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- 저자 : B. O'Leary (검색결과 4 건)
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Lhx2 regulates bone remodeling in mice by modulating RANKL signaling in osteoclasts
Kim, J H,Youn, B U,Kim, K,Moon, J B,Lee, J,Nam, K-I I,Park, Y-W,O'Leary, D D M,Kim, K K,Kim, N Macmillan Publishers Limited 2014 CELL DEATH AND DIFFERENTIATION Vol.21 No.10
The LIM homeobox 2 (Lhx2) transcription factor Lhx2 has a variety of functions, including neural induction, morphogenesis, and hematopoiesis. Here we show the involvement of Lhx2 in osteoclast differentiation. Lhx2 was strongly expressed in osteoclast precursor cells but its expression was significantly reduced during receptor activator of nuclear factor-κB ligand (RANKL)-mediated osteoclastogenesis. Overexpression of Lhx2 in bone marrow-derived monocyte/macrophage lineage cells (BMMs), which are osteoclast precursor cells, attenuated RANKL-induced osteoclast differentiation by inhibiting the induction of nuclear factor of activated T cells c1 (NFATc1). Interestingly, interaction of Lhx2 proteins with c-Fos attenuated the DNA-binding ability of c-Fos and thereby inhibited the transactivation of NFATc1. Furthermore, Lhx2 conditional knockout mice exhibited an osteoporotic bone phenotype, which was related with increased osteoclast formation in vivo. Taken together, our results suggest that Lhx2 acts as a negative regulator of osteoclast formation in vitro and in vivo. The anti-osteoclastogenic effect of Lhx2 may be useful for developing a therapeutic strategy for bone disease.
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Cornish, M. Lynn,O' Leary, Stephen J.B.,Garbary, David J. The Korean Society of Phycology 2013 ALGAE Vol.28 No.1
Intact phycobilisomes from a wild-type red Chondrus crispus and its vegetatively derived green mutant were isolated by centrifugation through a discontinuous sucrose density gradient. Pigment composition was subsequently characterized by spectrophotometry. Vegetative thalli of the two strains grown together for six months in the laboratory resulted in different pigment profiles. Two pigmented phycobilisome bands appeared in the sucrose gradient of the wild-type alga, a purple coloured one, and a pink one, whereas only a single blue band appeared in the gradient of the green mutant. Spectrophotometric and fluorescence analyses identified the phycobiliprotein composition of the purple band as the typical phycoerythrin-phycocyanin-allophycocyanin complement in the wild-type, but there was no detectable phycoerythrin present in the blue band of the green mutant. Sodium dodecyl sulphate, preparative polyacrylamide gel electrophoresis analysis confirmed the presence of allophycocyanin subunits in all extracts, but firm evidence of an R-phycoerythrin linker polypeptide in the blue band was missing. These results highlight the ability of C. crispus to adapt to a phycoerythrin deficiency by adjusting light harvesting pigment ratios.
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M. Lynn Cornish,Stephen J. B. O’Leary,David J. Garbary 한국조류학회I 2013 ALGAE Vol.28 No.1
Intact phycobilisomes from a wild-type red Chondrus crispus and its vegetatively derived green mutant were isolated by centrifugation through a discontinuous sucrose density gradient. Pigment composition was subsequently characterized by spectrophotometry. Vegetative thalli of the two strains grown together for six months in the laboratory resulted in different pigment profiles. Two pigmented phycobilisome bands appeared in the sucrose gradient of the wild-type alga, a purple coloured one, and a pink one, whereas only a single blue band appeared in the gradient of the green mutant. Spectrophotometric and fluorescence analyses identified the phycobiliprotein composition of the purple band as the typical phycoerythrin-phycocyanin-allophycocyanin complement in the wild-type, but there was no detectable phycoerythrin present in the blue band of the green mutant. Sodium dodecyl sulphate, preparative polyacrylamide gel electrophoresis analysis confirmed the presence of allophycocyanin subunits in all extracts, but firm evidence of an R-phycoerythrin linker polypeptide in the blue band was missing. These results highlight the ability of C. crispus to adapt to a phycoerythrin deficiency by adjusting light harvesting pigment ratios.
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