Details

Autor(en) / Beteiligte

• SCHUPPAN, D
• CANTALUPPI, M. C
• BECKER, J
• VEIT, A
• BUNTE, T
• TROYER, D
• SCHUPPAN, F
• SCHMID, M
• ACKERMANN, R
• HAHN, E. G

Titel

Undulin, an extracellular matrix glycoprotein associated with collagen fibrils

Ist Teil von

• The Journal of biological chemistry, 1990-05, Vol.265 (15), p.8823-8832

Ort / Verlag

Bethesda, MD: American Society for Biochemistry and Molecular Biology

Erscheinungsjahr

1990

Quelle

MEDLINE

Beschreibungen/Notizen

• Undulin, a novel noncollagenous extracellular matrix protein, was isolated from skin and placenta. In polyacrylamide gels most of the unreduced protein migrates with Mr above 1,000,000 yielding bands A (Mr 270,000), B1 (Mr 190,000), and B2 (Mr 180,000) after reduction. Undulin is biochemically and immunochemically distinct from other previously characterized large matrix glycoproteins. Immunoblotting using monoclonal antibodies suggests that bands A and B are closely related. Electron microscopy reveals undulin as structures consisting of an approximately 80-nm-long-tail with a nodule on one end and with one or two shorter arms on the other. Ultrastructurally immunolabeled undulin is found mainly between densely packed mature collagen fibrils. Indirect immunofluorescence shows bundles of uniform wavy fibers in dense connective tissues superimposable on a subpopulation of type I collagen structures. This suggests that undulin serves a specific yet unknown function in the supramolecular organization of collagen fibrils in soft tissues.