Differential expression of basement membrane type IV collagen α chains in gastric intramucosal neoplastic lesions

Baba, Yoshifumi; Iyama, Ken Ichi; Ikeda, Koei; Ishikawa, Satoshi; Hayashi, Nariyuki; Miyanari, Nobutomo; Honda, Yasuhiro; Sado, Yoshikazu; Ninomiya, Yoshifumi; Baba, Hideo

doi:10.1007/s00535-007-2112-2

Cited by 20 publications

(17 citation statements)

References 37 publications

(34 reference statements)

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“…Similarly, we found that TGF-β1 stimulation, in a dose-dependent manner, increased the production and mRNA expression of α1(IV) and α2(IV) chains, but not α3(IV) to α6(IV) chains, by cultured human lung fibroblasts. Consistent with our data are findings that α3 (IV) to α6(IV) chains tended to disappear in acinar and ductal BMs of the labial salivary gland in Sjögren's syndrome 33 and in the BM of several malignant neoplasms, such as bronchioloalveolar carcinoma 18 and gastric carcinoma, 34 but that α1(IV) and α2(IV) chains were expressed continuously in the BM even in those pathologic conditions. Moreover, no reliable report about α3(IV) to α6(IV) chains being produced by cultured fibroblasts in vitro has been published.…”

Section: Discussionsupporting

confidence: 91%

Role of α1 and α2 chains of type IV collagen in early fibrotic lesions of idiopathic interstitial pneumonias and migration of lung fibroblasts

Urushiyama

Terasaki

Nagasaka

et al. 2015

Laboratory Investigation

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Early fibrotic lesions are thought to be the initial findings of fibrogenesis in idiopathic interstitial pneumonias, but little is known about their properties. Type IV collagen comprises six gene products, α1-α6, and although it is known as a major basement membrane component, its abnormal deposition is seen in fibrotic lesions of certain organs. We studied the expression of type I and III collagen and all α chains of type IV collagen in lung specimens from patients with usual interstitial pneumonia (UIP) or organizing pneumonia (OP) via immunohistochemistry. With cultured lung fibroblasts, we analyzed the expression and function of all α chains of type IV collagen via immunohistochemistry, western blotting, realtime quantitative PCR, and a Boyden chamber migration assay after the knockdown of α1 and α2 chains. Although we observed type I and III collagens in early fibrotic lesions of both UIP and OP, we found type IV collagen, especially α1 and α2 chains, in early fibrotic lesions of UIP but not OP. Fibroblasts enhanced the expression of α1 and α2 chains of type IV collagen after transforming growth factor-β1 stimulation. Small interfering RNA against α1 and α2 chains increased fibroblast migration, with upregulated phosphorylation of focal adhesion kinase (FAK), and adding medium containing fibroblast-produced α1 and α2 chains reduced the increased levels of fibroblast migration and phosphorylation of FAK. Fibroblasts in OP were positive for phosphorylated FAK but fibroblasts in UIP were not. These results suggest that fibroblasts in UIP with type IV collagen deposition, especially α1 and α2 chains, have less ability to migrate from early fibrotic lesions than fibroblasts in OP without type IV collagen deposition. Thus, type IV collagen deposition in early fibrotic lesions of UIP may be implicated in refractory pathophysiology including migration of lesion fibroblasts via a FAK pathway.

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Section: Discussionsupporting

confidence: 91%

Role of α1 and α2 chains of type IV collagen in early fibrotic lesions of idiopathic interstitial pneumonias and migration of lung fibroblasts

Urushiyama

Terasaki

Nagasaka

et al. 2015

Laboratory Investigation

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“…In this connection, other investigations have focused on the expression of ECM components in the stomach and their role in pathological gastric conditions (Gillensen et al 1993, Shahin et al 1997, Baba et al 2007). …”

Section: Introductionmentioning

confidence: 99%

Distribution of collagen types I, III, and IV in gastric tissue of marmosets (Callithrix spp., Callitrichidae: Primates)

