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Ann Thorac Surg 2003;76:1777
© 2003 The Society of Thoracic Surgeons
a Department of Cardiothoracic and Vascular Surgery, Friedrich-Schiller-University, Bachstrasse 18, 07743 Jena, Germany
b Department of Ultrastructure Research, Friedrich-Schiller-University, Bachstrasse 18, 07743 Jena, Germany
e-mail: florian.opitz{at}med.uni-jena.de
To the Editor:
We read with great interest the article by Hoerstrup and colleagues [1]. In Figure 4C, the authors claim to show "cell elements typical of secretionally active myofibroblasts such as collagen fibrils and elastin." In this context, we question whether mature extracellular matrix proteins such as collagen fibrils or elastin exist in the cytoplasm of physiologic myofibroblasts.
Collagen is assembled from the soluble precursor protein procollagen. Procollagen is cotranslationally transported into the endoplasmic reticulum followed by exocytosis by way of the Golgi apparatus. Only after secretion into the extracellular space are the N- and C-terminal propeptides of procollagen removed by specific proteases, steps in the formation of collagen fibrils [2]. This mechanism prevents the potentially catastrophic assembly of collagen fibrils within the cell.
Elastin-producing cells such as myofibroblasts secrete tropoelastin as an approximately 70-kDa monomer into the extracellular space [3]. The secreted tropoelastin monomers subsequently form elastin.
Taking this information into account, we think it unlikely that the described structures are collagen fibrils and elastin. We routinely perform transmission electron microscopy with ovine vascular myofibroblasts and have found the same intracellular structures as described by Hoerstrup and associates. To our knowledge, the putative collagen fibrils are myofilaments, and the described elastin represents rough endoplasmic reticulum. Our results indicate that collagen fibrils and elastin are strictly confined to the extracellular space.
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