Intercellular Adhesion Molecule-1 Is Upregulated via the Protein Kinase C Pathway in Human Thyroid Carcinoma Cell Lines

Bassi, V.; Riu, S. De; Feliciello, Antonio; Altomonte, Maresa; Allevato, Giovanna; Rossi, Giulio De; Fenzi, Gianfranco

doi:10.1089/thy.1998.8.23

Cited by 7 publications

(5 citation statements)

References 16 publications

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“…tPA is an agonist of protein kinase C (PKC) (20), and inhibition of PKC can diminish PN death in organotypic cultures initiated at P3 (18). We found that a PKC antagonist, Gö 6976 (2 M), greatly inhibited PN death in nr cerebellar slice cultures initiated at P9 (P Ͻ 0.05) (Fig.…”

Section: Resultsmentioning

confidence: 83%

Purkinje neuron degeneration in nervous ( nr ) mutant mice is mediated by a metabolic pathway involving excess tissue plasminogen activator

Teng

et al. 2006

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

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Purkinje neurons (PNs), the central cells in cerebellar circuitry and function, constitute a vulnerable population in many human genetic, malignant, hypoxic, and toxic diseases. In the nervous (nr) mutant mouse, the majority of PNs die in the fourth to fifth postnatal weeks, but the responsible molecules are unknown. We first disclose a remarkable increase in mRNA expression and protein concentration in the nr cerebellum of tissue plasminogen activator (tPA), a gene closely linked to the mapped but as-yetuncloned nr locus. Evidence that excessive tPA triggers nr PN death was obtained with organotypic slice cultures expressing the nr PN phenotype, in which an inhibitor of tPA led to increased nr PN survival. An antagonist of protein kinase C, a downstream component in the tPA pathway, also increased nr PN survival. Additional downstream targets in the tPA pathway (the mitochondrial voltage-dependent anion channel, brain-derived neurotrophic factor, and neurotrophin 3) were also abnormal, in parallel with the alterations in PN mitochondrial morphology, dendritic growth, and synaptogenesis that culminate in nr PN death and motor incoordination. We thus propose a molecular pathway by which the excessive tPA in nr cerebellum mediates PN degeneration.dendrite development ͉ mitochondria ͉ neurotrophin ͉ synapse ͉ voltage-dependent anion channel

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Section: Resultsmentioning

confidence: 83%

Purkinje neuron degeneration in nervous ( nr ) mutant mice is mediated by a metabolic pathway involving excess tissue plasminogen activator

Teng

et al. 2006

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

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“…The possible reason of this discrepancy may depend upon the presence of several adhesion molecules, which display redundant functions in cell-cell adhesion and are all substrates of ADAM17/TACE. For example, a previous report showed the expression of ICAM-1 in thyroid carcinoma cells [39].…”

Section: Discussionmentioning

confidence: 99%

Activated Leukocyte Cell Adhesion Molecule Expression and Shedding in Thyroid Tumors

et al. 2011

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Activated leukocyte cell adhesion molecule (ALCAM, CD166) is expressed in various tissues, cancers, and cancer-initiating cells. Alterations in expression of ALCAM have been reported in several human tumors, and cell adhesion functions have been proposed to explain its association with cancer. Here we documented high levels of ALCAM expression in human thyroid tumors and cell lines. Through proteomic characterization of ALCAM expression in the human papillary thyroid carcinoma cell line TPC-1, we identified the presence of a full-length membrane-associated isoform in cell lysate and of soluble ALCAM isoforms in conditioned medium. This finding is consistent with proteolytically shed ALCAM ectodomains. Nonspecific agents, such as phorbol myristate acetate (PMA) or ionomycin, provoked increased ectodomain shedding. Epidermal growth factor receptor stimulation also enhanced ALCAM secretion through an ADAM17/TACE-dependent pathway. ADAM17/TACE was expressed in the TPC-1 cell line, and ADAM17/TACE silencing by specific small interfering RNAs reduced ALCAM shedding. In addition, the CGS27023A inhibitor of ADAM17/TACE function reduced ALCAM release in a dose-dependent manner and inhibited cell migration in a wound-healing assay. We also provide evidence for the existence of novel O-glycosylated forms and of a novel 60-kDa soluble form of ALCAM, which is particularly abundant following cell stimulation by PMA. ALCAM expression in papillary and medullary thyroid cancer specimens and in the surrounding non-tumoral component was studied by western blot and immunohistochemistry, with results demonstrating that tumor cells overexpress ALCAM. These findings strongly suggest the possibility that ALCAM may have an important role in thyroid tumor biology.

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“…ICAM-1 expression is increased by PKC activators such as phorbol ester and phorbol dibutyrate [36,[160][161][162][163] and PKC activity in a variety of cell types is required for the induction of ICAM-1 by inflammatory mediators such as IL-1␤, TNF-␣, IFN-␥, nitric oxide, UVB, and LPS [13,21,82,[164][165][166][167][168][169]. Indeed, pharmacological agents that block PKC activity inhibit induced ICAM-1 transcription, although different PKC isoforms may be involved depending on the cell type and stimuli [161,[169][170][171][172].…”

Section: Pkc Regulation Of Icam-1mentioning

confidence: 99%

Regulation of intercellular adhesion molecule-1 (CD54) gene expression

Roebuck

Finnegan

1999

Journal of Leukocyte Biology

507

497

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Intercellular adhesion molecule-1 (ICAM-1, CD54) is an inducible cell adhesion glycoprotein of the immunoglobulin supergene family expressed on the surface of a wide variety of cell types. ICAM-1 interactions with the beta2 integrins CD11a/CD18 (LFA-1) and CD11b/CD18 (MAC-1) on the surface of leukocytes are important for their transendothelial migration to sites of inflammation and their function as costimulatory molecules for T cell activation. ICAM-1 is constitutively expressed on the cell surface and is up-regulated in response to a variety of inflammatory mediators, including proinflammatory cytokines, hormones, cellular stresses, and virus infection. These stimuli increase ICAM-1 expression primarily through activation of ICAM-1 gene transcription. During the past decade much has been learned about the cell type- and stimulus-specific transcription of ICAM-1. The architecture of the ICAM-1 promoter is complex, containing a large number of binding sites for inducible transcription factors, the most important of which is nuclear factor-kappa B (NF-kappaB). NF-kappaB acts in concert with other transcription factors and co-activators via specific protein-protein interactions, which facilitate the assembly of distinct stereospecific transcription complexes on the ICAM-1 promoter. These transcription complexes presumably mediate the induction of ICAM-1 expression in different cell types and in response to different stimuli. In this review, we summarize our current understanding of ICAM-1 gene regulation with a particular emphasis on the transcription factors and signal transduction pathways critical for the cell type- and stimulus-specific activation of ICAM-1 gene transcription.

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Intercellular Adhesion Molecule-1 Is Upregulated via the Protein Kinase C Pathway in Human Thyroid Carcinoma Cell Lines

Cited by 7 publications

References 16 publications

Purkinje neuron degeneration in nervous ( nr ) mutant mice is mediated by a metabolic pathway involving excess tissue plasminogen activator

Purkinje neuron degeneration in nervous ( nr ) mutant mice is mediated by a metabolic pathway involving excess tissue plasminogen activator

Activated Leukocyte Cell Adhesion Molecule Expression and Shedding in Thyroid Tumors

Regulation of intercellular adhesion molecule-1 (CD54) gene expression

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