Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Review: History of the amyloid fibril
Autore:
Sipe, JD; Cohen, AS;
Indirizzi:
NIH, Ctr Sci Review, Bethesda, MD 20892 USA NIH Bethesda MD USA 20892NIH, Ctr Sci Review, Bethesda, MD 20892 USA Boston Univ, Sch Med, Amyloid Program, Boston, MA 02118 USA Boston Univ Boston MA USA 02118 ed, Amyloid Program, Boston, MA 02118 USA
Titolo Testata:
JOURNAL OF STRUCTURAL BIOLOGY
fascicolo: 2-3, volume: 130, anno: 2000,
pagine: 88 - 98
SICI:
1047-8477(200006)130:2-3<88:RHOTAF>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNOGLOBULIN LIGHT CHAINS; ALZHEIMERS-DISEASE; PRE-ALBUMIN; PROTEIN; POLYNEUROPATHY; FIBRILLOGENESIS; TRANSTHYRETIN; PROTEOGLYCANS; PRION;
Keywords:
amyloid fibril; amyloid protein; amyloidosis; electron microscopy; history;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Sipe, JD NIH, Ctr Sci Review, 6701 Rockledge Dr,Room 4106,MSC 7814, Bethesda, MD 20892 USA NIH 6701 Rockledge Dr,Room 4106,MSC 7814 Bethesda MD USA 20892 SA
Citazione:
J.D. Sipe e A.S. Cohen, "Review: History of the amyloid fibril", J STRUCT B, 130(2-3), 2000, pp. 88-98

Abstract

Rudolph Virchow, in 1854, introduced and popularized the term amyloid to denote a macroscopic tissue abnormality that exhibited a positive iodine staining reaction. Subsequent light microscopic studies with polarizing opticsdemonstrated the inherent birefringence of amyloid deposits, a property that increased intensely after staining with Congo red dye. In 1959, electronmicroscopic examination of ultrathin sections of amyloidotic tissues revealed the presence of fibrils, indeterminate in length and, invariably, 80 to100 Angstrom in width. Using the criteria of Congophilia and fibrillar morphology, 20 or more biochemically distinct forms of amyloid have been identified throughout the animal kingdom; each is specifically associated with aunique clinical syndrome. Fibrils, also 80 to 100 A in width, have been isolated from tissue homogenates using differential sedimentation or solubility. X-ray diffraction analysis revealed the fibrils to be ordered in the beta pleated sheet conformation, with the direction of the polypeptide backbone perpendicular to the fibril axis (cross beta structure). Because of the similar dimensions and tinctorial properties of the fibrils extracted from amyloid-laden tissues and amyloid fibrils in tissue sections, they have been assumed to be identical. However, the spatial relationship of proteoglycans and amyloid P component (AP), common to all forms of amyloid, to the putative protein only fibrils in tissues, has been unclear. Recently, it has been suggested that, in situ, amyloid fibrils are composed of proteoglycans and AP as well as amyloid proteins and thus resemble connective tissue microfibrils. Chemical and physical definition of the fibrils in tissues will be needed to relate the in vitro properties of amyloid protein fibrils to the pathogenesis of amyloid fibril formation in vivo. (C) 2000 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/04/20 alle ore 03:28:00