Human tissue factor: cDNA sequence and chromosome localization of the gene

Em, Scarpati; D, Wen; Gj, Broze; Jp, Miletich; Rr, Flandermeyer; Nr, Siegel; Sadler, J. Evan

doi:10.1021/bi00391a004

Cited by 187 publications

(93 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Briefly, 1 µg of total RNA was reverse transcribed by MuLV reverse transcriptase in the presence of random hexamer, followed by indicated cycles of PCR reaction (95°C for 1 min, 55°C for 1 min, and 72°C for 1 min) in the presence of 2 µM TF specific primers (30 cycles), VEGF specific primers (28 cycles), or the β-actin-specific primers (16 cycles) as a control. The TF primers were designed (Potgens et al, 1994), the reverse primer (5′-CAGTGCAATATAGCATTTGCAGTAGC-3′) is complementary to positions 1005-980, and the forward primer (5′-CTACT-GTTTCAGTGTTCAAGCAGTGA-3′) corresponds to positions 723-748 (Scarpati et al, 1987). The VEGF primers (Weindel et al, 1992) included the reverse primer (5′-CCTGGTGAGAGATCTG-GTTC-3′) spanning bases 861-842 and the forward primer (5′-TCGGGCCTCCGAAACCATGA-3′) spanning bases 141-160.…”

Section: Rna Isolation and Reverse Transcription Polymerase Chain Reamentioning

confidence: 99%

True

2000

Br J Cancer

View full text Add to dashboard Cite

Vascular endothelial growth factor (VEGF) is a potent angiogenic factor in human gliomas. VEGF-induced proteins in endothelial cells, tissue factor (TF), osteopontin (OPN) and α v β 3 integrin have been implicated as important molecules by which VEGF promotes angiogenesis in vivo. Sixty-eight gliomas were immunohistochemically stained with TF, VEGF, OPN and α v β 3 integrin antibody. Twenty-three tumours, six normal brains and nine glioma cell lines were evaluated for their mRNA expression of VEGF and TF by reverse transcription polymerase chain reaction analysis. The data indicated that TF as well as VEGF was a strong regulator of human glioma angiogenesis. First, TF expression in endothelial cells which was observed in 74% of glioblastomas, 54% of anaplastic astrocytomas and none of low-grade astrocytomas, correlated with the microvascular density of the tumours. Double staining for VEGF and TF demonstrated co-localization of these two proteins in the glioblastoma tissues. Second, there was a correlation between TF and VEGF mRNA expression in the glioma tissues. Third, glioma cell conditioned medium containing a large amount of VEGF up-regulated the TF mRNA expression in human umbilical vein endothelial cells. OPN and α v β 3 integrin, were also predominantly observed in the microvasculature of glioblastomas associated with VEGF expression. Microvascular expression of these molecules could be an effective antiangiogenesis target for human gliomas. © 2000 Cancer Research Campaign

show abstract

Section: Rna Isolation and Reverse Transcription Polymerase Chain Reamentioning

confidence: 99%

True

2000

Br J Cancer

View full text Add to dashboard Cite

show abstract

“…Similar synchrony induced by bradykinin was shown to depend on intercellular gap junctions. 2 These synchronous signals go on for more than 1 h and can be stopped by washing off the agonist (for FXa) or by adding an inhibitor of serine proteases (benzamidine). In contrast, thrombin-induced signals decay with time and disappear completely after 30 -45 min.…”

Section: Ca 2ϩ Signals Induced By Factors Viia and Xa In Mdck Cellsmentioning

confidence: 99%

“…The cloning of TF cDNA (1)(2)(3)(4) revealed that it was a member of the cytokine receptor superfamily (5). Binding of FVIIa to TF activates the protease and also induces Ca 2ϩ oscillations in several different cell types (6).…”

mentioning

confidence: 99%

Coagulation Factors VII and X Induce Ca2+ Oscillations in Madin-Darby Canine Kidney Cells Only When Proteolytically Active

