Cancer metastasis

Nicolson, Garth L.

doi:10.1016/0304-419x(82)90020-8

Cited by 303 publications

(42 citation statements)

References 402 publications

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“…Changes of cell-surface carbohydrates accompanying malignant transformation have been implicated in the altered growth behavior of tumor cells (19,20). In many instances, carbohydrate moieties that were expressed during certain stages of embryonic development, but suppressed later on, were found to be reexpressed in tumor cells (21,22).…”

Section: Discussionmentioning

confidence: 99%

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Reexpression of poly(sialic acid) units of the neural cell adhesion molecule in Wilms tumor.

Roth¹,

Zuber²,

Wagner³

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

163

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A unique structural feature of the neural cell adhesion molecule N-CAM is the presence of homopolymers of alpha (2----8)-linked sialic acid units. We have used two specific probes for the detection of poly(sialic acid) in normal human kidney and Wilms tumor: a monoclonal antibody against meningococci group B capsular polysaccharide (homopolymers of alpha (2----8)-linked sialic acid units), which shows no crossreactivity with polynucleotides and denaturated DNA, and bacteriophage-induced endosialidases specifically hydrolyzing alpha (2----8)-linked poly(sialic acid) units. Additionally, for the detection of N-CAM, antibodies recognizing the polypeptide portion of the molecule and biotinylated antisense RNA transcribed from a cDNA clone for N-CAM were applied. Poly(sialic acid) was regionally detectable in human embryonic kidney but undetectable in normal adult kidney, as already reported for rat kidney. The malignant Wilms tumor, which is characterized by the presence of structural components resembling those found in embryonic kidney, reexpressed poly(sialic acid) units and showed positive immunostaining for the polypeptide portion of N-CAM. Immunoblot analysis of Wilms tumor as well as human embryonic kidney and brain with the monoclonal anti-poly(sialic acid) antibody revealed in each case the same high molecular mass broad band. In situ hybridization demonstrated the presence of mRNA for N-CAM in Wilms tumor. We conclude that poly(sialic acid), most probably present on N-CAM, is an oncodevelopmental antigen in human kidney.

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Section: Discussionmentioning

confidence: 99%

“…Alterations in certain cell-surface properties known to accompany malignant transformation in vitro have been correlated with the abnormal growth of tumor cells (19)(20)(21)(22) …”

Section: Discussionmentioning

confidence: 99%

Reexpression of poly(sialic acid) units of the neural cell adhesion molecule in Wilms tumor.

Roth¹,

Zuber²,

Wagner³

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

163

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“…Because entry into and departure from capillaries are critical steps in tumor colonization of distant sites (20), it will be of particular interest to determine whether PNI inhibits tumor cell destruction of endothelial cell basement membranes.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of tumor-cell-mediated extracellular matrix destruction by a fibroblast proteinase inhibitor, protease nexin I.

Bergman¹,

Scott²,

Bajpai³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

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Human fibrosarcoma (HT-1080) cells, in contrast to normal fibroblasts, rapidly hydrolyze the glycoprotein, collagen, and elastin extracellular matrix (ECM) synthesized by cultured rat aortic smooth muscle cells. This degradation occurs at a rapid rate in the presence of serum, indicating that the cellular proteases responsible are relatively insensitive to serum proteinase inhibitors. Here it is shown that protease nexin I (PNI), a fibroblast-secreted inhibitor of urokinase, plasmin, and certain other serine proteinases, effectively inhibited the HT-1080 cell-mediated degradation of this ECM. PNI at 2.0 nM significantly inhibited matrix destruction for 1-2 days and at 0.2 ,uM caused a virtually complete inhibition that persisted for the entire 10-day period of observation. Inhibition of ECM destruction was accompanied by a transient arrest of HT-1080 cell proliferation that took place during the first 3 days after PNI addition. PNI did not inhibit the growth of normal fibroblasts and also did not inhibit the growth of HT-1080 cells that were seeded onto plastic dishes rather than onto ECM. Like many types of malignant cells, HT-1080 cells release large amounts of urokinase. Antibody against this plasminogen activator partially protected ECM from HT-1080 cell-mediated hydrolysis, indicating that it may have been a target of PNM. One potential physiological function ofPNI could be to help maintain the integrity of connective tissue matrices, protection that malignant cells could overcome by secreting proteinases in excessive amounts. (5, 6). Ossowski and Reich (7) recently reported that anti-urokinase antibody inhibited the metastasis of human epidermoid carcinoma cells seeded onto chicken embryo chorioallantoic membranes. In view of the ability of PNI to inhibit urokinase and plasmin, the present investigation was undertaken to determine the effect of this inhibitor on tumor-cell-mediated destruction of extracellular matrix (ECM). Jones and DeClerk (8)

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“…The desmosomes ogy between tumor foci in vivo and monolayer-covered were quantified by ultrastructural morphometry and microcarrier beads in culture [15]. Since metastasis is a expressed per 1000 pm of closely apposed membrane process whereby tumor cells leave their original location (within 50 pm) in the sequence, 68.5 (SIGC), 44.5 (SV- [1], an acquired ability of cells to detach from a mono-SIGC), 23.1 (female SV-SIGC tumors), 20.7 (male SVlayer in cell scattering assays is considered to be a step SIGC tumors), and 2.5 (T-SV-SIGC). These results toward in vitro metastasis and thus assumed to repre-suggested that about a third of the desmosomes were sent reduced strength of adhesion between cells [20].…”

Section: Progression Toward In Vitro Metastasis Was Associatedmentioning

confidence: 99%

Concomitant Alterations of Desmosomes, Adhesiveness, and Diffusion through Gap Junction Channels in a Rat Ovarian Transformation Model System

Stein

Echols

et al. 1993

Experimental Cell Research

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Cancer metastasis

Cited by 303 publications

References 402 publications

Reexpression of poly(sialic acid) units of the neural cell adhesion molecule in Wilms tumor.

Reexpression of poly(sialic acid) units of the neural cell adhesion molecule in Wilms tumor.

Inhibition of tumor-cell-mediated extracellular matrix destruction by a fibroblast proteinase inhibitor, protease nexin I.

Concomitant Alterations of Desmosomes, Adhesiveness, and Diffusion through Gap Junction Channels in a Rat Ovarian Transformation Model System

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