Identification of C3 beta chain as the human serum eosinophil cytotoxicity inhibitor

نویسندگان

  • M S Minkoff
  • W W Wong
  • D S Silberstein
چکیده

An eosinophil cytotoxicity inhibitor (ECI) was purified from serum of a human subject with severe allergic dermatitis. Molecular weight of the isolated polypeptide (75,000) and its NH2-terminal amino acid sequence identified it as the beta chain of the C3 complement component (apparently free, but perhaps attached to very small fragments of the alpha chain). Free beta chain, prepared from normal plasma by reduction of C3, inhibited both eosinophil cytotoxicity and neutrophil adherence functions, with half-maximal activity at approximately 250 ng/ml. Apparently free C3 beta chain was detected in certain human biological fluids associated with inflammation; the presence of C3 beta chain correlated with ECI activity. This evidence demonstrates a potential role for free C3 beta chain as a suppressor of eosinophil and neutrophil functions in inflammation.

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

Identification of C 3 / 3 Chain as the Human Serum Eosinophil Cytotoxicity Inhibitor

An eosinophil cytotoxicity inhibitor (ECI) was purified from serum of a human subject with severe allergic dermatitis. Molecular weight of the isolated polypeptide (75,000) and its NHzterminal amino acid sequence identified it as the 13 chain of the C3 complement component (apparently free, but perhaps attached to very small fragments of the c~ chain). Free/3 chain, prepared from normal plasma ...

متن کامل

Purification of a major serum protein of rainbow trout (Salmo gairdneri) homologous to the third component of mammalian complement.

The present paper describes the purification and characterization of a major serum protein of the rainbow trout (Salmo gairdneri) required for complement-related functions (target cell lysis and opsonization). This protein, termed C3-1, was identified as the third component (C3) of rainbow trout complement. It is homologous to component C3 of human and other mammalian complements based on its s...

متن کامل

Development of New Modified Simple Polymerase Chain Reaction and Real-time Polymerase Chain Reaction for the Identification of Iranian Brucella abortus Strains

Brucellosis is primarily a worldwide zoonotic disease caused by Brucella species. The genus Brucella contains highly infectious species that are classified as biological threat agents. In this regard, the identification of Brucella can be a time-consuming and labor-intensive process posing a real risk of laboratory-acquired infection to the laboratory staff. This stud...

متن کامل

Identification of Intracellular Sources Responsible for Endogenous Reactive Oxygen Species Formation

The endogenous reactive oxygen species ("ROS") formation is associated with many pathologic states such as inflammatory diseases, neurodegenerative diseases, brain and heart ischemic injuries, cancer, and aging. The purpose of this study was to investigate the endogenous sources for "ROS" formation in intact isolated rat hepatocytes, in particular, peroxisomal oxidases, monoamine oxidase, xanth...

متن کامل

Inactivator of the third component of complement as an inhibitor in the properdin pathway.

Evidence has been obtained that a single protein, known to modulate classical complement activation, also acts as an inhibitor in the properdin or alternate complement pathway. A highly purified inactivator of the third component of complement (C3) from human serum inhibited the proteolysis of Factor B in the properdin system (glycine-rich beta-glycoprotein) by glycine-rich beta-glycoproteinase...

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:
  • The Journal of Experimental Medicine

دوره 174  شماره 

صفحات  -

تاریخ انتشار 1991