Camerer¹,

Røttingen

Iversen

et al. 1996

Journal of Biological Chemistry

133

101

View full text Add to dashboard Cite

We have recently reported that the activated serine protease and blood coagulation Factor VII (FVIIa) can induce Ca 2؉ oscillations in Madin-Darby canine kidney cells. We now demonstrate a similar response by MadinDarby canine kidney cells to the active coagulation Factor X (FXa), which is also a serine protease and a substrate of the tissue factor (TF)⅐FVIIa complex in the initiation of the coagulation cascade. The phosphatidyl inositol-specific phospholipase C inhibitor U73122 inhibited the signals elicited by both FVIIa and FXa. Lack of sensibility to the tyrosine kinase inhibitors herbimycin A, genistein, and the tyrphostin AG18 and discordance between TF expression and FVIIa responsiveness argued against TF acting as a cytokine-like receptor, with tyrosine kinase-mediated activation by FVIIa. As demonstrated using the protease inhibitor benzamidine and by specific active site inhibition with 1,5-dansylGlu-Gly-Arg chloromethyl ketone, both FVIIa and FXa lost their ability to elicit a calcium response when devoid of their proteolytic activity. Consistent with this, the native (zymogen) form of Factor X did not induce Ca 2؉ transients. Homologous but not heterologous inhibition of FVIIa-and FXa-evoked Ca 2؉ signals by 1,5-dansyl-Glu-Gly-Arg chloromethyl ketone-inactivated FVIIa and FXa suggested that each factor had its own specific cell surface anchoring receptor. The two coagulation factors did not show homologous desensitization as seen for thrombin stimulation. Studies with hirudin excluded involvement of the established activation pathway through thrombin itself. Lack of desensitization of the response to FVIIa or FXa by thrombin ruled out any involvement of proteinase activated receptor-1 (PAR-1), the thrombin receptor. We speculate that FXa and FVIIa may work via a receptor (possibly common) analogous to PAR-1 or its functional homologue PAR-2. Although TF is essential for the FVIIa-induced signaling event, its role in the phosphatidyl inositol-specific phospholipase C-mediated Ca 2؉ signal may be in anchoring FVIIa to the cell surface rather than in transmembrane signal mediation.

show abstract

“…The normal, wildtype human TF cDNA is composed of 6 exons. 22 Another TF transcript, designated in this figure as TF-A, is a novel TF transcript containing exon IA and thus consists of 7 exons. A third TF transcript, TF-B, originally observed by van der Logt and coworkers 16 and confirmed in our study, is generated by inclusion of 955 bp of the first intron.…”

mentioning

confidence: 99%

Identification of a novel human tissue factor splice variant that is upregulated in tumor cells

Chand

Ness

Kisiel

2005

Intl Journal of Cancer

View full text Add to dashboard Cite

Tissue factor (TF) is a transmembrane glycoprotein that serves as the prime initiator of blood coagulation and plays a critical role in thrombosis and hemostasis. In addition, a variety of tumor cells overexpress cell-surface TF, which appears to be important for tumor angiogenesis and metastasis. To elucidate the mechanism involved in the upregulation of TF in human tumor cells, a comprehensive analysis of TF mRNA from various normal and tumor cells was performed. The results of these studies indicate that, in addition to possessing a normal full-length TF transcript and minor levels of an alternatively spliced transcript known as alternatively-spliced tissue factor (asTF) (Bogdanov et al., Nat Med 2003;9:458-62), human tumor cells express additional full-length TF transcripts that are also generated by alternative splicing. Reverse transcriptase-polymerase chain reaction (RT-PCR) and 5 0 -rapid amplification of cDNA ends-(5 0 -RACE) based analyses of cytoplasmic RNA from normal and tumor cells revealed that there is alternative splicing of the first intron between exon I and exon II resulting in 2 additional TF transcripts. One of the transcripts has an extended exon I with inclusion of most of the first TF intron (955 bp), while the second transcript is formed by the insertion of a 495 bp sequence, referred to as exon IA, derived from an internal sequence of the first intron. The full length TF transcript with alternatively spliced novel exon IA, referred to as alternative exon 1A-tissue factor (TF-A), represented~1% of the total TF transcripts in normal cells, but constituted 7-10% of the total TF transcript in tumor cells. Quantitative real-time RT-PCR analysis indicated that cultured human tumor cells contain 10-25-fold more copy numbers of TF-A in comparison to normal, untransformed cells. We propose that high-level expression of the novel TF-A transcript, preferentially in tumor cells, may have utility in the diagnosis and staging of a variety of solid tumors. ' 2005 Wiley-Liss, Inc.

show abstract

Human tissue factor: cDNA sequence and chromosome localization of the gene

Cited by 187 publications

References 36 publications

True

True

Coagulation Factors VII and X Induce Ca2+ Oscillations in Madin-Darby Canine Kidney Cells Only When Proteolytically Active

Identification of a novel human tissue factor splice variant that is upregulated in tumor cells

Contact Info

Product

Resources

About