Molecular cloning of mouse β2-glycoprotein I and mapping of the gene to chromosome 11

Matsuda, Yoichi; Shiroishi, Toshihiko; Moriwaki, Kazuo; Nonaka, Manabu; Natsuume‐Sakai, Shunnosuke

doi:10.1016/0888-7543(92)90022-k

Cited by 28 publications

(22 citation statements)

References 20 publications

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“…Furthermore, anti-␤ 2 -GP1 antibodies have also been indirectly implicated in the pathogenesis of thrombosis in in vitro systems. We predicted that, based on the marked sequence homology between human and mouse ␤ 2 -GP1, [21][22][23] human anti-␤ 2 -GP1 autoantibodies would recognize mouse ␤ 2 -GP1, thus justifying a mouse model of thrombosis. Furthermore, antiphospholipid autoantibodies derived from patients with antiphospholipid syndrome were previously shown to react equivalently with human and mouse ␤ 2 -GP1.…”

Section: Resultsmentioning

confidence: 99%

β2-glycoprotein-1 autoantibodies from patients with antiphospholipid syndrome are sufficient to potentiate arterial thrombus formation in a mouse model

Arad

Proulle

Furie

et al. 2011

Blood

126

101

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Antiphospholipid syndrome is characterized by thrombosis, recurrent fetal loss, and the presence of the lupus anticoagulant, anticardiolipin antibodies, or anti–β2-glycoprotein-1 (anti–β2-GP1) antibodies. Although anti–β2-GP1 antibodies have been documented as a biomarker for diagnosis of antiphospholipid syndrome, their direct role in the pathogenesis of thrombosis is unknown. We have demonstrated using intravital microscopy that anti–β2-GP1 autoantibodies purified from the sera of patients with antiphospholipid syndrome complicated by thrombosis greatly amplify thrombus size after laser-induced vessel wall injury in live mice. Anti–β2-GP1 autoantibodies from 3 patients with antiphospholipid syndrome were affinity-purified using human β2-GP1 bound to agarose. The effects of purified anti–β2-GP1 IgG autoantibodies, of anti–β2-GP1–depleted IgG, and of IgG from normal human sera on thrombus formation were measured in mice after arterial injury in the cremaster muscle. Before injury, purified anti–β2-GP1 IgG autoantibodies, anti–β2-GP1 antibody–depleted IgG, or IgG from normal human sera were infused. Increasing amounts of purified anti–β2-GP1 autoantibodies increased thrombus size in a dose-dependent manner, whereas neither anti–β2-GP1 antibody-depleted IgG nor IgG from normal serum affected thrombus size. These results indicate that anti–β2-GP1 IgG autoantibodies in antiphospholipid syndrome patient sera are not only a marker of antiphospholipid syndrome but are directly involved in the pathogenesis of thrombosis.

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Section: Resultsmentioning

confidence: 99%

β2-glycoprotein-1 autoantibodies from patients with antiphospholipid syndrome are sufficient to potentiate arterial thrombus formation in a mouse model

Arad

Proulle

Furie

et al. 2011

Blood

126

101

View full text Add to dashboard Cite

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“…However, the physiological function of APO-H is not well understood. Nonaka et al reported that the mRNA expression of APO-H was detected in the liver, but not in the kidney, heart, spleen, lung or brain (Nonaka et al, 1992). We detected the APO-H gene expression in STIL-C5-CM stimulated bone marrow by nested-PCR (Fig.…”

Section: Discussionmentioning

confidence: 85%

“…While the purified NIL-3 was homologous with bovine APO-H, there was a possibility that the NIL-3 might also be homologous with murine APO-H, because only a single amino acid difference existed in the first 8 amino acids of murine APO-H, which were GRICPKPD (Nonaka et al, 1992). Therefore, we performed nested-PCR to investigate the gene expression of murine APO-H in bone marrow cells.…”

Section: Pcr Analysismentioning

confidence: 99%

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Identification of Negative Regulator of Interleukin-3 (NIL-3) in Bone Marrow.

Adachi

Sugimoto²,

Sato³

et al. 2002

Cell Struct. Funct.

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ABSTRACT. We have reported that an inhibitor of interleukin-3 (NIL-3) is produced from murine bone marrow cells in response to excess stimulation of interleukin-3. In this report, we attempted the purification of the NIL-3 activity from bone marrow culture supernatant in the presence of interleukin-3. The purified NIL-3 activity was a protein with relative molecular weight of 54.5 kDa (SDS-PAGE), which inhibited the growth of IL-3 dependent DA-1 cell growth in a dose dependent manner. The N-terminal amino acid sequence of purified NIL-3 activity was determined to be homologous to beta-2 glycoprotein I (apolipoprotein H: APO-H). The gene expression of APO-H was detected by nested-PCR in STIL-3 C5-CM stimulated total bone marrow cells and STIL-3 C5-CM stimulated bone marrow fraction 2 (Fr. 2) which has been reported as a hematopoietic stem cell rich fraction. These observations indicate the possibility that the APO-H is the NIL-3 which was produced from bone marrow cells in response to excess IL-3 stimuli.

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“…␤ 2GPI strongly binds to anionic phospholipids; the fifth sushi domain (domain V) being the major phospholipid-binding region (5)(6)(7)(8)(9). The high structural homology among the human, bovine, rat, and mouse ␤ 2GPI molecules suggests that ␤ 2GPI might play an important physiological role in vivo (10). ␤ 2GPI exhibits anticoagulant properties in vitro, such as the inhibition of the intrinsic blood coagulation pathway (11,12), and the prothrombinase activity of activated platelets (13).…”

mentioning

confidence: 99%

Anti-beta2-glycoprotein I (beta2GPI) monoclonal antibodies with lupus anticoagulant-like activity enhance the beta2GPI binding to phospholipids.

et al. 1997

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Molecular cloning of mouse β2-glycoprotein I and mapping of the gene to chromosome 11

Cited by 28 publications

References 20 publications

β2-glycoprotein-1 autoantibodies from patients with antiphospholipid syndrome are sufficient to potentiate arterial thrombus formation in a mouse model

β2-glycoprotein-1 autoantibodies from patients with antiphospholipid syndrome are sufficient to potentiate arterial thrombus formation in a mouse model

Identification of Negative Regulator of Interleukin-3 (NIL-3) in Bone Marrow.

Anti-beta2-glycoprotein I (beta2GPI) monoclonal antibodies with lupus anticoagulant-like activity enhance the beta2GPI binding to phospholipids.

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