Changes of Tissue Factor and Thrombomodulin Levels in Isolated Leukemic Cells from a Patient with Acute Promyelocytic Leukemia during All-trans Retinoic Acid Therapy

Oguchi, Atsushi; Morioka, Machiko; Obi, Naomi; Miyamoto, Hirofumi; Nishida, Junji; Kinoshita, Tadatoshi

doi:10.2491/jjsth.7.140

Jpn J Thromb Hemost

1996

DOI: 10.2491/jjsth.7.140

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Changes of Tissue Factor and Thrombomodulin Levels in Isolated Leukemic Cells from a Patient with Acute Promyelocytic Leukemia during All-trans Retinoic Acid Therapy

Atsushi Oguchi¹,

Machiko Morioka²,

Naomi Obi³

et al.

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2005

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“…We hypothesized that the PtdSer-anxA5 portal of cell entry may internalize membrane proteins that are embedded in the PtdSer-expressing membrane patch. A close interaction has been described for PtdSer and the coagulation protein tissue factor (TF) (13,14). TF, a 47-kDa transmembrane glycoprotein, is a member of the cytokine receptor superfamily that initiates blood coagulation by binding the coagulation factor VII in its non-activated (FVII) and activated form (FVIIa) (15).…”

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Annexin A5 Down-regulates Surface Expression of Tissue Factor

Ravassa

Bennaghmouch

Kenis

et al. 2005

Journal of Biological Chemistry

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Phosphatidylserine (PtdSer) is exposed on the external leaflet of the plasma membrane during apoptosis. The protein annexin A5 (anxA5) shows high affinity for PtdSer. When anxA5 binds to the PtdSer-expressing membranes during apoptosis, it crystallizes as an extended two-dimensional network and activates thereby a novel portal of cell entry that results in the internalization of the PtdSer-expressing membrane patches. This novel pathway of cell entry is potentially involved in the regulation of the surface expression of membrane receptors. In this study we report the regulation of surface expression of the initiator of blood coagulation tissue factor (TF) by this novel pathway of cell entry. AnxA5 induces the internalization of tissue factor expressed on the surface of apoptotic THP-1 macrophages. This down-regulation depends on the abilities of anxA5 to bind to PtdSer and to form a two-dimensional crystal at the membrane. We furthermore show that THP-1 cells produce and externalize anxA5 that cause the internalization of TF in an autocrine type of mechanism. We extended our in vitro work to the in vivo situation and show in a mouse model that anxA5 causes the downregulation of TF expression by smooth muscle cells of the media of the carotid artery that was mechanically injured. In conclusion, anxA5 down-regulates surfaceexpressed TF by activating the novel portal of cell entry. This mechanism may be part of a more general autocrine function of anxA5 to regulate the plasma membrane receptor repertoir under stress conditions associated with the surface expression of PtdSer.

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mentioning

confidence: 99%

Annexin A5 Down-regulates Surface Expression of Tissue Factor

Ravassa

Bennaghmouch

Kenis

et al. 2005

Journal of Biological Chemistry

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Changes of Tissue Factor and Thrombomodulin Levels in Isolated Leukemic Cells from a Patient with Acute Promyelocytic Leukemia during All-trans Retinoic Acid Therapy

Cited by 1 publication

References 27 publications

Annexin A5 Down-regulates Surface Expression of Tissue Factor

Annexin A5 Down-regulates Surface Expression of Tissue Factor

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