Hollfelder D, Frasch M, Reim I (2014)
Publication Status: Published
Publication Type: Journal article, Original article
Publication year: 2014
Publisher: BIOMED CENTRAL LTD
Book Volume: 14
Conclusions: Assembly of the cardiac ECM depends primarily on laminin, whereas collagen IV is needed for stabilization. Our data underscore the importance of a correctly assembled ECM particularly for the development of cardiac tissues and their lateral connections. The mutational analysis suggests that the beta 6/beta 3/beta 8 interface of the laminin beta LN domain is highly critical for formation of contiguous cardiac ECM layers. Certain mutations in the collagen IV triple helix-forming domain may exert a semi-dominant effect leading to an overall weakening of ECM structures as well as intracellular accumulation of collagen and other molecules, thus paralleling observations made in other organisms and in connection with collagen-related diseases.
APA:
Hollfelder, D., Frasch, M., & Reim, I. (2014). Distinct functions of the laminin beta LN domain and collagen IV during cardiac extracellular matrix formation and stabilization of alary muscle attachments revealed by EMS mutagenesis in Drosophila. Bmc Developmental Biology, 14. https://doi.org/10.1186/1471-213X-14-26
MLA:
Hollfelder, Dominik, Manfred Frasch, and Ingolf Reim. "Distinct functions of the laminin beta LN domain and collagen IV during cardiac extracellular matrix formation and stabilization of alary muscle attachments revealed by EMS mutagenesis in Drosophila." Bmc Developmental Biology 14 (2014).
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