Extension of the Life-Span of Human Endothelial Cells by an Interleukin-1αAntisense Oligomer

Maier, Jeanette A.M.; Voulalas, Pamela J.; Roeder, David; Maciag, Thomas

doi:10.1126/science.2218499

Cited by 382 publications

(200 citation statements)

References 86 publications

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“…Cells became progressively larger with increasing passage number (Figure 1a ± c), a typical sign of cellular senescence (Maier et al, 1990). In addition, cell proliferation rate decreased as measured by a progressive lengthening of the passage doubling time and by a dramatic reduction in [ 3 H]thymidine incorporation (Figure 2).…”

Section: Morphology and Proliferation Of Hdmec Cultured With Or Withomentioning

confidence: 95%

“…Like many other cell types, vascular endothelial cells undergo senescence when cultured in vitro (Maier et al, 1990). However, previous studies of endothelial senescence were conducted without the addition of vascular permeability factor/vascular endothelial growth factor (VPF/VEGF), a cytokine now known to be critically important in the regulation of many aspects of endothelial cell function.…”

Section: Introductionmentioning

confidence: 99%

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Vascular permeability factor/vascular endothelial growth factor (VPF/VEGF) delays and induces escape from senescence in human dermal microvascular endothelial cells

et al. 1997

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Section: Morphology and Proliferation Of Hdmec Cultured With Or Withomentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

Vascular permeability factor/vascular endothelial growth factor (VPF/VEGF) delays and induces escape from senescence in human dermal microvascular endothelial cells

et al. 1997

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“…Glyceraldehyde-3-phosphate dehydrogenase cDNA was amplified as a control for cDNA quality. 29 The amplified products were subjected to electrophoresis on a 6.5% polyacrylamide gel, followed by silver staining. DNA bands corresponding to the normal and abnormal size transcripts were purified using the GFX PCR DNA and Gel Band Purification Kit (Amersham Biosciences, Piscataway, NJ), and sequenced on the ABI PRISM 310 Genetic Analyzer (Applied Biosystems, Foster City, CA).…”

Section: Reverse Transcription-pcr Analysismentioning

confidence: 99%

Molecular alterations in the tumor suppressor gene WWOX in oral leukoplakias

et al. 2008

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SummaryOral leukoplakia is the most prevalent and potentially malignant disorder of the oral mucosa. Previous studies have demonstrated that molecular changes of the WWOX gene (WW-domain containing oxidoreductase), a candidate tumor suppressor gene located at 16q23.3-24.1 that spans FRA16D, the second most common fragile site, are present in several malignant neoplasias, including oral squamous cell carcinoma. In this report, the role of the WWOX gene was investigated in 23 cases of oral leukoplakias. Using nested RT-PCR and immunohistochemistry, altered mRNA transcription and/or reduced Wwox protein expression was observed in 35% of the lesions when compared with normal mucosa. The majority of lesions (4/6) with altered transcripts had a reduction in the expression of Wwox protein. Although normal WWOX expression was found in some lesions with dysplasia, all lesions with WWOX mRNA and/or protein expression showed histological evidence of dysplasia and none of the cases without dysplasia presented this alteration. These results show that the WWOX gene alteration is an early genetic alteration and may contribute to oral carcinogenesis.

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“…42,44 Like IL-33, IL-1a also displays dual actions as both an intracellular nuclear factor and an extracellular cytokine. 50,51 IL-1a precursor (pro-IL-1a) is also biologically active and capable of binding to the IL-1 receptor. 52 The pro-IL-1a is not a substrate of caspase-1 but can be cleaved by calpain to release 17-kDa IL-1a.…”

Section: Can Il-33 Be Secreted?mentioning

confidence: 99%

The enigmatic processing and secretion of interleukin-33

Zhao

2010

Cell Mol Immunol

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Interleukin-33 (IL-33) is the most attractive novel cytokine identified as an IL-1 family member. IL-33 was first named NF-HEV (nuclear factor from high endothelial venules), as it was known to interact with nuclear chromatin although its exact intracellular functions are still to be clarified. IL-33 is now recognized as the specific ligand for the orphan IL-1 receptor family member ST2 and to be involved in polarization of T cells towards T helper 2 cell phenotype and in activation of mast cells, bosophils, eosinophils and natural killer cells. It is essential for IL-33 to be extracellularly released in order to bind to the ST2 receptor and consequently play a crucial role in inflammatory, infectious and autoimmune diseases. However, like the IL-1 family members, IL-1b and IL-18, IL-33 mRNA is translated without a signal sequence for secretion. Additionally, IL-33 cannot be released by the processing and secretion mechanism shared by IL-1b and IL-18 as IL-33 is not a substrate of caspase-1 and does not require proteolysis for activation. In contrast, IL-33 can be inactivated by apoptotic caspases. Accordingly, IL-33 is proposed to be released as an alarmin from necrotic cells but to be deleted during apoptosis. Besides the known autocrine, paracrine, intracrine, juxtacrine and retrocrine mechanisms of cellular interaction with cytokines, release by necrotic cells is another pathway for a cytokine to display its function, which we suggest might be called 'necrocrine'. This mini review summarizes recent progress of how IL-33 displays potential immunoregulatory roles with a particular focus on its enigmatic production. INTRODUCTIONIn the ever-growing list of cytokines, interleukin-33 (IL-33), one of the IL-1 family members (also called IL-1F11), is a most interesting novel cytokine. This cytokine was first named in 2003 as NF-HEV (nuclear factor from high endothelial venules), as it was known to interact with nuclear chromatin in an intracrine manner. 1 It was rediscovered in 2005 as the specific extracellular ligand for the orphan IL-1 receptor family member ST2, and named IL-33. 2 ST2 (also known as IL-1RL1, DER4, T1 and FIT-1) belongs to the Toll-like/IL-1 receptor superfamily. [3][4][5] It has been well documented to be the cellular marker for differentiated T helper 2 (Th2) cells 6,7 and to be expressed on mast cells. 8,9 As a nuclear factor, the intracellular functions of IL-33 remain to be further clarified, although overexpression studies suggested a role as a transcriptional repressor. 10 As an extracellular cytokine, binding of IL-33 to the ST2 receptor activates nuclear factor-kB and mitogen-activated protein kinases, [3][4][5]11 and is involved in the polarization of T cells towards the Th2 cell phenotype 2,6,7,[11][12][13][14] and in activation of mast cells, 15-20 bosophils, 14,20-24 eosinophils, 24-26 and natural killer cells. 14,27 IL-33 must be present extracellularly in order to play the crucial role in inflammatory, infectious and autoimmune diseases including anaphylactic shock, asthma, rheum...

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Extension of the Life-Span of Human Endothelial Cells by an Interleukin-1αAntisense Oligomer

Cited by 382 publications

References 86 publications

Vascular permeability factor/vascular endothelial growth factor (VPF/VEGF) delays and induces escape from senescence in human dermal microvascular endothelial cells

Vascular permeability factor/vascular endothelial growth factor (VPF/VEGF) delays and induces escape from senescence in human dermal microvascular endothelial cells

Molecular alterations in the tumor suppressor gene WWOX in oral leukoplakias

The enigmatic processing and secretion of interleukin-33

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