Fibrinogen - Derived Peptide B i 91 - 42 Is

نویسندگان

  • William F. Skogen
  • Robert M. Senior
  • Gail L. Griffin
  • George D. Wilner
چکیده

The formation and degradation of fibrin play a central role in hemostasis, but other activities have been associated with fibrin(ogen)-derived peptides, which suggests that products of fibrin(ogen) turnover may be involved in infiammation and wound healing. The present study was undertaken to determine whether the plasmic fibrinogen-derived peptide B191 -42 has effects on inflammatory cells and fibroblasts (FB). B/91 -42 was found to be a potent chemotaxin for neutrophils (PMN) and FB. maximally stimulating PMN migration at iO mol/L peptide. Unlike the chemotactic factors f-Met-Leu-Phe and C5a. B$1 -42 did not induce the release of lysosomal hydrolases and superoxide anion from PMN, nor did it stimulate directed movement of monocytes (MN). These features of B$1 -42 resemble the properties of human fibrinopeptide B (hFpB). the 14residue, thrombin-cleaveable fragment that constitutes the amino terminus of Bfl1 -42. and suggested that the chemotactic effects of B$1 -42 are mediated through its

برای دانلود رایگان 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

Immunochemical Characterization of Fibrinogen , Fibrin I , and Fibrin II in Human

Arterial thrombi and atherosclerotic lesions were analyzed immunochemically and examined histologically. The extent of in vivo proteolytic cleavage of the amino-terminal end of fibrinogen by thrombin and plasmin was determined and quantitated by specific radioimmunoassays. The samples were treated with cyanogen bromide (CNBr). and the total amount of fibrinogen and fibrin-derived protein was de...

متن کامل

Immunochemical characterization of fibrinogen, fibrin I, and fibrin II in human thrombi and atherosclerotic lesions.

Arterial thrombi and atherosclerotic lesions were analyzed immunochemically and examined histologically. The extent of in vivo proteolytic cleavage of the amino-terminal end of fibrinogen by thrombin and plasmin was determined and quantitated by specific radioimmunoassays. The samples were treated with cyanogen bromide (CNBr), and the total amount of fibrinogen and fibrin-derived protein was de...

متن کامل

Optimization of a Method to Prepare Liposomes Containing HER2/Neu-Derived Peptide as a Vaccine Delivery System for Breast Cancer

The purpose of this study was to optimize a method for the encapsulation of P5 peptide, a new designed peptide containing MHC class I epitopes from rat HER2/neu protein, into liposomes as an approach for breast cancer vaccine formulation. The efficiency of liposomal encapsulation of peptides is generally low and development of an optimized method to increase encapsulation efficiency is a big ch...

متن کامل

Optimization of a Method to Prepare Liposomes Containing HER2/Neu-Derived Peptide as a Vaccine Delivery System for Breast Cancer

The purpose of this study was to optimize a method for the encapsulation of P5 peptide, a new designed peptide containing MHC class I epitopes from rat HER2/neu protein, into liposomes as an approach for breast cancer vaccine formulation. The efficiency of liposomal encapsulation of peptides is generally low and development of an optimized method to increase encapsulation efficiency is a big ch...

متن کامل

Sequence of fibrinogen proteolysis and platelet release after intrauterine infusion of hypertonic saline.

Plasma fibrinopeptide B (Bbeta1-14 or FPB) immunoreactivity was studied by radioimmunoassay in patients who received intrauterine infusion of hypertonic saline to terminate pregnancy. FPB immunoreactivity increased with thrombin treatment (TIFPB) suggesting the presence of a larger FPB-containing peptide, since purified FPB is not altered by thrombin, whereas thrombin increases the immunoreacti...

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

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2005