Publications by authors named "Hibi M"

Tec/Btk tyrosine kinases are members of a subgroup of Src tyrosine kinase family. They are reported to be activated in response to cytokines, such as IL-3 and IL-6. Janus kinases (JAKs) are known to associate with certain cytokine receptors, e.

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CD40-mediated signals can induce cell aggregation, proliferation and rescue from apoptosis in WEHI231. To define which segment of cytoplasmic domain of CD40 and how signals are involved in those events, we generated mutant CD40 transfectants. We demonstrated the same 10 amino acid segment that could bind to tumor necrosis factor receptor associated factor-2 and -3 mediated all those responses.

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The pattern of changes in leukocyte counts and the blood concentration of G-CSF were observed in 15 patients undergoing aortocoronary bypass surgery. Myelopoietic function was assessed by examining the myelogram and performing flow cytometry to identify human leukocyte differentiation antigens on bone marrow aspirates obtained from the sternum when opening and closing the sternotomy. The blood concentration of G-CSF increased gradually after removal of the aortic cross clamp and peaked on the first postoperative day (232 +/- 98 ngml).

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Currently, poststernotomy mediastinitis frequently is being treated by debridement and immediate closure with omental drainage. This method is useful, but subcutaneous infection occasionally occurs. Divided omental transfer to the presternal space may be helpful in preventing this complication.

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JAK is believed to be an essential tyrosine kinase that mediates signals from the cytokine receptor to its downstream events. JAK associates with the cytoplasmic domain of the type I cytokine receptor superfamily and upon the ligand stimulation it can be activated, resulting in the receptor phosphorylation. In signaling from gp130, a common signal transducer for the IL-6 family cytokines, STAT3, a transcription factor that contains an SH2 domain, is recruited by phosphotyrosines on gp130 and is subsequently phosphorylated by gp130-associated JAKs.

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It was found that Syk protein-tyrosine kinase is rapidly activated in B cells after H2O2 treatment (oxidative stress) or increased extracellular NaCl concentration (osmotic stress) as well as in response to B cell receptor activation. In this study we examined the involvement of Syk in responses elicited by these types of extracellular stress, particularly Ca2+ responses and c-Jun amino-terminal kinase (JNK) activation, using a chicken B cell line, DT40, as well as the DT40-derived mutant DT40/Syk(-), which does not express Syk. Osmotic stress evokes increases in [Ca2+]i by stimulating an extracellular Ca2+ influx in both DT40 and DT40/Syk(-) cells.

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Vav is a hematopoietic cell-specific proto-oncogene. We show that interleukin-6 (IL-6) induces transient tyrosine phosphorylation of Vav in a human myeloma cell line, U266. A membrane-distal part of the cytoplasmic region of gp130 is critical for association between Vav and gp130, and the IL-6-induced tyrosine phosphorylation of Vav.

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We report herein the unusual case of a patient in whom postoperative angiography following coronary artery bypass grafting (CABG) revealed a lateral origin of the right internal thoracic artery (ITA) and a normal origin of the left ITA, both of which were demonstrated to be patent and did not follow a tortuous course. The CABG had involved revascularization of the left anterior descending artery (LAD) with the right ITA, and the obtuse marginal artery with the left ITA. The patient had an uneventful postoperative course and developed no respiratory symptoms.

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We report two cases of coronary artery bypass grafting following radical mastectomy using bilateral internal thoracic arterial grafts. One was a 68-year-old woman with angina pectoris, and the other was a 71-year-old woman with old myocardial infarction. Dissection of the internal thoracic arterial pedicles from the chest wall was not so difficult in both cases.

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Structurally related serine/threonine kinases recognize similar phosphoacceptor peptides in vitro yet in vivo, they phosphorylate distinct substrates. To understand the basis for this specificity, we studied the interaction between the Jun kinases (JNKs) and Jun proteins. JNKs phosphorylate c-Jun very efficiently, JunD less efficiently, but they do not phosphorylate JunB.

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We treated four cases with mediastinitis after coronary artery bypass grafting using the right gastroepiploic artery. These four patients were treated with the pedicled omentum. Omental transfer was successful in three cases.

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gp130 is a common signal transducer for the interleukin-6-related cytokines. To delineate the gp130-mediated growth signal, we established a series of pro-B cell lines expressing chimeric receptors composed of the extracellular domain of the granulocyte colony-stimulating factor receptor and the transmembrane and cytoplasmic domains of gp130. The second tyrosine (from the membrane) of gp130, which was required for the tyrosine phosphorylation of SHP-2, its association with GRB2, and activation of a MAP kinase, was essential for mitogenesis, but not for anti-apoptosis.

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Reimplantation of all intercostal arteries was performed with a T-shaped graft for spinal cord protection in a 64-year-old man who required long-segment replacement of the descending thoracic aorta. The T-shaped graft maintained blood flow to the intercostal arteries, and no neurologic deficits developed.

