J Varani, D Trinh, T E Carey, M Liebert, M J Wheelock
{"title":"Expression of cell surface adhesion molecules on the epithelium of Organ-cultured skin.","authors":"J Varani, D Trinh, T E Carey, M Liebert, M J Wheelock","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Human neonatal foreskin was maintained in organ culture under serum-free, growth-factor-free conditions or in the presence of a combination of growth factors that are known to stimulate keratinocyte proliferation in monolayer culture. Previously, we have shown that normal histology is maintained when growth-factor-free conditions are used but that the epithelium undergoes a hyperproliferative response and invades the dermis in the presence of the exogenous growth factors. In the present study, the tissue was examined by immunofluorescence for expression of alpha 6 and beta 4 integrin components and for E-cadherin. Under growth factor-free conditions, both alpha 6 and beta 4 were localized to the basal surface of epithelial cells in contact with the basement membrane. In contrast, both epitopes were diffusely distributed throughout the basal epithelium in the presence of growth factors. E-cadherin expression was rapidly lost from the tissue in organ culture. This occurred in both the presence and absence of exogenous growth factors. On the basis of these immunochemical results, we conclude that the same changes in alpha 6 and beta 4 expression that are seen in rapidly proliferating keratinocytes and squamous epithelial cell tumors can be seen in the epidermis of organ-cultured skin when it is maintained in the presence of epithelial growth factors. The observed loss of E-cadherin, in contrast, appears to be a consequence of incubation in organ culture.</p>","PeriodicalId":14452,"journal":{"name":"Invasion & metastasis","volume":"15 5-6","pages":"189-96"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19737853","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
J Fujimoto, M Hori, S Ichigo, S Morishita, T Tamaya
{"title":"Estrogen activates invasiveness of endometrial cancel cells to the interstitium.","authors":"J Fujimoto, M Hori, S Ichigo, S Morishita, T Tamaya","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Invasiveness of endometrial cancer cells such as Ishikawa, HEC-1-A and HHUA cells, to the interstitium was significantly enhanced by estradiol, while medroxyprogesterone acetate (MPA) significantly diminished the estradiol-enhanced invasive potential. All of these endometrial cancer cells possess estrogen receptors. It is suggested that invasiveness to the interstitium, and consequently infiltration to the uterine myometrium (which means local advance) are activated by estradiol via a mechanism related to the estrogen receptor, and that MPA as an antiestrogen agent partly inactivates the invasive ability.</p>","PeriodicalId":14452,"journal":{"name":"Invasion & metastasis","volume":"15 3-4","pages":"135-43"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19599632","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Expression of basic fibroblast growth factor and its mRNA in uterine endometrial cancers.","authors":"J Fujimoto, M Hori, S Ichigo, T Tamaya","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>to evaluate the potential of growth, invasion and metastasis of endometrial cancer cells associated with neovascularization, the expression of basic fibroblast growth factor (FGF) and its mRNA in endometrial cancers and normal endometria as controls was determined by enzyme-linked immunosorbent assay, reverse transcription-polymerase chain reaction and Southern blot. the relationship between FGF expression and histological grades, and the degree of myometrial invasion or clinical stages of endometrial cancers were analyzed. The level of basic FGF was found significantly higher in endometrial cancers of G3 and stage III-IV compared to normal endometria. Likewise, the level of basic FGF mRNA was significantly higher in endometrial cancers of G3, level C and stage IV-IV compared to normal endometria. In cancers of other categories, G1 and G2, levels of A and B, and stage I evaluation in the levels of basic FGF and its mRNA did not differ significantly from those in normal endometria. Since lethal lesions are mostly confined to endometrial cancers of G3, level C, and stages III-IV, the increase of basic FGF, which leads to neovascularization, could be one of the characteristics of highly malignant and /or advanced endometrial cancers, and may contribute to the acceleration of growth, invasion, and metastasis.</p>","PeriodicalId":14452,"journal":{"name":"Invasion & metastasis","volume":"15 5-6","pages":"203-10"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19736598","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
C Munaut, A Noël, U H Weidle, H W Krell, J M Foidart
