Anders Aspberg

Address: Section for Connective Tissue Biology, BMC C12,
221 84, Lund. Sweden.
tel: (46) 046 222 9587
fax: (46) 046 211 34 17

email: Anders.Aspberg@med.lu.se

Docent

Our overall research interest is to understand how the extracellular matrix (ECM) is constructed. It is clear that many important processes in the body are governed by the ECM and cellular interactions with the matrix through specific receptors, such as integrins. Much information to that effect has been gained from in vitro interaction studies, but in vivo the matrix components are assembled into complex three-dimensional networks. This may have significant effects. When in complexes, the individual components may well adopt different structural conformations as compared to when in isolation. In addition, the cells in vivo are surrounded by this elaborate matrix and thus exposed to a number of different components simultaneously. Understanding the organization of the extracellular matrix is thus crucial for understanding its functions in development and normal tissue homeostasis as well as in different pathophysiological conditions. We have focused our work on two different proteins / protein families. In the main project we are studying the aggrecan family G3 domains and their functions. In a second project we are assessing the interactions and functions of PRELP, a unique heparin-binding member of the LRR family.

1. The aggrecan G3 domain and its functions.

2. PRELP - a unique heparin binding LRR protein.

Lorenzo P, Aspberg A, Onnerfjord P, Bayliss M, Neame P, Heinegard D. Identification and characterization of Asporin - A novel member of the leucine rich repeat protein family closely related to decorin and biglycan. J Biol Chem. 2001 Jan 10.

Olin AI, Mörgelin M, Sasaki T, Timpl R, Heinegård D, Aspberg A. The Proteoglycans Aggrecan and Versican Form Networks with Fibulin-2 through Their Lectin Domain Binding. J. Biol Chem. 2001 Jan 12;276(2):1253-1261.

Bengtsson E, Aspberg A, Heinegård D, Sommarin Y, Spillmann D. The amino-terminal part of PRELP binds to heparin and heparan sulfate. J. Biol Chem. 2000 Dec29;275(52):40695-702.

Fibulin is a ligand for the C-type lectin domains of aggrecan and versican. Anders Aspberg, Susanne Adam, Gunter Kostka, Rupert Timpl and Dick Heinegård. J. Biol. Chem. 274 (29) 20444-20449.

Miura R, Aspberg A, Ethell IM, Hagihara K, Schnaar RL, Ruoslahti E, Yamaguchi Y. The proteoglycan lectin domain binds sulfated cell surface glycolipids and promotes cell adhesion. J Biol Chem. 1999 Apr 16;274(16):11431-8.

Aspberg A, Miura R, Bourdoulous S, Shimonaka M, Heinegard D, Schachner M, Ruoslahti E, Yamaguchi Y. The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety. Proc Natl Acad Sci U S A. 1997 Sep 16;94(19):10116-21.

Aspberg A, Binkert C, Ruoslahti E. Related Articles The versican C-type lectin domain recognizes the adhesion protein tenascin-R. Proc Natl Acad Sci U S A. 1995 Nov 7;92(23):10590-4.