Premium
The organization of collagen in cryofractured rabbit articular cartilage: A scanning electron microscopic study
Author(s) -
Clark John M.
Publication year - 1985
Publication title -
journal of orthopaedic research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.041
H-Index - 155
eISSN - 1554-527X
pISSN - 0736-0266
DOI - 10.1002/jor.1100030102
Subject(s) - glutaraldehyde , scanning electron microscope , cartilage , fixation (population genetics) , rabbit (cipher) , materials science , electron microscope , collagen fibril , anatomy , articular cartilage , fibril , biomedical engineering , chemistry , biophysics , pathology , osteoarthritis , composite material , biology , optics , chromatography , medicine , biochemistry , statistics , mathematics , physics , alternative medicine , gene
Abstract Adult rabbit articular cartilage was prepared for scanning electron microscopy using, in order, glutaraldehyde fixation, enzymatic removal of proteoglycan, dehydration in ethanol, cryofracture in liquid nitrogen, and criticalpoint drying. Enzymes were effective in fixed material. Fixation, cryofracture, alignment of fracture surfaces with “split lines,” and retention of subchondral bone were found to be necessary steps for the preservation of collagen detail. The fibrous framework was found to be similar to that proposed by Benninghoff and favored by more recent phase‐contrast microscopic studies. Vertical fibers extending from subchondral bone and a network of tangentially oriented superficial fibrils converge in the transitional zone. No random layer is seen. Pericellular capsules interdigitate with the vertical fibers. When cartilage is prepared in a manner that minimizes tissue damage, scanning electron microscopy provides useful, unique information.