2010

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317Pesq. Vet. Bras. 30(4):317-320, abril 2010 RESUMO.-[Distribuição dos colágenos tipo I, III e IV em tecido gástrico de sagüis (Callithrix spp., Callitrichidae: Primates).] Os componentes da matriz extra-celular (MEC), como os colágenos fibrilares, desempenham um papel fundamental no reparo de feridas, tendo sido estudados em gastroenterologia, em associação com a cicatrização da úlcera gástrica. No entanto, não há estudos até o presente momento, que relatem a descrição e caracterização de componentes da MEC no tecido gástrico, quer seja normal ou com lesão, de espécies de primatas. O objetivo deste estudo foi investigar a expressão dos colágenos tipo I, III e IV no tecido gástrico de sagüis (Callithrix sp.). Foram avaliadas amostras do estômago de 6 Callithrix jacchus, 12 C. kuhli e 12 C. geoffroyi. As amostras foram submetidas à reação de imuno-histoquímica com anticorpos policlonais anti-colágenos tipo I e III e monoclonal anticolágeno tipo IV. Os colágenos tipo I e III foram detectados na submucosa e na lâmina própria da mucosa, entre as glândulas gástricas, enquanto que o colágeno tipo IV foi detectado na muscularis mucosae, nas camadas musculares, nos vasos sanguíneos e na camada mucosa, entre as glândulas gástricas. Estes achados poderão contribuir com estudos futuros relacionados aos componentes da MEC no tecido gástrico de primatas e com estudos comparativos na área da gastroenterologia. com Extracellular matrix (ECM) components such as fibrillar collagens play a fundamental role in wound repair and have also been studied in association with the gastric ulcer healing process in gastroenterology. Nevertheless, there have been no studies in the literature to date regarding the description and characterization of ECM components, neither in normal nor in injured gastric tissue of primate species. The objective of this study was to investigate the expression of gastric collagen types I, III, and IV in marmosets (Callithrix sp.). Histological specimens from the stomach of 6 Callithrix jacchus, 12 C. kuhli, and 12 C. geoffroyi were evaluated. The specimens were immunostained with anti-types I and III collagen polyclonal antibodies and anti-type IV collagen monoclonal antibody. Collagen types I and III were detected in the submucosa and lamina propria between the mucosal glands while collagen type IV was detected in the muscularis mucosae, muscular layers, blood vessels, and gastric mucosa between the mucosal glands. It is hoped that these findings can contribute to future studies on the gastric extracellular matrix components in primates and to comparative studies in the area of gastroenterology.

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“…All six type IV collagen α-chains have been identified in the human colon by immunofluorescence staining using chain-specific monoclonal antibodies [7]. Invasive growth is a hallmark of malignancy in cancers and several studies suggest that the loss of tissue specific α(IV) chains in the epithelial BM may be related to biologically significant events in the invasive stage of cancer in different tissues [8-17]. …”

Section: Introductionmentioning

confidence: 99%

Collagen mRNA levels changes during colorectal cancer carcinogenesis

et al. 2009

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BackgroundInvasive growth of epithelial cancers is a complex multi-step process which involves dissolution of the basement membrane. Type IV collagen is a major component in most basement membranes. Type VII collagen is related to anchoring fibrils and is found primarily in the basement membrane zone of stratified epithelia. Immunohistochemical studies have previously reported changes in steady-state levels of different α(IV) chains in several epithelial cancer types. In the present study we aimed to quantitatively determine the mRNA levels of type IV collagen (α1/α4/α6) and type VII collagen (α1) during colorectal cancer carcinogenesis.MethodsUsing quantitative RT-PCR, we have determined the mRNA levels for α1(IV), α4(IV), α6(IV), and α1(VII) in colorectal cancer tissue (n = 33), adenomas (n = 29) and in normal tissue from the same individuals. In addition, corresponding tissue was examined from healthy volunteers (n = 20). mRNA levels were normalized to β-actin. Immunohistochemical analysis of the distributions of type IV and type VII collagens were performed on normal and affected tissues from colorectal cancer patients.ResultsThe α1(IV) and α1(VII) mRNA levels were statistically significantly higher in colorectal cancer tissue (p < 0.001) as compared to corresponding tissue from healthy controls. This is an early event as tissue from adenomas also displayed a higher level. There were small changes in the levels of α4(IV). The level of α6(IV) was 5-fold lower in colorectal cancer tissue as compared to healthy individuals (p < 0.01). The localisation of type IV and type VII collagen was visualized by immunohistochemical staining.ConclusionOur results suggest that the down-regulation of α6(IV) mRNA coincides with the acquisition of invasive growth properties, whereas α1(IV) and α1(VII) mRNAs were up-regulated already in dysplastic tissue. There are no differences in collagen expression between tissues from healthy individuals and normal tissues from affected individuals.

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Differential expression of basement membrane type IV collagen α chains in gastric intramucosal neoplastic lesions

Abstract: The loss of alpha5/alpha6(IV) chains might be a useful diagnostic finding for gastric intramucosal carcinoma in GINL cases.

Cited by 20 publications

References 37 publications

Role of α1 and α2 chains of type IV collagen in early fibrotic lesions of idiopathic interstitial pneumonias and migration of lung fibroblasts

Role of α1 and α2 chains of type IV collagen in early fibrotic lesions of idiopathic interstitial pneumonias and migration of lung fibroblasts

Distribution of collagen types I, III, and IV in gastric tissue of marmosets (Callithrix spp., Callitrichidae: Primates)

Collagen mRNA levels changes during colorectal cancer carcinogenesis

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