American Society for Matrix Biology Subforums

Publication year: 2010
Source: Matrix Biology, In Press, Accepted Manuscript, Available online 6 February 2010

Helen K., Graham , Nigel W., Hodson , Judith A., Hoyland , Sarah J., Millward-Sadler , David, Garrod , ...

Conventional approaches for ultrastructural high resolution imaging of biological specimens induce profound changes in bio-molecular structures. By combining tissue cryo-sectioning with non-destructive atomic force microscopy (AFM) imaging we have developed a methodology that may be applied by the non-specialist to both preserve and visualize biomolecular structures (in particular extracellular matrix assemblies) in situ. This tissue section AFM technique is capable of: i) resolving nm-μm scale features of intra- and extra-cellular structures in tissue cryosections; ii) imaging the same tissue region before and after experimental interventions; iii) combining ultrastructural imaging with complimentary microscopical and micromechanical methods. Here, we employ this technique...

Publication year: 2010
Source: Matrix Biology, In Press, Accepted Manuscript, Available online 4 February 2010

Li, Kong , Qingyun, Tian , Fengjin, Guo , Maria T., Mucignat , Roberto, Perris , ...

In an effort to define the biological functions of COMP, a functional genetic screen was performed. This led to the identification of extracellular matrix protein 1 (ECM1) as a novel COMP-associated partner. COMP directly binds to ECM1 both in vitro and in vivo. The EGF domain of COMP and the C-terminus of ECM1 mediate the interaction between them. COMP and ECM1 Colocalize in the Growth Plates in Vivo. ECM1 inhibits chondrocyte hypertrophy, matrix mineralization, and endochondral bone formation, and COMP overcomes the inhibition by ECM1. In addition, COMP-mediated neutralization of ECM1 inhibition depends on their interaction, since COMP largely fails...

Publication year: 2010
Source: Matrix Biology, In Press, Accepted Manuscript, Available online 25 January 2010

Guy G., Hoffman , Amanda M., Branam , Guorui, Huang , Francisco, Pelegri , William G., Cole , ...

Genes for tetrapod fibrillar procollagen chains can be divided into two clades, A and B, based on sequence homologies and differences in protein domain and gene structures. Although the major fibrillar collagen types I-III comprise only clade A chains, the minor fibrillar collagen types V and XI comprise both clade A chains and the clade B chains pro-α1(V), pro-α3(V), pro-α1(XI) and pro-α2(XI), in which defects can underlie various genetic connective tissue disorders. Here we characterize the clade B procollagen chains of zebrafish. We demonstrate that in contrast to the four tetrapod clade B chains, zebrafish have six clade B chains,...