title: Change in cytoskeletal phenotype and extracellular matrix production of muscularis mucosae during early invasive colorectal adenocarcinoma.
abstract: Bundles of eosinophilic spindle cells are often found in histological preparations of the stroma of invasive colorectal adenocarcinomas. To clarify their significance, especially during the early invasive phase, we histologically and immunohistochemically studied 33 submucosally invasive colorectal adenocarcinomas in terms of their relationship with the muscularis mucosa, their cytoskeletal phenotype, and their production of extracellular matrix (ECM). Histological continuity between bundles of eosinophilic spindle cells and the muscularis mucosa was identified in 19 out of 33 adenocarcinomas (57.6%). With respect to their cytoskeletal phenotypes, the expression of alpha-smooth muscle actin (alpha-SMA) did not differ between the muscularis mucosa and the eosinophilic spindle cells, whereas the expression of desmin and high molecular weight caldesmon (h-CD) of the eosinophilic spindle cells was decreased compared with that of the muscularis mucosa (p<0.05). Definitive type I procollagen (procollagen I) expression was identified, at least in part, in 16 out of 20 (80%) areas of the eosinophilic spindle cells that were continuous with the muscularis mucosa, and in 26 out of 29 (89.7%) areas of the eosinophilic spindle cells that were not. These findings suggest that the muscularis mucosa is the origin of the eosinophilic spindle cells, that they undergo phenotypic changes separately from the smooth muscle, that is, myofibroblastic changes, and that they contribute to carcinomatous stroma formation through production of an ECM component. These findings should be taken into consideration when determining the level of submucosal invasion by colorectal adenocarcinomas.
authors.affiliation: Dept. of Pathology, Saitama Medical School, Iruma, Japan. shinba@saitama-med.ac.jp
authors.forename: S
authors.initials: S
authors.lastname: Ban
authors.forename: Y
authors.initials: Y
authors.lastname: Goto
authors.forename: N
authors.initials: N
authors.lastname: Mitsuki
authors.forename: K
authors.initials: K
authors.lastname: Kamada
authors.forename: T
authors.initials: T
authors.lastname: Fujita
authors.forename: M
authors.initials: M
authors.lastname: Takahama
mesh_terms: D000199:Actins / Q000378:metabolism; D000230:Adenocarcinoma / Q000378:metabolism* / Q000473:pathology; D002148:Calmodulin-Binding Proteins / Q000378:metabolism; D015179:Colorectal Neoplasms / Q000378:metabolism* / Q000473:pathology; D003599:Cytoskeleton / Q000473:pathology*; D003893:Desmin / Q000378:metabolism; D004804:Eosinophils / Q000473:pathology; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D006801:Humans; D007124:Immunoenzyme Techniques; D007413:Intestinal Mucosa / Q000378:metabolism* / Q000473:pathology; D009130:Muscle, Smooth / Q000378:metabolism* / Q000473:pathology; D009361:Neoplasm Invasiveness; D010641:Phenotype; D011347:Procollagen / Q000378:metabolism
chemical_list: D000199:Actins; D002148:Calmodulin-Binding Proteins; D003893:Desmin; D016326:Extracellular Matrix Proteins; D011347:Procollagen