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Supramolecuar Structure and Dynamics in Connective Tissues: Modulation of Aggrecan and Collagen VI Network Assembly by Extracellular Matrix Components.

Principal investigator; Mörgelin, Matthias, Associate Professor, PhD

Clinical speciality:

Phone: +4646-2220741

Co-workers:

Connective tissues play important roles in the form of three-dimensional supportive and structural formations characterized by a low cell density and an abundant ECM. The ECM molecules are often substituted with complex glycosaminoglycans (GAG), oligosaccharides, phosphate and sulphate groups. The characteristics, interactions, and relative abundance of the matrix molecules largely define the properties of different connective tissues. They are secreted by the cells, which also govern their assembly into the complex supramolecular structures by highly ordered processes.

We investigate how aggrecan and collagen VI network components specifically assemble into networks and how matrix proteins modulate and/or stabilize network assembly. We apply an integral approach, combining light and electron microscopy with more conventional methods, to directly identify interacting proteins. The unique features of electron microscopy complement higher resolution structure elucidation techniques, such as X-ray diffraction and nuclear magnetic resonance spectroscopy (NMR) by 1) directly recording images as opposed to diffraction patterns or spectra, 2) the capability of exploring biological structure at all levels from the macroscopic to the atomic scale.

Key elements in all connective tissues are networks of different fibers contributing to the mechanical strength, elasticity and resiliency of the tissue. Alterations in tissue organization often result in progressive disease, severely precluding mobility and life quality of the patient.

Link to project homepage: http://www.cmb.lu.se/

5 recent original publications

Wiberg C, Heinegård D, Wenglén C, Timpl R, Mörgelin M.
Biglycan organizes collagen VI into hexagonal-like networks resembling tissue structures.
J Biol Chem. 2002; 277: 49120-49126

Wiberg C, Klatt AR, Wagener R, Paulsson M, Bateman JF, Heinegård D and Mörgelin M
Complexes of Matrilin-1 and Biglycan or Decorin Connect Collagen VI Microfibrils to both Collagen II and Aggrecan.
J Biol Chem. 2003; 278: 37698-37704

Wiberg C, Hedbom E, Khairullina A, Lamandé S R, Oldberg Å, Timpl R, Mörgelin M and Heinegård D
Biglycan and Decorin Bind Close to the N-terminal Region of the Collagen Type VI Triple Helix.
J. Biol. Chem.. 2001; 276: 18947-18952

Fitzgerald J, Mörgelin M, Lamandé S, Selan C and Bateman JF
The Amino-terminal N5 Subdomain of the a3(VI) Chain is Important for Collagen VI Microfibril Formation.
J. Biol. Chem.. 2001; 276: 187 – 193

Olin A, Mörgelin M, Sasaki T, Chu ML, Timpl R, Heinegård D and Aspberg A
The Aggregating Proteoglycans Form Networks With Fibulin-2 Through Lectin Domain Binding.
J. Biol. Chem.. 2001; 276: 1253 - 1261

Further publications here (new window)

Financing/year