Author
Ri Yao Yang
Other affiliations: Scripps Research Institute, La Jolla Institute for Allergy and Immunology, University of California, Davis
Bio: Ri Yao Yang is an academic researcher from University of Texas MD Anderson Cancer Center. The author has contributed to research in topics: Galectin & Immunotherapy. The author has an hindex of 20, co-authored 33 publications receiving 3358 citations. Previous affiliations of Ri Yao Yang include Scripps Research Institute & La Jolla Institute for Allergy and Immunology.
Topics: Galectin, Immunotherapy, Cytotoxic T cell, Jurkat cells, Apoptosis
Papers
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TL;DR: Galectin-3 is a regulator of cell growth and apoptosis and it may function through a cell death inhibition pathway that involves Bcl-2, a well-characterized suppressor of apoptosis.
Abstract: Galectin-3 is a member (if a large family of beta-galactoside-binding animal lectins. It has been shown that the expression of galectin-3 is upregulated in proliferating cells, suggesting a possible role for this lectin in regulation of cell growth. Previously, we have shown that T cells infected with human T-cell leukemia virus type I express high levels of galectin-3, in contrast to uninfected cells, which do not express detectable amounts of this protein. In this study, we examined growth properties of human leukemia T cells transfected with galectin-3 cDNA, and thus constitutively overexpressing this lectin. Transfectants expressing galectin-3 displayed higher growth rates than control transfectants, which do not express this lectin. Furthermore, galectin-3 expression in these cells confers resistance to apoptosis induced by anti-Fas antibody and staurosporine. Galectin-3 was found to have significant sequence similarity with Bcl-2, a well-characterized suppressor of apoptosis. In particular, the lectin contains the NWGR motif that is highly conserved among members of the Bcl-2 family and shown to be critical for the apoptosis-suppressing activity. We further demonstrated that galectin-3 interacts with Bc1-2 in a lactose-inhibitable manner. We conclude that galectin-3 is a regulator of cell growth and apoptosis and it may function through a cell death inhibition pathway that involves Bcl-2.
750 citations
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TL;DR: Current research indicates that galectins play important roles in diverse physiological and pathological processes, including immune and inflammatory responses, tumour development and progression, neural degeneration, atherosclerosis, diabetes, and wound repair, and may be a therapeutic target or employed as therapeutic agents for inflammatory diseases, cancers and several other diseases.
Abstract: Galectins are a family of animal lectins that bind β-galactosides. Outside the cell, galectins bind to cell-surface and extracellular matrix glycans and thereby affect a variety of cellular processes. However, galectins are also detectable in the cytosol and nucleus, and may influence cellular functions such as intracellular signalling pathways through protein–protein interactions with other cytoplasmic and nuclear proteins. Current research indicates that galectins play important roles in diverse physiological and pathological processes, including immune and inflammatory responses, tumour development and progression, neural degeneration, atherosclerosis, diabetes, and wound repair. Some of these have been discovered or confirmed by using genetically engineered mice deficient in a particular galectin. Thus, galectins may be a therapeutic target or employed as therapeutic agents for inflammatory diseases, cancers and several other diseases.
701 citations
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TL;DR: It was found that peritoneal macrophages from gal3(-/-) mice were more prone to undergo apoptosis than those from Gal3(+/+) mice when treated with apoptotic stimuli, suggesting that expression of galectin-3 in inflammatory cells may lead to longer cell survival, thus prolonging inflammation.
Abstract: Galectin-3 is a member of a growing family of β-galactoside-binding animal lectins. Previous studies have demonstrated a variety of biological activities for this protein in vitro, including activation of cells, modulation of cell adhesion, induction of pre-mRNA splicing, and regulation of apoptosis. To assist in fully elucidating the physiological and pathological functions of this protein, we have generated galectin-3-deficient (gal3−/−) mice by targeted interruption of the galectin-3 gene. Gal3−/− mice consistently developed fewer inflammatory cell infiltrations in the peritoneal cavities than the wild-type (gal3+/+) mice in response to thioglycollate broth treatment, mainly due to lower numbers of macrophages. Also, when compared to cells from gal3+/+ mice, thioglycollate-elicited inflammatory cells from gal3−/− mice exhibited significantly lower levels of NF-κB response. In addition, dramatically different cell-spreading phenotypes were observed in cultured macrophages from the two genotypes. Whereas macrophages from gal3+/+ mice exhibited well spread out morphology, those from gal3−/− mice were often spindle-shaped. Finally, we found that peritoneal macrophages from gal3−/− mice were more prone to undergo apoptosis than those from gal3+/+ mice when treated with apoptotic stimuli, suggesting that expression of galectin-3 in inflammatory cells may lead to longer cell survival, thus prolonging inflammation. These results strongly support galectin-3 as a positive regulator of inflammatory responses in the peritoneal cavity.
