Ruxolitinib changes the natural course of myelofibrosis and its transplant outcome.
Blood Research.2013;48(1):68-69. doi:10.5045/br.2013.48.1.68
Blood Research
1969 to Present ISSN: 2287-979X
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Many questions raised by a question on JAK1/2 inhibitors in primary myelofibrosis.
Blood Research.2013;48(1):67-67. doi:10.5045/br.2013.48.1.67
No abstract available.
Primary Myelofibrosis
Primary Myelofibrosis
New approaches for cholestasis in hemoglobinopathies.
Blood Research.2015;50(2):118-121. doi:10.5045/br.2015.50.2.118
Pseudo gray platelet syndrome: the first case report in Korea.
Blood Research.2015;50(2):117-118. doi:10.5045/br.2015.50.2.117
Prevalent factor XII deficiency in cancer patients with isolated aPTT prolongation.
Blood Research.2015;50(2):114-117. doi:10.5045/br.2015.50.2.114
Blood Research.2015;50(2):113-114. doi:10.5045/br.2015.50.2.113
Blood Research.2015;50(2):109-112. doi:10.5045/br.2015.50.2.109
BACKGROUND: The eosin-5'-maleimide (EMA) binding test using flow cytometry is a common method to measure reduced mean channel fluorescence (MCF) of EMA-labeled red blood cells (RBCs) from patients with red cell membrane disorders. The basic principle of the EMA-RBC binding test involves the covalent binding of EMA to lysine-430 on the first extracellular loop of band 3 protein. METHODS: In the present study, the MCF of EMA was analyzed for samples derived from 12 healthy volunteers (controls) to determine the stability (i.e., the percentage decrease in fluorescence) of EMA over a period of 1 year. RESULTS: Comparison of periodical MCF readings over time, that is, at 2-month intervals, showed that there were no significant changes in mean channel fluorescence for up to 6 months; however, there was a significant decrease in MCF at 8 months. CONCLUSION: For optimal dye utilization, EMA remained stable only for up to 6 months. Therefore, we recommend reconstitution of the dye every 6 months when implementing this test and storage at -80degrees C in dark conditions.
Anion Exchange Protein 1, Erythrocyte ; Cell Membrane* ; Erythrocytes ; Flow Cytometry ; Fluorescence ; Healthy Volunteers ; Humans ; Reading
Anion Exchange Protein 1, Erythrocyte ; Cell Membrane* ; Erythrocytes ; Flow Cytometry ; Fluorescence ; Healthy Volunteers ; Humans ; Reading
Human coagulation factor VIII domain-specific recombinant polypeptide expression.
Blood Research.2015;50(2):103-108. doi:10.5045/br.2015.50.2.103
BACKGROUND: Hemophilia A is caused by heterogeneous mutations in F8. Coagulation factor VIII (FVIII), the product of F8, is composed of multiple domains designated A1-A2-B-A3-C1-C2. FVIII is known to interact with diverse proteins, and this characteristic may be important for hemostasis. However, little is known about domain-specific functions or their specific binding partners. METHODS: To determine F8 domain-specific functions during blood coagulation, the FVIII domains A1, A2, A3, and C were cloned from Hep3B hepatocytes. Domain-specific recombinant polypeptides were glutathione S-transferase (GST)- or polyhistidine (His)-tagged, over-expressed in bacteria, and purified by specific affinity chromatography. RESULTS: Recombinant polypeptides of predicted sizes were obtained. The GST-tagged A2 polypeptide interacted with coagulation factor IX, which is known to bind the A2 domain of activated FVIII. CONCLUSION: Recombinant, domain-specific polypeptides are useful tools to study the domain-specific functions of FVIII during the coagulation process, and they may be used for production of domain-specific antibodies.
Antibodies ; Bacteria ; Blood Coagulation ; Chromatography, Affinity ; Clone Cells ; Factor IX ; Factor VIII* ; Glutathione Transferase ; Hemophilia A ; Hemostasis ; Hepatocytes ; Humans ; Peptides
Antibodies ; Bacteria ; Blood Coagulation ; Chromatography, Affinity ; Clone Cells ; Factor IX ; Factor VIII* ; Glutathione Transferase ; Hemophilia A ; Hemostasis ; Hepatocytes ; Humans ; Peptides
Blood Research.2015;50(2):97-102. doi:10.5045/br.2015.50.2.97
BACKGROUND: Few clinical studies have clarified the prognostic factors that affect clinical outcomes for patients with relapsed or refractory diffuse large B-cell lymphoma (DLBCL) after immunochemotherapy. METHODS: A total of 158 patients with relapsed or refractory DLBCL were enrolled. All patients underwent positron emission tomography/computed tomography (PET/CT) before and after salvage therapy. All enrolled patients previously received the ifosfamide, carboplatin, and etoposide regimen. Clinical outcomes were compared according to several factors (age > or = 65 years, low age-adjusted International Prognostic Index [aa-IPI], maximum standardized uptake value [SUVmax] <6.0 on PET/CT, time to relapse > or =12 months, complete response after salvage therapy). A low aa-IPI, SUVmax <6.0, and time to relapse > or = 12 months were independent prognostic factors for survival. RESULTS: In univariate analysis and multivariate analysis, SUVmax below 6.0 (P<0.001 for progression-free survival (PFS), P<0.001 for overall survival (OS)) and low aa-IPI (P<0.001 for PFS, P<0.001 for OS) were independent prognostic factors associated with favorable outcome. CONCLUSION: The aa-IPI and initial SUVmax were powerful prognostic factors in patients with relapsed or refractory DLBCL.
