Synchrotron fibre diffraction identifies and locates foetal collagenous breast tissue associated with breast carcinoma.

Synchrotron fibre diffraction studies of collagenous breast tissue have revealed clear and consistent differences in the diffraction intensity patterns between samples taken from patients with breast carcinoma and those taken from controls. These changes, prelusive to carcinoma, are related to changes in and breakdown of the molecular structure of the collagen type IV support collagen adjacent to the type I, type III and type V collagen fibrils. In order to locate the positions and sequence of the different molecular arrangements, multiple samples were taken from a number of patients. The first of these was taken as near to the tumour site as was possible. Subsequent samples were taken at intervals along ducts leading away from the tumour. The results reveal that the collagen distal from the tumour is similar to that of the controls and this was taken as the standard molecular structure of breast tissue. It usually contained some fat. For normal samples taken closer to the tumour site, the wide diffraction ring associated with fat disappears leaving only the fibrillar pattern. Moving closer to the tumour a 'foetal-like tissue' was observed. The tissue immediately adjacent to the tumour was found to have the same molecular structure as that of foetal tissue.

[1]  Y. Amemiya,et al.  Molecular structural changes in human fetal tissue during the early stages of embryogenesis. , 1998, Biochimica et biophysica acta.

[2]  Y. Amemiya,et al.  Two very long periodicities in collagen. , 1993, Biochimica et Biophysica Acta.

[3]  L. Basiricò,et al.  A new form of tumor and fetal collagen that binds laminin. , 1993, Biochemistry.

[4]  A. Howell,et al.  Changes in the extracellular matrix of the normal human breast during the menstrual cycle , 1992, Cell and Tissue Research.

[5]  M. Capel,et al.  The d-spacing of collagen from mitral heart valves changes with ageing, but not with collagen type III content. , 1991, Biochimica et biophysica acta.

[6]  J. Foidart,et al.  The presence of a type IV collagen skeleton associated with periductal elastosis in breast cancer. , 1990, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[7]  T. Salo,et al.  Tumor-promoting phorbol esters and cell proliferation stimulate secretion of basement membrane (type IV) collagen-degrading metalloproteinase by human fibroblasts. , 1985, The Journal of biological chemistry.

[8]  K. Tryggvason,et al.  Characterization of the procollagen IV cleavage products produced by a specific tumor collagenase. , 1984, The Journal of biological chemistry.

[9]  J. Seltzer,et al.  The function of Ca+ in the action of mammalian collagenases. , 1976, Archives of biochemistry and biophysics.

[10]  R. Burgeson,et al.  Structure and function of collagen types , 1987 .

[11]  高エネルギー物理学研究所 Photon Factory activity report , 1984 .