTOR-BINDING, PROTEOGLYCANS, IDENTIFICATION, FIBROBLASTS, METABOLISM, OXIDATION, APO-B100, SITE, LDL
  • Akdeniz Üniversitesi Adresli: Evet

Özet

Heparin binding to human low density lipoproteins (LDL) and the effect of heparin on the ability of LDL to bind to the LDL receptor has been investigated. Emphasis has been made on the physiological conditions of temperature, pH and the ionic strength. Intrinsic fluorescence spectroscopy of LDL has been applied to follow heparin binding. Fluorescence anisotropy has been measured to describe the changes in apoB and dansyl-heparin dynamics upon binding. Eu3+-labeled LDL binding to the intact LDL receptor has been monitored by time-resolved fluorescence spectroscopy technique. We have found that heparin binds to LDL under the physiological conditions, probably by Van der Waals interactions and hydrogen bonding. Temperature seems to be the most important factor influencing the interaction. Furthermore, the presence of heparin inhibits LDL binding to the intact LDL receptor that might have consequences on the cholesterol metabolism in vivo. (C) 2005 Elsevier B.V. All rights reserved.