Kazumichi Furuyama

Kazumichi Furuyama

Department Of Molecular Biology And Applied Physiology, Tohoku University Graduate School Of Medicine, 2-1 Seiryo-Machi, Aoba-Ku, Sendai, Miyagi, 980-8575, Japan

Direct Impact

Concepts for which Kazumichi Furuyama has direct influence:

sideroblastic anemia
heme oxygenase
erythroid cells
alas2 gene
point mutation
ho-1 expression
mitochondrial import

External impact

Concepts related to the work of other authors for which Kazumichi Furuyama has influence:

heme oxygenase-1
iron uptake
erythroid differentiation
chorionic villi
tissue damage
alas2 gene
sideroblastic anemia

Prominent publications by Kazumichi Furuyama

KOL-Index: 50 Sideroblastic anemias are anemic disorders characterized by the presence of ring sideroblasts in a patient’s bone marrow. These disorders are typically divided into two types, congenital or acquired sideroblastic anemia. Recently, several genes were reported as responsible for congenital sideroblastic anemia; however, the relationship between the function of the gene products and ring ...
Known for
Ring Sideroblasts | Anemic Disorders | Sideroblastic Anemias | Patient’s Bone Marrow
KOL-Index: 31 Polyclonal B lymphocytosis was found in four patients having clinical and hematologic features resembling those of hairy cell leukemia (HCL). All four patients were women between 37 and 67 years of age. Three patients had splenomegaly. Lymphadenopthy was absent or slight. Persistent lymphocytosis was seen in all the patients, and anemia and/or thrombopenia was observed in three of the ...
Known for
Weak Tartrate-Resistant Acid Phosphatase | 37 67 | Hairy | Cd11c
KOL-Index: 25 Hypoxia induces expansion of erythroid precursor cells through erythropoietin production. However, it has also been suggested that hypoxia could enhance hemoglobin production in erythroid cells directly. To identify the molecules that are involved in hemoglobin production under hypoxia, we examined the expression profile of mRNAs in YN-1 human erythroleukemia cells under hypoxia. DNA array ...
Known for
Mitoferrin Mrna | Factor‐β Signaling | Induces Erythroid‐specific | Expression Alas2
KOL-Index: 25 Heme oxygenase cleaves heme to form biliverdin, carbon monoxide (CO), and iron, and consists of two structurally related isozymes, HO-1 and HO-2. HO-2 is also known as a potential oxygen sensor. Here we show that the relative CO content in arterial blood, which reflects the total amount of endogenous heme degradation, dynamically changes in mice during acclimatization to normobaric hypoxia ...
Known for
Potential Oxygen Sensor | Ho-1 Ho-2 Proteins | Acclimatization | 10 O2
KOL-Index: 24 Intracellular heme concentrations are maintained in part by heme degradation, which is catalyzed by heme oxygenase. Heme oxygenase consists of two structurally related isozymes, HO-1 and HO-2. Recent studies have identified HO-2 as a potential oxygen sensor. To gain further insights into the regulatory role of HO-2 in heme homeostasis, we analyzed the expression profiles of HO-2 and the ...
Known for
Exogenous Hemin | Biochemical Consequences | Structurally Isozymes | Siho-2
KOL-Index: 22 A novel missense mutation, A1754G, in exon 11 of the erythroid-specific delta-aminolaevulinate synthase gene (ALAS2) was identified in a Japanese male with sideroblastic anaemia. ALAS activity in bone marrow cells of the patient was reduced to 53.3% of the normal control. Consistent with this finding, activity of a bacterially expressed ALAS2 mutant protein harbouring this mutation was 19.5% ...
Known for
Sideroblastic | Bone Marrow Cells | Pyridoxal | A1754g
KOL-Index: 22 Erythroid-specific 5-aminolevulinate synthase (ALAS2) is essential for hemoglobin production, and a loss-of-function mutation of ALAS2 gene causes X-linked sideroblastic anemia. Human ALAS2 protein consists of 587 amino acids and its carboxyl(C)-terminal region of 33 amino acids is conserved in higher eukaryotes, but is not present in prokaryotic ALAS. We explored the role of this C-terminal ...
Known for
Region Alas2 | Half Vivo | Synthase Acts | Hemoglobin Production
KOL-Index: 21 (Pro)renin receptor ((P)RR), a specific receptor for renin and prorenin, is expressed in erythroblastic cells. (P)RR has multiple biological actions: prorenin activation, stimulation of the intracellular signaling including extracellular signal-regulated kinases, and functional complex formation with vacuolar H+-ATPase (v-ATPase). However, the functional implication of (P)RR in erythroblast ...
Known for
Erythropoiesis K562 | Vacuolar H-Atpase | Heme Synthesis | Mrna Increased
KOL-Index: 20 Alas2 encodes the erythroid-specific delta-aminolevulinate synthase (ALAS2 or ALAS-E), the first enzyme in heme biosynthesis in erythroid cells. Mice with the Alas2-null phenotype showed massive cytoplasmic, but not mitochondrial, iron accumulation in their primitive erythroblasts. Because these animals died by day 11.5 in utero, studies of iron metabolism in definitive erythroblasts were ...
Known for
Marked Deficiency | Heme Biosynthesis | Definitive Erythroblast | Alas2 Gene
KOL-Index: 18 Heme is an essential requirement for cell survival. Heme oxygenase (HO) is the rate-limiting enzyme in heme catabolism and consists of two isozymes, HO-1 and HO-2. To identify the protein that regulates the expression or function of HO-1 or HO-2, we searched for proteins that interact with both isozymes, using protein microarrays. We thus identified ...
Known for
Ho-2 Hepg2 | Pfkfb4 Protein | Coordinated Manner | Key Activator

Department of Molecular Biology and Applied Physiology, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai, Miyagi, 980-8575, Japan

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