{"title":"Modulation of the expression of interstitial and type-IV collagenases in coculture of HT1080 fibrosarcoma cells and fibroblasts.","authors":"C Munaut, A Noël, U H Weidle, H W Krell, J M Foidart","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Members of the metalloproteinase family (MMPs) are known to play a crucial role in the metastatic cascade. Here, we report some investigations about the synthesis of interstitial and type-IV collagenases (gelatinases A and B) in a model of coculture of human fibroblasts and HT 1080 fibrosarcoma cells. The interstitial collagenase activity, mainly found in the conditioned medium of fibroblasts, and its mRNA level were increased in the in vitro coculture model. In contrast, gelatinase A was produced by both cell types. The HT 1080 cells additionally synthesised gelatinase B. In coculture, an enhancement of gelatinase A and the presence of its activated form were observed. Northern blot analysis demonstrated that this enzymatic enhancement occurred at a pretranslational level. The stimulation of the interstitial collagenase activity was partially mediated through soluble factor(s), whereas increased gelatinase A appeared to require direct cell-cell interactions. The extracellular matrix component, type-I collagen, stimulated the enzymatic activities released by the individual cells, but it did not modulate the synthesis of interstitial collagenase in coculture. Our results demonstrate that distinct MMPs are modulated by distinct mechanisms, all depending on specific interactions between tumour cells and host fibroblasts.</p>","PeriodicalId":14452,"journal":{"name":"Invasion & metastasis","volume":"15 5-6","pages":"169-78"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19737851","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Y Kaneda, S Yamamoto, T Kihira, Y Tsutsumi, S Nakagawa, M Miyake, K Kawasaki, T Mayumi
{"title":"Synthetic cell-adhesive laminin peptide YIGSR conjugated with polyethylene glycol has improved antimetastatic activity due to a longer half-life in blood.","authors":"Y Kaneda, S Yamamoto, T Kihira, Y Tsutsumi, S Nakagawa, M Miyake, K Kawasaki, T Mayumi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>This study was conducted to determine the mechanisms for the enhanced inhibitory effect of cell-adhesive peptides conjugated to polyethylene glycol (PEG) on tumor metastasis. Tyr-Ile-Gly-Ser-Arg (YIGSR), a laminin-derived peptide, conjugated with amino-PEG (YIGSR-aPEG) inhibited lung metastasis of B16-BL6 melanoma cells more effectively than unconjugated YIGSR peptide. [125I]-YIGSR-aPEG and native [125I]-YIGSR showed similar biphasic elimination and profiles after intravenous injection into C57BL/6 mice. Both [125I]-YIGSR and [125I]-YIGSR-aPEG expressed similar plasma half-lives and organ distributions. The radioactivity of both compounds was transported rapidly from the blood to the kidneys, and immediately excreted into the urine. [125I]-YIGSR was almost completely degraded in the urine, but [125I]-YIGSR-aPEG was not. In an in vitro stability assay, [125I]-YIGSR was degraded immediately upon incubation with mouse serum, whereas [125I]-YIGSR-aPEG was not degraded after 180 min incubation in mouse serum. These findings indicate that the enhanced inhibitory effect of YIGSR-aPEG on lung metastasis might be due to its increased stability in the blood.</p>","PeriodicalId":14452,"journal":{"name":"Invasion & metastasis","volume":"15 3-4","pages":"156-62"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19599634","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
N Yamada, Y S Chung, K Maeda, T Sawada, T Ikehara, H Nishino, M Okuno, M Sowa
{"title":"Increased expression of sialyl Lewis A and sialyl Lewis X in liver metastases of human colorectal carcinoma.","authors":"N Yamada, Y S Chung, K Maeda, T Sawada, T Ikehara, H Nishino, M Okuno, M Sowa","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Sialyl Lewis A (SLA) and sialyl Lewis X (SLX) have been shown to be specific ligands for endothelial leukocyte adhesion molecule-1 (ELAM-1), and may be involved in the process of adhesion between cancer cells and endothelium. We used immunohistochemical methods to study the expression of SLA, SLX and CEA in both primary tumors and matched metastatic liver lesions of colorectal carcinomas. Specimens from primary tumors and matched liver metastases from 24 patients with colorectal carcinomas were studied immunohistochemically. The degree of expression of CEA in liver metastases was similar to that in primary tumors, but SLA and SLX were expressed on a larger proportion of tumor cells in liver metastases than in primary tumors. Our findings suggest that colorectal carcinoma cells expressing SLA and/or SLX form metastatic liver tumors. They also suggest that expression of SLA and SLX in primary of colorectal carcinoma can be used as a prognostic indicator of metastasis.</p>","PeriodicalId":14452,"journal":{"name":"Invasion & metastasis","volume":"15 3-4","pages":"95-102"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19599637","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
N Daémi, T Vallet, N Thomasset, M F Jacquier, N Zebda, J F Doré, B Sordat, L Rémy