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Background: Nafamostat mesilate (FUT-175) is a synthetic serine protease inhibitor that inactivates coagulation, fibrinolysis, and platelet aggregation. Nafamostat mesilate may suppress the blood-foreign surface reaction similar to biocompatible materials by blocking factor XIIa.

Methods: We performed an in vitro study of cardiopulmonary bypass (CPB) with fresh human blood among the following three groups: standard CPB sets (C), biocompatible CPB sets (B), and standard CPB sets with FUT-175 (10 mg/L) (F).

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The Jun proteins are nuclear proteins that combine with Fos proteins to form a gene-regulatory protein, AP-1. They have highly conserved DNA-binding and dimerization domains, resulting in almost identical sequence-recognition properties. Nevertheless, there are many indications that each Jun protein activates a distinct and only partially overlapping set of AP-1 target genes.

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Interleukin-6 (IL-6) induces either differentiation or growth of a variety of cells. Little is known about the molecular basis of this cellular decision. The family of signal transducer and activator of transcription (Stat) proteins are involved in signaling through a variety of cytokine and growth factor receptors, although their biological roles have not been established.

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Interleukin-6 (IL-6) induces growth arrest and macrophage differentiation through its receptor in a murine myeloid leukaemic cell line, M1, although it is largely unknown how the IL-6 receptor generates these signals. By using chimeric receptors consisting of the extracellular domain of growth hormone receptor and the transmembrane and cytoplasmic domain of gp130 with progressive C-terminal truncations, we showed that the membrane-proximal 133, but not 108, amino acids of gp130 could generate the signals for growth arrest, macrophage differentiation, down-regulation of c-myc and c-myb, induction of junB and IRF1 and Stat3 activation. Mutational analysis of this region showed that the tyrosine residue with the YXXQ motif was critical not only for Stat3 activation but also for growth arrest and differentiation, accompanied by down-regulation of c-myc and c-myb and immediate early induction of junB and IRF1.

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We herein report the case of a 56-year-old man with idiopathic thrombocytopenic purpura who required an emergency aortic arch replacement. Intraoperatively, hemostasis was achieved using platelet transfusions. Postoperatively, the use of high-dose gamma-globulin therapy was able to maintain an adequate platelet count and good hemostasis.

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The interleukin 6 (IL-6) cytokine family, which includes IL-6, leukemia inhibitory factor (LIF), oncostatin M (OSM), ciliary neurotrophic factor (CNTF), IL-11 and cardiotrophin-1 (CT-1), exhibits pleiotropy and redundancy in biological activities. The IL-6 family cytokines exhibit a helical structure. Their receptors belong to the type 1 cytokine receptor family.

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The heterotrimeric G protein, G alpha i2, transduces signals from seven membrane spanning receptors to effectors such as adenylyl cyclase and ion channels. The purpose of this study was to identify these or other cellular proteins that interact with G alpha i2 by use of the yeast two-hybrid system. A human B cell cDNA library was screened by this system using full length G alpha i2.

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Twelve cases of malignant tumor (mean age 64 years) underwent the cardiac operation. The procedure of cardiac operations were 10 coronary artery bypass grafting and 2 mitral valve replacement. The detail of malignant tumors were 4 gastric cancer, 3 colon cancer, 3 lung cancer, 1 esophageal cancer and 1 lip cancer.

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Mitral valve replacement was performed through a right thoracotomy using femorofemoral bypass under profound systemic hypothermia in a 62-year-old man who had undergone coronary artery bypass grafting using both internal thoracic arteries. The right thoracotomy approach minimizes the risk of injury to the arterial grafts, and deep hypothermia obviates the need to interrupt the grafts to administer cardioplegia. This technique provides excellent exposure of the mitral valve while minimizing the operative risk.

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We reported a case of left atrial myxoma in advanced age. The case was eighty years old man. He admitted with congestive heart failure.

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Protein phosphorylation is commonly used to modulate transcription factor activity. However, all existing genetic evidence for stimulation of transcription factor activity by phosphorylation rests on loss-of-function mutations. To demonstrate conclusively that phosphorylation of a transcription factor potentiates its transactivation potential in vivo, we constructed a c-Jun mutant that is phosphorylated by the cAMP-sensitive protein kinase A (PKA) instead of the UV- and Ras-responsive protein kinase JNK.

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Nafamostat mesilate (FUT-175) is a protease inhibitor, working as an inactivator of coagulation, fibrinolysis and platelet aggregation. Although FUT-175 directly blocks contact factors in coagulation, it also may decrease activation of humoral cascade systems when used in cardiopulmonary bypass circuits. We performed an in vitro study using fresh human blood in the following cardiopulmonary bypass circuits: standard circuit (C), biosurfaced circuit (B) and standard circuit containing FUT-175 (F).

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