Fluorescent opsonization assay: binding of plasma fibronectin to fibrin-derivatized fluorescent particles does not enhance their uptake by macrophages.

نویسنده

  • D J Falcone
چکیده

A simple method for assessing the opsonic properties of plasma fibronectin is described. The method is based on the uptake of protein-derivatized fluorescent particles by mouse peritoneal macrophages. With this system, fibronectin stimulated the uptake of gelatin conjugated to carboxylated fluorescent particles. In contrast to the gelatinized particles, neither the covalent nor noncovalent interaction of fibronectin with fibrin particles stimulated their uptake by macrophages. These results provide additional evidence that fibronectin is not a conventional opsonin and that enhanced phagocytosis is not an obligatory response by macrophages to fibronectin-coated particles.

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

Uptake of toxic silica particles by isolated rat liver macrophages (Kupffer cells) is receptor mediated and can be blocked by competition.

Silica particles (quartz dust) are toxic to macrophages after their uptake into these cells. These experiments describe the opsonization mechanism(s) and macrophage receptor(s) involved in silica uptake. Freshly isolated rat liver macrophages (Kupffer cells) were incubated at 37 degrees C with silica particles in the presence or absence of autologous or heterologous plasma or purified plasma fi...

متن کامل

Fibronectin stimulates macrophage uptake of low density lipoprotein-heparin-collagen complexes.

In this study, we investigated whether fibronectin will enhance macrophage uptake of particulate complexes of low density lipoproteins (LDL), heparin, and fibrillar collagen and whether fibronectin's opsonic effect could be modulated by the heparin component in these model matrices. We isolated a heparin fraction (HepFn) based on its affinity to fibronectin. HepFn appeared more charged than unf...

متن کامل

Fibronectin dependent macrophage fibrin binding.

Plasma fibronectin has been shown to increase the binding of fibrin monomer to macrophages in vitro. In the present study we began characterization of the mechanism underlying this fibronectin activity. Fragments of fibronectin containing the amino terminus enhanced macrophage fibrin binding to the same extent as intact fibronectin on an equimolar basis. However, fibronectin fragments containin...

متن کامل

Fibronectin as an enhancer of nonopsonic phagocytosis of Pseudomonas aeruginosa by macrophages.

Fibronectin is capable of enhancing uptake by macrophages of Pseudomonas aeruginosa grown in vivo in rats or mice or in vitro on nutrient agar plates. It was demonstrated that concentrations as low as 27 nM fibronectin produced significant enhancement of macrophage phagocytosis. Washing of fibronectin-treated macrophages did not prevent phagocytosis enhancement, but washing of fibronectin-treat...

متن کامل

Biochemical characterization of PE_PGRS61 family protein of Mycobacterium tuberculosis H37Rv reveals the binding ability to fibronectin

Objective(s): The periodic binding of protein expressed by Mycobacterium tuberculosis H37Rv with the host cell receptor molecules i.e. fibronectin (Fn) is gaining significance because of its adhesive properties.  The genome sequencing of M. tuberculosis H37Rv revealed that the proline-glutamic (PE) proteins contain polymorphic GC-rich repetitive sequences (PGRS) which have clinical importance i...

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:
  • Journal of leukocyte biology

دوره 39 1  شماره 

صفحات  -

تاریخ انتشار 1986