Tissue Factor Expression during Monocyte-Macrophage Differentiation

Eijnden, Mark M. E. D. van den; Steenhauer, S. I.; Reitsma, Pieter H.; Bertina, R. M.

doi:10.1055/s-0038-1656125

Cited by 29 publications

(32 citation statements)

References 34 publications

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“…Whole HMDM lysates were subjected to SDS-PAGE under reducing conditions and probed for expression of annexin II and CD71, a macrophage marker not expressed on monocytes ( Figure 5A). 41,42 CD71 was expressed by monocyte/macrophages in only trace amounts on day 5, but increased 6.5-fold in intensity by day 15. At the same time, there was a 2.7-fold increase in total cellular annexin II.…”

Section: Annexin II Expression Is Enhanced On Monocyte Differentiationmentioning

confidence: 96%

Annexin II mediates plasminogen-dependent matrix invasion by human monocytes: enhanced expression by macrophages

Brownstein

Deora

Jacovina

et al. 2004

Blood

110

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Monocytes and macrophages participate in a wide variety of host defense mechanisms. Annexin II, a fibrinolytic receptor, binds plasminogen and tissue plasminogen activator (t-PA) independently at the cell surface, thereby enhancing the catalytic efficiency of plasmin production. We demonstrated previously that annexin II on the surface of both cultured monocytoid cells and monocyte-derived macrophages promotes their ability to remodel extracellular matrix. Here, we demonstrate that human peripheral blood monocytes represent the major circulating annexin II-expressing cell. Annexin II supported t-PA-dependent generation of cell surface plasmin and the matrixpenetrating activity of human monocytes. Compared to polymorphonuclear leukocytes, monocytes supported a 12.9-fold greater rate of plasmin generation in the presence of exogenous t-PA, and this activity was largely attributable to annexin II. Likewise, anti-annexin II IgG directed against the t-PA-binding tail domain inhibited plasminogen-dependent, cytokine-directed monocyte migration through extracellular matrix. On differentiation of monocytes to macrophages, there was a 2.4-fold increase in annexin II-specific mRNA, and a 7.9-fold increase in surface annexin II. Thioglycolate-elicited peritoneal macrophages, furthermore, displayed an additional 3.8-fold increase in annexin II surface expression compared with resident cells. Thus, annexin II-mediated assembly of plasminogen and t-PA on monocyte/macrophages contributes to plasmin generation, matrix remodeling, and directed migration. IntroductionAnnexin II belongs to a family of widely distributed, phospholipidbinding, calcium-regulated, peripheral membrane proteins known as the annexins. 1 Annexin II is richly expressed in the epithelial cells of intestine and lung and is also found on the cell surface of vascular endothelial cells, myelomonocytic leukemia cells, 2 and cells of several monocyte-like lines. 3 Through the expression of independent binding sites for both plasminogen and tissue plasminogen activator (t-PA), annexin II assembles these 2 proteins on the cell surface, thereby accelerating the production of plasmin. 4 Kinetic studies indicate that annexin II enhances the catalytic efficiency (k cat /K m ) of t-PA-dependent plasminogen activation by 60-fold, 5 suggesting that endothelial cell surface generation of plasmin likely contributes to fibrinolytic surveillance, thereby promoting blood vessel patency.Monocytes and macrophages are large, motile, phagocytic cells that have a wide range of biosynthetic and secretory activities depending on their exposure to local stimuli and mediators. 6 They participate routinely in host defense mechanisms, including antigen presentation and clearance of debris, and contribute critically to acute and chronic inflammatory responses, pathogen clearance, and wound healing. 7,8 In many pathologic processes, such as atherosclerosis or disorders of lipid metabolism, furthermore, lipid-laden macrophages accumulate in tissues. 9 The monocyte/macrophage, moreover, ma...

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Section: Annexin II Expression Is Enhanced On Monocyte Differentiationmentioning

confidence: 96%

Annexin II mediates plasminogen-dependent matrix invasion by human monocytes: enhanced expression by macrophages

Brownstein

Deora

Jacovina

et al. 2004

Blood

110

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“…During this process, the cells temporarily express a relatively low level of TF. Expression peaks at day 4 of culture (21). The results in Table 5 also shows that these low levels are detected with ease using the NASBA procedure that shows a 1 log increase of expression.…”

Section: Tf and Cd14 Expression During A Long-term Culture Of Human Mmentioning

confidence: 85%

“…Monocytes were isolated from five human donors and were cultured on Teflon membranes as described in van den Eijnden et al (21). We used a series of RNA preparations sampled at various time points during a 13 day culture of human monocytes in suspension, during which period the cells differentiate into macrophages.…”

Section: Monocyte Isolation From Whole Blood and Culture Conditionsmentioning

confidence: 99%

“…Total RNA from monocytes was purified as described by van den Eijnden et al (21). RNA aliquots (~5 µg) were stored under ethanol at -70°C.…”

Section: Rna Isolation From Isolated Monocytes and Northern Blottingmentioning

confidence: 99%

“…Next the nucleic acid suspensions were diluted 100-fold in water, and 5 µl of these dilutions were used per NASBA reaction. Northern blot analysis was essentially as described in van den Eijnden et al (21).…”

Section: Rna Isolation From Isolated Monocytes and Northern Blottingmentioning

confidence: 99%

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A novel quantitative multiplex NASBA method: application to measuring tissue factor and CD14 mRNA levels in human monocytes

Deursen¹,

Gunther²,

Riel

et al. 1999

Nucleic Acids Research

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A new method to quantify two individual mRNAs in a single NASBA reaction is described. In this study, tissue factor and CD14 mRNAs were used as a model system. RNA ratios of -4 to +4 log units were determined with good precision (within 0.3 log) and accuracy (within 0.2 log). By measuring both mRNAs in human monocytes that were stimulated with LPS, the multiplex Q-NASBA proved to be a successful tool to monitor the expression levels of two individual mRNAs in a single-tube amplification system. The method has potential in all fields in which quantitative information is needed on two individual RNAs.

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The biology and tumour-related properties of monocyte tissue factor

Lwaleed

Bass²,

Cooper³

2001

J. Pathol.

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Tissue factor (TF, coagulation factor III, CD142) is not only the main physiological initiator of normal blood coagulation, but is also important in the natural history of solid malignancies in that it potentiates metastasis and angiogenesis and mediates outside-in signalling. TF is expressed constitutively by many tissues which are not in contact with blood and by other cells upon injury or activation; the latter include endothelial cells, tissue macrophages, and peripheral blood monocytes. It can exist encrypted and unavailable functionally in the plasma membrane and the appearance of functional TF may be due to synthesis and/or de-encryption. Inflammatory cells often express TF and act to induce its production or de-encryption by other cells locally and, apparently, at remote sites. Inappropriate expression of TF by endothelial cells, macrophages or monocytes is thought to be an important trigger of coagulation in various pathological conditions. Several studies have shown that measurements of monocyte TF (mTF) may provide clinically significant information, particularly in patients with malignant and inflammatory diseases.

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Tissue Factor Expression during Monocyte-Macrophage Differentiation

Cited by 29 publications

References 34 publications

Annexin II mediates plasminogen-dependent matrix invasion by human monocytes: enhanced expression by macrophages

Annexin II mediates plasminogen-dependent matrix invasion by human monocytes: enhanced expression by macrophages

A novel quantitative multiplex NASBA method: application to measuring tissue factor and CD14 mRNA levels in human monocytes

The biology and tumour-related properties of monocyte tissue factor

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