{"title":"Expression of the alpha 6, beta 1 and beta 4 integrin subunits, basement membrane organization and proteolytic capacities in low and high metastatic human colon carcinoma xenografts.","authors":"N Daémi, T Vallet, N Thomasset, M F Jacquier, N Zebda, J F Doré, B Sordat, L Rémy","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Malignant transformation is associated with alterations in both cell-cell and cell-matrix interactions. The E2 and C5 clones, derived from the human colon adenocarcinoma LoVo cell line, show, respectively, low and high metastatic capacity as experimental xenografts in vivo. In this study, we have assessed the adhesion and spreading of E2 and C5 cells on basement membrane laminin, expression of the laminin receptor integrins alpha 6 beta 1 and alpha 6 beta 4 and expression of gelatinolytic and plasminogen-dependent activities. On days 5 and 7 after subcutaneous grafting to immunosuppressed newborn rats, well-differentiated E2 tumors displayed a polarized expression of these integrin subunits, with the exception of the beta 1 subunit which remained pericellular. In contrast, C5 tumors were unorganized and the three integrin subunits remained nonpolarized and pericellular. Flow cytometry results showed that the expression of alpha 6 beta 1 and alpha 1 beta 4 integrins was weaker in the highly metastatic C5 clone than in the E2 clone whereas laminin expression was not significantly different. Under-expression and pericellular localization of these integrin receptors in C5 cells as compared to E2 cells may explain the difference in their binding and spreading capacity on laminin, organization of peritumoral basement membrane and maintenance of a differentiated phenotype. Whereas similar levels of gelatinolytic and plasminogen activator activities have been detected in the culture supernatant of the two clones, histozymograms showed that plasminogen-dependent caseinolysis appeared earlier in sections of C5 and parental tumors than in those of E2 xenografts. These results suggest that enhanced aggressiveness of C5 tumors in vivo may be linked to both an impairment of basement membrane setting due to integrin underexpression and distribution and of proteolytic activities modulated by tumor/host interactions.</p>","PeriodicalId":14452,"journal":{"name":"Invasion & metastasis","volume":"15 3-4","pages":"103-15"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19599702","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"EGF enhances attachment of metastatic rat mammary adenocarcinoma cell clone MTLn3 to fibronectin and collagen.","authors":"B Rohde-Schulz, R B Lichtner","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Attachment of highly metastatic rat mammary adenocarcinoma MTLn3 cells to matrix proteins and its modulation by EGF was examined. Plastic plates were coated with varying amounts of collagen or fibronectin. MTLn3 cells exhibited a dose-dependent adhesion to both matrix proteins, however, they attached more efficiently to collagen than to fibronectin. When EGF or TGF alpha were added at 0.3 to 10 ng/ml for 30 min, a dose-dependent increase in adhesion to both matrix proteins was observed. Maximal stimulation (2-fold) was seen with 10 ng/ml of either growth factor. However, EGF was more potent at lower concentrations (0.3-3 ng/ml) than TGF alpha. The ability of growth factors to stimulate adhesion was also dependent on the amount of matrix the cells were exposed to. While EGF increased rapid attachment of MTLn3 cells to both matrix proteins similarly, subsequent cell spreading and formation of lamellar extensions was faster in cells plated on collagen. These results are suggestive of a functional link between EGF receptor and specific integrin activities.</p>","PeriodicalId":14452,"journal":{"name":"Invasion & metastasis","volume":"15 1-2","pages":"1-10"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18674977","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
K Tokita, S Sugihara, T Hiraoka, Y Miyauchi, T Kambara, T Yamamoto
{"title":"Effects of serine protease and deoxyribonuclease on intravascular tumor cell arrest in rat blood-borne lung metastasis.","authors":"K Tokita, S Sugihara, T Hiraoka, Y Miyauchi, T Kambara, T Yamamoto","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Effects of alpha-chymotrypsin and deoxyribonuclease I (DNase I) on the early phase of blood-borne lung metastasis in rats were studied using confocal laser scanning microscopy and AH-109A cells labeled either with carboxyfluorescein diacetate succinimyl ester or with 51Cr. Intravenous administration of alpha-chymotrypsin or DNase I appeared to enhance or inhibit, respectively, the tumor cell arrest in lung microvasculature as a reflection of reduction or promotion of the tumor cell clearance in the microvasculature. These results suggest that the effects of alpha-chymotrypsin and DNase I are related to induction of tumor cell aggregation and disaggregation in the blood stream, respectively.</p>","PeriodicalId":14452,"journal":{"name":"Invasion & metastasis","volume":"15 1-2","pages":"46-59"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18674980","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Resistance mechanisms in human lung cancer.","authors":"J Mattern, M Volm","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Drug resistance is an important problem in the treatment of lung cancer. Patients become resistant not only to the drugs used initially, but also to those to which they have not yet been exposed. Multiple mechanisms contribute to drug resistance in this disease, all or any combination of which may occur simultaneously within each cell, producing an overall drug-resistant phenotype. The limited success of hitherto applied strategies in their ability to circumvent drug resistance in lung cancer suggests that new approaches are required.</p>","PeriodicalId":14452,"journal":{"name":"Invasion & metastasis","volume":"15 3-4","pages":"81-94"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19599636","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}