417 citations
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TL;DR: Transfectants of HeLa and DLD-1 cells ectopically expressing galectin-7 were found to be more susceptible to apoptosis than control transfectants and this protein is a pro-apoptotic protein that functions intracellularly upstream of JNK activation and cytochrome c release.
202 citations
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TL;DR: Fourteen members of the galectin family, proteins with conserved carbohydrate-recognition domains that bind β-galactoside, have been cloned and more are expected to be discovered in the near future, with the only member known so far to inhibit apoptosis.
Abstract: Fourteen members of the galectin family, proteins with conserved carbohydrate-recognition domains that bind β-galactoside, have been cloned and more are expected to be discovered in the near future. Many aspects of galectin biology have been thoroughly explored, and functional studies have implicated these proteins in cell growth, differentiation and apoptosis, in addition to cell adhesion, chemoattraction and cell migration. In some cases a galectin can either promote or suppress cell growth, depending on the cell types and doses used. Galectin-3 is the only member known so far to inhibit apoptosis, while galectin-1, -7 and -9 promote this cellular process. Galectins can act either extracellularly or intracellularly to exert effects on cell growth and apoptosis.
198 citations
Cited by
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TL;DR: It is demonstrated that >90% of all macrophages in WAT of obese mice and humans are localized to dead adipocytes, where they fuse to form syncytia that sequester and scavenge the residual “free” adipocyte lipid droplet and ultimately form multinucleate giant cells, a hallmark of chronic inflammation.
2,235 citations
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TL;DR: Current research indicates that galectins have important roles in cancer; they contribute to neoplastic transformation, tumour cell survival, angiogenesis and tumour metastasis, and might have a key role helping tumours to escape immune surveillance.
Abstract: Galectins are a family of animal lectins with diverse biological activities. They function both extracellularly, by interacting with cell-surface and extracellular matrix glycoproteins and glycolipids, and intracellularly, by interacting with cytoplasmic and nuclear proteins to modulate signalling pathways. Current research indicates that galectins have important roles in cancer; they contribute to neoplastic transformation, tumour cell survival, angiogenesis and tumour metastasis. They can modulate the immune and inflammatory responses and might have a key role helping tumours to escape immune surveillance. How do the different members of the Galectin family contribute to these diverse aspects of tumour biology?
1,335 citations
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TL;DR: Through specific interactions with a variety of intra- and extracellular proteins galectin-3 affects numerous biological processes and seems to be involved in different physiological and pathophysiological conditions, such as development, immune reactions, and neoplastic transformation and metastasis.
1,003 citations
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TL;DR: The pivotal role of keratinocytes in epithelialization is focused on, including cellular processes and mechanisms of their regulation during re-epithelialization, and their cross talk with other cell types participating in wound healing.
Abstract: Significance: Keratinocytes, a major cellular component of the epidermis, are responsible for restoring the epidermis after injury through a process termed epithelialization. This review will focus on the pivotal role of keratinocytes in epithelialization, including cellular processes and mechanisms of their regulation during re-epithelialization, and their cross talk with other cell types participating in wound healing. Recent Advances: Discoveries in epidermal stem cells, keratinocyte immune function, and the role of the epidermis as an independent neuroendocrine organ will be reviewed. Novel mechanisms of gene expression regulation important for re-epithelialization, including microRNAs and histone modifications, will also be discussed. Critical Issues: Epithelialization is an essential component of wound healing used as a defining parameter of a successful wound closure. A wound cannot be considered healed in the absence of re-epithelialization. The epithelialization process is impaired in all types o...
914 citations
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TL;DR: In this paper, a frontal affinity chromatography (FAC) was used to quantitatively analyze the interactions at 20 °C between 13 galectins including 16 CRDs originating from mammals, chick, nematode, sponge, and mushroom, with 41 pyridylaminated (PA) oligosaccharides.
888 citations