Carboplatin ; Disease-Free Survival ; Electrons* ; Etoposide ; Humans ; Ifosfamide ; Lymphoma, B-Cell* ; Multivariate Analysis ; Positron-Emission Tomography ; Positron-Emission Tomography and Computed Tomography ; Recurrence ; Salvage Therapy
Carboplatin ; Disease-Free Survival ; Electrons* ; Etoposide ; Humans ; Ifosfamide ; Lymphoma, B-Cell* ; Multivariate Analysis ; Positron-Emission Tomography ; Positron-Emission Tomography and Computed Tomography ; Recurrence ; Salvage Therapy
Bortezomib inhibits the survival and proliferation of bone marrow stromal cells.
Blood Research.2015;50(2):87-96. doi:10.5045/br.2015.50.2.87
BACKGROUND: Bortezomib is widely used for the treatment of multiple myeloma. Bone marrow stromal cells (BMSCs) endow myeloma cells with survival and growth advantages. However, the influence of bortezomib on BMSCs is not well elucidated. We examined the effects of bortezomib on the survival and growth of BMSCs in vitro. METHODS: The effects of bortezomib on the survival and proliferation of the BMSC MS-5 cell line and on BMSCs obtained from healthy individuals (N=4) and newly diagnosed myeloma patients (N=5) were investigated in vitro. Transmembrane cell migration was evaluated using the Transwell system. A short interfering RNA strategy was used to knock down the expression of chemokine (CXC motif) ligand 12 (CXCL12) mRNA. To examine the effects of bortezomib-exposed BMSCs on the migration and localization of myeloma cells, MS-5 monolayers were treated with bortezomib for 24 hr, washed, and then overlaid with human RPMI8226 myeloma cells. RESULTS: Bortezomib inhibited BMSC proliferation in a concentration-dependent manner, and induced cellular apoptosis. Bortezomib decreased CXCL12 production by BMSCs. Knockdown of CXCL12 mRNA in BMSCs revealed that CXCL12 served as an autocrine growth factor. Short-term bortezomib treatment of BMSC monolayers reduced the tendency of myeloma cells to locate to positions under the monolayers. CONCLUSION: Bortezomib inhibits the survival and growth of BMSCs via downregulation of CXCL12, which may contribute to the clinical effects of this agent.
Apoptosis ; Cell Line ; Cell Movement ; Down-Regulation ; Humans ; Mesenchymal Stromal Cells* ; Multiple Myeloma ; RNA, Messenger ; RNA, Small Interfering ; Bortezomib
Apoptosis ; Cell Line ; Cell Movement ; Down-Regulation ; Humans ; Mesenchymal Stromal Cells* ; Multiple Myeloma ; RNA, Messenger ; RNA, Small Interfering ; Bortezomib
Country
Republic of Korea
Publisher
Korean Society of Hematology; Korean Society of Blood and Marrow Transplantation; Korean Society of Pediatric Hematology-Oncology; Korean Society on Thrombosis and Hemostasis
ElectronicLinks
http://synapse.koreamed.org/LinkX.php?code=3072BREditor-in-chief
Seog-Woon Kwon
journal@bloodresearch.or.kr
Abbreviation
Blood Res
Vernacular Journal Title
ISSN
2287-979X
EISSN
2288-0011
Year Approved
2007
Current Indexing Status
Currently Indexed
Start Year
1969
Description
Blood Research is a peer-reviewed open-access journal and delivers important clinical, translational and basic research results in hematology to the readers worldwide. The research areas covered by Blood Research include hematopoiesis, stem cell biology, stem cell transplantation, thrombosis, hemostasis, hematologic malignancy, pediatric hematology, laboratory hematology, immunohematology, transfusion medicine, immunology, and other hematology-related fields. Blood Research publishes Original Articles, Review Articles, Editorials, Perspectives, Letters to the Editor, and Images of Hematology. It is published online (http://bloodresearch.or.kr) and in print quarterly (March 31, June 30, September 30, and December 31). Any physicians or researchers throughout the world can submit a manuscript written in English.
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