Binding of urokinase-type plasminogen activator–plasminogen activator inhibitor-1 complex to the endocytosis receptors α2-macroglobulin receptor/low-density lipoprotein receptor-related protein and very-low- density lipoprotein receptor involves basic residues in the inhibitor

نویسندگان

  • Kees W. RODENBURG
  • Lars KJØLLER
  • Helle H. PETERSEN
  • Peter A. ANDREASEN
چکیده

Binding of urokinase-type plasminogen activator–plasminogen activator inhibitor-1 complex to the endocytosis receptors α2-macroglobulin receptor/low-density lipoprotein receptor-related protein and very-lowdensity lipoprotein receptor involves basic residues in the inhibitor Kees W. RODENBURG, Lars KJØLLER, Helle H. PETERSEN and Peter A. ANDREASEN Department of Molecular and Structural Biology, Aarhus University, 10 Gustav Wieds Vej, DK 8000 AI rhus C, Denmark

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Inhibition of plasminogen activator inhibitor-1 binding to endocytosis receptors of the low-density-lipoprotein receptor family by a peptide isolated from a phage display library.

The functions of the serpin PAI-1 (plasminogen activator inhibitor-1) are based on molecular interactions with its target proteases uPA and tPA (urokinase-type and tissue-type plasminogen activator respectively), with vitronectin and with endocytosis receptors of the low-density-lipoprotein family. Understanding the significance of these interactions would be facilitated by the ability to block...

متن کامل

Molecular dissection of ligand binding sites on the low density lipoprotein receptor-related protein.

The low density lipoprotein receptor-related protein (LRP) is a large multifunctional receptor that is involved in the cellular uptake of a number of functionally diverse ligands including apoE-rich remnant lipoproteins, lipoprotein lipase, alpha 2-macroglobulin-protease complexes, plasminogen activator-inhibitor complexes, and the active protease tissue-type plasminogen activator. Ligand bindi...

متن کامل

Analysis of a two-domain binding site for the urokinase-type plasminogen activator-plasminogen activator inhibitor-1 complex in low-density-lipoprotein-receptor-related protein.

The low-density-lipoprotein-receptor (LDLR)-related protein (LRP) is composed of several classes of domains, including complement-type repeats (CR), which occur in clusters that contain binding sites for a multitude of different ligands. Each approximately 40-residue CR domain contains three conserved disulphide linkages and an octahedral Ca(2+) cage. LRP is a scavenging receptor for ligands fr...

متن کامل

gp330 on type II pneumocytes mediates endocytosis leading to degradation of pro-urokinase, plasminogen activator inhibitor-1 and urokinase-plasminogen activator inhibitor-1 complex.

Glycoprotein 330 (gp330) is a member of a family of receptors related to the low density lipoprotein receptor (LDLR). Although several ligands have been shown to bind gp330 in solid-phase assays, the ability of gp330 to mediate ligand endocytosis has not been demonstrated. To develop a cellular model for gp330 function we screened a variety of cultured cell lines and identified several that exp...

متن کامل

The urokinase/PAI-2 complex: a new high affinity ligand for the endocytosis receptor low density lipoprotein receptor-related protein.

The efficient inactivation of urokinase plasminogen activator (uPA) by plasminogen activator inhibitor type 2 (PAI-2) at the surface of carcinoma cells is followed by rapid endocytosis of the uPA-PAI-2 complex. We now show that one pathway of this receptor-mediated endocytosis is mediated via the low density lipoprotein receptor-related protein (LRP) in prostate cancer cells. Detailed biochemic...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 1997