Literature DB >> 3652738

Amyloid fibril formation in the bovine mammary gland: an ultrastructural study.

S C Nickerson1.   

Abstract

Bovine mammary secretory tissue was examined histologically to determine the origin of amyloid fibrils and their mode of deposition. Spherical bodies of amyloid fibrils found in alveolar lumina and epithelium were closely associated with epithelial and monocytoid cells. Small bundles of parallel fibrils were observed within and between alveolar epithelial cells, and large spherical bodies occasionally developed in these positions, protruding into the luminal space. Bundles of parallel fibrils at the periphery of amyloid bodies in the alveolar lumen appeared to develop from the apical epithelial plasma membrane or in the cytoplasm just within the cell border. Bundles of parallel amyloid fibrils were also observed in slight indentations in the plasma membrane of monocytoid cells. In some cases, the point of contact between single fibrils and the plasma membrane was not discerned, and fibrils appeared continuous with the cytoplasm. The alveolar lumina appeared to be the major site of amyloid body formation. It is suggested that epithelial and monocytoid cells elaborate a soluble precursor which polymerizes into fibrils at the plasma membrane and in the peripheral cytoplasm, or is secreted by the cell and polymerizes extracellularly.

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Year:  1987        PMID: 3652738

Source DB:  PubMed          Journal:  Cytobios        ISSN: 0011-4529


  2 in total

1.  Dissociation from the oligomeric state is the rate-limiting step in fibril formation by kappa-casein.

Authors:  Heath Ecroyd; Tomas Koudelka; David C Thorn; Danielle M Williams; Glyn Devlin; Peter Hoffmann; John A Carver
Journal:  J Biol Chem       Date:  2008-02-01       Impact factor: 5.157

2.  αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide.

Authors:  Francis C Dehle; Heath Ecroyd; Ian F Musgrave; John A Carver
Journal:  Cell Stress Chaperones       Date:  2010-07-15       Impact factor: 3.667

  2 in total

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