Open AccessCollagen fibril formation during embryogenesis.
Author(s) -
Raúl Fleischmajer,
Bjørn R. Olsen,
Rupert Timpl,
Jerome S. Perlish,
Olivia Lovelace
Publication year - 1983
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.80.11.3354
Subject(s) - fibrillogenesis , immunoelectron microscopy , fibril , protein precursor , chemistry , type i collagen , biochemistry , gel electrophoresis , collagen, type i, alpha 1 , biology , antibody , extracellular matrix , enzyme , immunology , endocrinology
Chicken embryo skin of different ages and adult skin were labeled with antibodies against the amino propeptide and carboxyl propeptide of type I collagen and processed for indirect immunoelectron microscopy by the ferritin technique. The results indicate that the formation of thin collagen fibrils involves polymerization of pN-collagen. Fibrils that are thicker than 35-40 nm do not appear to contain the amino propeptide. How fibrils increase in size is not clear, but growth may involve mechanisms such as lateral aggregation of subfibril structures or fusion of thin fibrils. Carboxyl propeptides were localized near or in contact with thin collagen fibrils, but they did not appear to be arranged in a periodic manner along the fibrils. In experiments using antibodies against the amino propeptides of type III collagen, fibrils 20-40 nm in diameter were also labeled in a periodic fashion. pN-Collagen chains were extracted from embryonic skin and identified by NaDodSO4/polyacrylamide gel electrophoresis and by immunoblotting. The presence of significant amounts of pN-collagen in skin from 10- and 12-day chicken embryos agreed well with the labeling of amino propeptides by immunoelectron microscopy. This study provides evidence for the role of the amino propeptide in collagen fibrillogenesis in embryonic skin.