caa a22 4500 475774957 CHVBK 20180406123628.0 cr unu---uuuuu 170329e20000201xx s 000 0 eng 10.1007/s004180050014 doi (NATIONALLICENCE)springer-10.1007/s004180050014 Ultrastructural colocalization of nidogen-1 and nidogen-2 with laminin-1 in murine kidney basement membranes [Elektronische Daten] [N. Miosge, F. Köther, S. Heinemann, E. Kohfeldt, R. Herken, R. Timpl] Abstract : Nidogen-1, a key component of basement membranes, is considered to function as a link between laminin and collagen type IV networks. Recently a new member of the nidogen family, nidogen-2, has been characterized. Preliminary immunohistochemical data indicated that nidogen-1 and nidogen-2 show a similar tissue distribution at the light microscopic level. We have now localized nidogen-1 and nidogen-2, as well as their corresponding mRNAs, at the light and electron microscopic levels in adult mouse kidney, by in situ hybridization and immunogold histochemistry, as well as carrying out double labeling with laminin-1. Both nidogen-1 and nidogen-2 mRNAs are found not only in mesenchymal cells of embryonic tissues, but also in all epithelial and endothelial cells in adult mouse kidney. Both nidogens are ubiquitous basement membrane components in the mouse kidney, being found in glomerular, tubular, and capillary compartments and Bowman's capsule. Furthermore, a substantial fraction of nidogen-1 and nidogen-2 colocalizes with laminin-1. The results indicate that nidogen-1 and nidogen-2 could well substitute for one another in some of their biological activities in kidney, for example, stabilizing basement membrane networks in vivo. Springer-Verlag Berlin Heidelberg, 2000 Miosge N. Zentrum Anatomie, Abteilung Histologie, Kreuzbergring 36, 37075 Goettingen, Germany e-mail: nmiosge@gwdg.de Tel.:+49-551-397075, Fax: +49-551-397067, DE aut Köther F. Zentrum Anatomie, Abteilung Histologie, Kreuzbergring 36, 37075 Goettingen, Germany e-mail: nmiosge@gwdg.de Tel.:+49-551-397075, Fax: +49-551-397067, DE aut Heinemann S. Zentrum Anatomie, Abteilung Histologie, Kreuzbergring 36, 37075 Goettingen, Germany e-mail: nmiosge@gwdg.de Tel.:+49-551-397075, Fax: +49-551-397067, DE aut Kohfeldt E. Max-Planck-Institut für Biochemie, 82152 Martinsried, Germany, DE aut Herken R. Zentrum Anatomie, Abteilung Histologie, Kreuzbergring 36, 37075 Goettingen, Germany e-mail: nmiosge@gwdg.de Tel.:+49-551-397075, Fax: +49-551-397067, DE aut Timpl R. Max-Planck-Institut für Biochemie, 82152 Martinsried, Germany, DE aut https://doi.org/10.1007/s004180050014 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s004180050014 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Miosge N. Zentrum Anatomie, Abteilung Histologie, Kreuzbergring 36, 37075 Goettingen, Germany e-mail: nmiosge@gwdg.de Tel.:+49-551-397075, Fax: +49-551-397067, DE aut NATIONALLICENCE 700 1- Köther F. Zentrum Anatomie, Abteilung Histologie, Kreuzbergring 36, 37075 Goettingen, Germany e-mail: nmiosge@gwdg.de Tel.:+49-551-397075, Fax: +49-551-397067, DE aut NATIONALLICENCE 700 1- Heinemann S. Zentrum Anatomie, Abteilung Histologie, Kreuzbergring 36, 37075 Goettingen, Germany e-mail: nmiosge@gwdg.de Tel.:+49-551-397075, Fax: +49-551-397067, DE aut NATIONALLICENCE 700 1- Kohfeldt E. Max-Planck-Institut für Biochemie, 82152 Martinsried, Germany, DE aut NATIONALLICENCE 700 1- Herken R. Zentrum Anatomie, Abteilung Histologie, Kreuzbergring 36, 37075 Goettingen, Germany e-mail: nmiosge@gwdg.de Tel.:+49-551-397075, Fax: +49-551-397067, DE aut NATIONALLICENCE 700 1- Timpl R. Max-Planck-Institut für Biochemie, 82152 Martinsried, Germany, DE aut Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer