Shedding from the Cell Surface of Normal and Cancer Cells

Black, Paul H.

doi:10.1016/s0065-230x(08)60361-9

Cited by 197 publications

(94 citation statements)

References 629 publications

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“…Secondly, although in tumor cells vesicle shedding is constitutive, in normal cells the process is activated only by specific stimuli. 2 Accordingly, we found that shedding of vesicles by endothelial cells was modulated by serum and angiogenic factors. Serum, known to increase vesicle production by tumor cells, 3,4,19,25 is required for shedding by endothelial cells, because in the absence of serum the production of vesicles is hardly detectable.…”

Section: Discussionmentioning

confidence: 95%

“…1 Shedding is particularly active in proliferating and invasive cells, such as cancer cells, where cell surface components are continually released. 2 The consequences of vesicle shedding from cancer cells include effects on their ability to infiltrate, metastasize, and generally affect their microenvironment. Our previous studies demonstrated that vesicles shed by 8701-BC human breast carcinoma cells, 3 HT-1080 cells, 4 and CABA I ovarian carcinoma cells 5 contain matrix metalloproteinase (MMP)-9, MMP-2, and uPA.…”

mentioning

confidence: 99%

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Shedding of the Matrix Metalloproteinases MMP-2, MMP-9, and MT1-MMP as Membrane Vesicle-Associated Components by Endothelial Cells

Taraboletti

D’Ascenzo

Borsotti

et al. 2002

The American Journal of Pathology

509

381

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Production of matrix-degrading proteases, particularly matrix metalloproteinases (MMPs), by endothelial cells is a critical event during angiogenesis, the process of vessel neoformation that occurs in normal and pathological conditions. MMPs are known to be highly regulated at the level of synthesis and activation, however, little is known about the regulation of MMP secretion by endothelial cells. We found that cultured human umbilical vein endothelial cells shed vesicles (300 to 600 nm) originating from localized areas of the cell plasma membrane, as revealed by ultrastructural analysis. Normal and reverse zymography, Western blot, and immunogold analyses of the vesicles showed two gelatinases, MMP-2 and MMP-9, in both the active and proenzyme forms, the MT1-MMP proenzyme located on the external side of the vesicle membrane and the two inhibitors TIMP-1 and TIMP-2. Serum and the angiogenic factors, fibroblast growth factor-2 and vascular endothelial growth factor, stimulated the shedding of MMPs as vesicle components. Shedding the vesicle was rapid, as it was already completed after 4 hours. Addition of shed vesicles to human umbilical vein endothelial cells resulted in autocrine stimulation of invasion through a layer of reconstituted basement membrane (Matrigel) and cord formation on Matrigel. We conclude that endothelial cells shed MMP-containing vesicles and this may be a mechanism for regulating focalized proteolytic activity vital to invasive and morphogenic events during angiogenesis. (Am J Pathol 2002, 160:673-680)

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Section: Discussionmentioning

confidence: 95%

mentioning

confidence: 99%

Shedding of the Matrix Metalloproteinases MMP-2, MMP-9, and MT1-MMP as Membrane Vesicle-Associated Components by Endothelial Cells

Taraboletti

D’Ascenzo

Borsotti

et al. 2002

The American Journal of Pathology

509

381

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“…Neoplastic transformation and the evolution to metastatic disease are characterized by a dramatic aberration in cellular cohesive British Journal of Cancer (1998) 78(2) Malignant cells possess many membrane surface antigens that sICAM-1 (ng ml-') regulate fundamental cellular functions, including the MHC antigens, differentiation antigens, tumour-specific receptors and :erum sICAM-1 and sE-selectin levels in gastric cancer patients tumour-associated antigens (Black, 1980). These antigens are shed Dut peritoneal metastasis.…”

Section: Discussionmentioning

confidence: 99%

“…tiles and the thicker middle bars indicate the medians Molecules mediating leucocyte-endothelium adhesion may serve as tumour-associated antigens in a variety of solid tumours (Black, 1980). ICAM-1, together with MHC antigens, plays an important ns (Albelda, 1993;Juliano, 1987;Pauli et al, 1990; role in the human immune response, involving T-cell activation et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

Circulating intercellular adhesion molecule-1 and E-selectin levels in gastric cancer

Benekli

Güllü²,

Tekuzman³

et al. 1998

Br J Cancer

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Summary A diversity of adhesive interactions occur between the cancer cell and host extracellular matrix which potentiate neoplastic expansion and metastatic dissemination. In miscellaneous malignant diseases, tumour progression has been obse'rved to be associated with alterations in adhesion molecule expression. Recently, circulating soluble intercellular adhesion molecules have been identified. In this study, serum levels of soluble intercellular adhesion molecule-1 (sICAM-1) and soluble E-selectin (sE-selectin) were determined in patients with gastric cancer. The study group consisted of 27 patients with previously untreated gastric adenocarcinoma. Four patients had stage 11, two patients stage IlIl and 21 patients stage IV disease according to the TNM classification. Nineteen patients had distant metastasis. The sera obtained from 18 healthy volunteers served as controls. Serum sICAM-1 and sE-selectin concentrations were determined by enzyme-linked immunosorbent assay (ELISA). In addition, we also studied other tumour-associated antigens, i.e. CEA and CA 19-9. Serum sICAM-1 levels were significantly increased in patients with gastric cancer (P < 0.0001). However, sE-selectin levels did not differ from the controls. sICAM-1 concentrations were also significantly higher in patients with distant metastasis and peritoneal spread (P = 0.0045 and P = 0.0157 respectively), whereas sE-Selectin levels were elevated only in patients with peritoneal metastasis (P = 0.033). Serum concentrations of sICAM-1 and sE-selectin correlated with CEA levels (P = 0.0013 and P = 0.003 respectively). Elevated levels of sE-selectin were associated with poorer prognosis (P = 0.0099), whereas sICAM-1 had no significant impact on survival. Our results suggest that increased sICAM-1 serum levels may reflect widespread disease and contribute directly to the progression of gastric cancer. Further investigation of the molecular mechanisms of adhesive tumour-host interactions may lead to a better understanding of the natural history of gastric cancer.

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“…These membrane-bound glycolipids are released or shed in vitro by many cells, especially proliferating cells such as tumour cells. 1,2 It has been suggested that high concentrations of gangliosides, present in the circulation of tumour-bearing hosts, [3][4][5][6][7] may be tumour-related. 4 To date, however, there has been no report of direct visualisation and identification of a ganglioside in the plasma of patients with cancer that has not also been detected in normal plasma.…”

Section: Introductionmentioning

confidence: 99%

Detection of a Tumour-Associated Ganglioside in Plasma of Patients With Neuroblastoma

Ladisch¹,

Wu²

1985

The Lancet

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SummaryAn abnormal circulating ganglioside was found in patients with neuroblastoma. This ganglioside appeared as a single band by resorcinol-HCl staining of thin-layer chromatograms of purified total gangliosides isolated from as little as 1 ml of patient plasma. It is a major ganglioside of neuroblastoma tumour tissue and was present (250-1500 pmol lipid-bound sialic acid/ml) in the plasma of five patients with widespread neuroblastoma. In contrast, the ganglioside was not detected (<50 pmol/ml) in plasma samples of six patients in complete remission, nor in plasma samples of seventeen healthy children and adults. Measurement of this circulating tumourassociated ganglioside should be clinically useful in neuroblastoma, offering a new approach to the detection of tumour and the evaluation of therapy.

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Shedding from the Cell Surface of Normal and Cancer Cells

Cited by 197 publications

References 629 publications

Shedding of the Matrix Metalloproteinases MMP-2, MMP-9, and MT1-MMP as Membrane Vesicle-Associated Components by Endothelial Cells

Shedding of the Matrix Metalloproteinases MMP-2, MMP-9, and MT1-MMP as Membrane Vesicle-Associated Components by Endothelial Cells

Circulating intercellular adhesion molecule-1 and E-selectin levels in gastric cancer

Detection of a Tumour-Associated Ganglioside in Plasma of Patients With Neuroblastoma

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