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Extracellular compartments and collagen fibrillogenesis
Minisymposium 15: Molecular Biologyof ExtracellularMatrix (386-397)
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EXTRACELLULAR COMPARTMENTS AND COLLAGEN FIBRILLOGENESIS. D. Birk and R. Trelstad. Department of Pathology, Rutgers Medical School, Piscataway, NJ 08854. Morphogenesis in the animal kingdom is closely coupled with the intracellular synthesis and the extracellular deposition of collagen. These morphogenetic events involve multiple steps which begin in compartments inside the cell and continue in compartments outside the cell. The movement of matrix components from the intracellular compartments to the extracellular compartments is a functional continuum. Studies of embryonic chick tendon and cornea fibroblasts with the high voltage transmission electron microscope have provided the beginnings of an understanding of how this functional continuum is related to the structural compartments which the cells create. This series of compartments, inside and outside the cell, is involved in collagen fibrillogenesis, eollegen fibril bundle formation and tissue morphogenesis.
Discoidin I Influences Ordered Cell M i gration of Dictyostelium Discoideum. D.N.W. Cooper, W.R. Springer , and S.H. Barondes, Dept. of Psychiatry, University of California, San Diego, La Jolla, CA, 92093 and V.A. Medical Center, San Diego, CA. Discoidin I, a developmentally regulated N-acetylgalactosamine binding lectin from Dictyostelium discoideum blocks formation of organized streams during aggregation as does anti-diseoidin I. Synthetic peptides containing short specific sequences of diseoidin I which are structurally related to the cell attachment site of fibronectin also block formation of organized streams and, at higher concentrations block cell attachment and spreading to a plastic surface. Discoidin I deficient mutants fail to spread on plastic or to form organized streams. The results, when taken together, indicate that discoidin I functions like fibronectin, to somehow direct ordered cellular migration during morphogenesis. Supported by grants from USPHS and the McKnight Foundation, and by the Veterans Administration Medical Center.
159S
386
387
EXTRACELLULAR COMPARTMENTS AND COLLAGEN FIBRILLOGENESIS. D. Birk and R. Trelstad. Department of Pathology, Rutgers Medical School, Piscataway, NJ 08854. Morphogenesis in the animal kingdom is closely coupled with the intracellular synthesis and the extracellular deposition of collagen. These morphogenetic events involve multiple steps which begin in compartments inside the cell and continue in compartments outside the cell. The movement of matrix components from the intracellular compartments to the extracellular compartments is a functional continuum. Studies of embryonic chick tendon and cornea fibroblasts with the high voltage transmission electron microscope have provided the beginnings of an understanding of how this functional continuum is related to the structural compartments which the cells create. This series of compartments, inside and outside the cell, is involved in collagen fibrillogenesis, eollegen fibril bundle formation and tissue morphogenesis.
Discoidin I Influences Ordered Cell M i gration of Dictyostelium Discoideum. D.N.W. Cooper, W.R. Springer , and S.H. Barondes, Dept. of Psychiatry, University of California, San Diego, La Jolla, CA, 92093 and V.A. Medical Center, San Diego, CA. Discoidin I, a developmentally regulated N-acetylgalactosamine binding lectin from Dictyostelium discoideum blocks formation of organized streams during aggregation as does anti-diseoidin I. Synthetic peptides containing short specific sequences of diseoidin I which are structurally related to the cell attachment site of fibronectin also block formation of organized streams and, at higher concentrations block cell attachment and spreading to a plastic surface. Discoidin I deficient mutants fail to spread on plastic or to form organized streams. The results, when taken together, indicate that discoidin I functions like fibronectin, to somehow direct ordered cellular migration during morphogenesis. Supported by grants from USPHS and the McKnight Foundation, and by the Veterans Administration Medical Center.
159S