Immunologic Studies of Water-soluble Human Amyloid Fibrils

نویسندگان

  • Edward C. Franklin
  • Mordechai Pras
چکیده

Eight preparations of soluble amyloid and degraded amyloid (DAM) were compared immunologically. Unlike amyloid fibrils, six of eight preparations of DAM proved to be relatively strong immunogens. Antisera to DAM reacted weakly or not at all with normal human serum or extracts of normal tissues, but were specifically reactive with amyloid fibrils or DAM. Comparative studies of DAM'S from eight different subjects showed some degree of cross-reactivity among them, yet demonstrated that they were not identical. Similar conclusions were obtained by quantitative precipitin and complement fixation analyses. Comparison of the amyloid fibrils with the homologous DAM by complement fixation and absorption studies demonstrated the existence in DAM of antigenic determinants that were lacking or inaccessible in the native fibrils. A search for amyloid precursors and antibodies to amyloid in the sera of 12 patients proved unsuccessful.

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

Physical, Chemical, and Ultrastructural Studies of Water-soluble Human Amyloid Fibrils

Amyloid fibrils were isolated from the tissues of nine patients with amyloidosis in a state of high purity by homogenization of the tissue followed by extraction with distilled water. Physical, chemical, and ultrastructural studies suggest that amyloid fibrils from different individuals resemble each other, but are not identical. In tissue sections as well as by negative staining of isolated fi...

متن کامل

Inhibition of Amyloid Fibrils Formation from Hen Egg White Lysozyme by Satureia Hortensis Extract and its Effect on Learning and Spatial Memory of Rats

Background & Aims: Alzheimer's disease is a neurodegenerative disorder characterized by the abnormal aggregation of amyloid-β plaques in the brain. Although several studies have been done for finding effective medicines in the treatment of this disease, a drug that inhibits amyloid β aggregation and ameliorates the disorder has not been approved so far. One important therapeutic approach is use...

متن کامل

Noncooperative dimethyl sulfoxide-induced dissection of insulin fibrils: toward soluble building blocks of amyloid.

The enormous molecular weight complicates detailed structural studies of amyloid fibrils and obscures identification of biologically active forms of protein aggregates in amyloid-related diseases. Here we show that aqueous solutions of dimethyl sulfoxide (DMSO) solubilize insulin fibrils while maintaining their beta-pleated structure. This is accompanied by a marked decrease in the fluorescence...

متن کامل

Water-soluble tripeptide Abeta (9-11) forms amyloid-like fibrils and exhibits neurotoxicity.

A water-soluble, hydrophilic tripeptide GYE, having sequence identity with the N-terminal segment of amyloid peptides Abeta(9-11), upon self-association exhibits amyloid-like fibrils and significant neurotoxicity towards the Neuro2A cell line. However, the tripeptides GFE and GWE, in which the centrally located tyrosine residue has been replaced by phenylalanine or tryptophan, fail to show amyl...

متن کامل

A short water-soluble self-assembling peptide forms amyloid-like fibrils.

A water-soluble tripeptide Val-Ile-Ala (VIA) , bearing sequence identity with the C-terminal portion of the Alzheimer Abeta-peptide (Abeta(40-42)), self-assembles, in crystalline form, to produce an intermolecularly hydrogen bonded supramolecular beta-sheet structure which self-associates to form straight, unbranched nanofibrils exhibiting amyloid-like behavior; in contrast, the synthetic tripe...

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 130  شماره 

صفحات  -

تاریخ انتشار 1969