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Sequential appearance of macromolecules in bone induction in the rat
Author(s) -
Hulth Anders,
Johnell Olov,
Lindberg Lisbeth,
Heinegård Dick
Publication year - 1993
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.1100110308
Subject(s) - cartilage , bone sialoprotein , biglycan , chemistry , versican , osteopontin , proteoglycan , extracellular matrix , aggrecan , matrix (chemical analysis) , microbiology and biotechnology , decorin , anatomy , osteocalcin , pathology , biochemistry , biology , immunology , medicine , alkaline phosphatase , osteoarthritis , alternative medicine , chromatography , enzyme , articular cartilage
The appearance of noncollagenous proteins and proteoglycans during induction of cartilage and bone by implanted demineralized bone powder was studied by immunohistochemistry with polyclonal antibodies. Three bone proteins (osteopontin, sialoprotein, and a 62 kDa protein) were present in the bone powder grains before implantation. They appeared to be lost slowly from the granulation tissue but reappeared when bone formation started. The raw powder also contained a cartilage protein, biglycan (S1), chondrocalcin, cartilage oligomeric matrix protein, and the large proteoglycan aggrecan. The amounts of these molecules, however, increased significantly both within and outside the grains on cartilage formation. Cartilage matrix protein (148 kDa protein) appeared sparsely. The 58 kDa protein and fibromodulin (59 kDa protein), particularly the latter, were prevalent in fibrillar bundles. Antibodies against the laminin‐staining vessel basement membranes showed an abundant occurrence of capillaries within the matrix grains in the granulation tissue and in the precartilaginous tissue. Bone powder made noninductive by 4 M guanidine HCl did not induce cartilage and did not stain for antibodies against bone proteins or for molecules restricted to cartilage.