Search PubMed⌕ Search

Biomedical subjects

T Itano

Publications and source records attributed to T Itano.

At least 91 records · Page 5Linked to original sources
PubMed1989

Demonstration of different regional distributions of calcineurin subunits using monoclonal antibodies.

Immunohistochemical localizations of calcineurin subunits A (60 KDa) and B (20 KDa) were examined in a rat brain using subunit specific monoclonal antibodies. The immunoreactivity of the subunit A was abundant in the hippocampus, in the striatum, and in the thalamus, but weak in the neocortex. On the contrary, the immunoreactivity of the subunit B was more abundant in the cortex, and it was more ubiquitous than subunit A. The distribution of subunit A in the rat brain very well agreed with that of zinc, which is an intrinsic metal ion and a potent inhibitor of calcineurin phosphatase.

Animals↗
PubMed1989

The role of Ca2+ and protein kinase C in the differentiation of HL-60 cells induced by 1 alpha,25(OH)2D3 and diltiazem.

The roles of calcium (Ca2+) and protein kinase C in the differentiation of HL-60 cells induced by 1 alpha,25(OH)2D3 (D3) and/or a Ca2+ antagonist, diltiazem(D-cis, L-cis), were elucidated. D3 and diltiazem (100 microM) inhibited cell proliferation, and diltiazem enhanced the D3-induced differentiation. There was no difference in potency between the two isomers of diltiazem in the enhancing activity, in spite of their different pharmacological activity. The concentration of free Ca2+ in the HL-60 cells following D3 and/or diltiazem treatment significantly increased. A protein kinase C inhibitor, H-7, inhibited the phenotypic differentiation induced by D3. These results suggest that Ca2+ and protein kinase C play an important role in the differentiation of HL-60 cells induced by D3 and diltiazem.

Calcitriol↗
PubMed1987

A possible role for calmodulin in Ca2+-induced swelling of mitochondria.

Ca2+-induced mitochondrial swelling was inhibited by a low concentration of calmodulin antagonists. Two affinities of Ca2+ to mitochondrial swelling were observed: high (2-5 microM) and low (more than 100 microM) systems. The high-affinity change was inhibited by micromolar level of trifluoperazine and W-7, but not by W-5. The possible mechanism of this inhibition and the role of CaM in mitochondria are discussed.

Animals↗
PubMed1986

Identification of calmodulin-binding proteins in pure mitochondria by photoaffinity labeling.

Calmodulin-binding proteins (CaM-BPs) were identified in the submitochondrial fractions obtained from highly purified rat liver mitochondria. The matrix fraction contained five CaM-BPs with apparent molecular weights (MW) of 27K, 38K, 47K, 76K, and 84K Da in a Ca solution. Electron transfer particles also contained five CaM-BPs, but their MWs were 31K, 35K, 53K, 66K, and 73K in a Ca solution. Nonspecific calcium-independent CaM-BPs were also identified in matrix fractions, having MWs of 10K, 25K, and 49K Da.

Animals↗
PubMed1985

A direct evidence of the localization of mitochondrial calmodulin.

The presence and localization of mitochondrial calmodulin was directly proved immuno-electron microscopically by the protein A-gold technique. In the ultra-pure mitochondria the complexes of anti-calmodulin antibody and protein A-gold clearly showed the localization of mitochondrial calmodulin on the inner membrane and in the matrix space.

Animals↗
PubMed1984

Cell-cycle-dependent changes of the negative surface charges in L929 cells.

The negative charges of cell surface were studied by the adsorption method of methylene blue in the synchronized cultures of L929 cells and its spontaneously transformed cell strain. The negative surface charges of the transformed cells were twice those of the original cells through all cell cycle phases. The surface charges cell-cycle-dependently changed in both cell systems and there were two maximum peaks at early G1 and S phase.

Animals↗
PubMed1982

Purification of the Ca2+-and Mg2+-requiring ATPase from rat brain synaptic plasma membrane.

A Ca2+-ATPase (Ca2+- and Mg2+-requiring ATPase) was purified from a synaptic plasma-membrane fraction of rat brain. This enzyme had properties similar to those of plasma-membrane Ca2+-ATPases from other organs: its splitting of ATP was dependent on both Ca2+ and Mg2+, it bound in a Ca2+-dependent fashion to calmodulin-Sepharose and it cross-reacted with specific antibodies raised against human erythrocyte-membrane Ca2+-ATPase. It had an apparent Mr of 138 000, similar to those of plasma-membrane ATPases from human erythrocyte and from dog heart sarcolemma. Previous high-Ca2+-affinity ATPases observed in brain had Mr 100 000; in at least one case, such an ATPase probably represented a different type of enzyme, derived from coated vesicles.

Animals↗