Yin Ying Ho

University of Melbourne

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Peter Hoffmann

University of South Australia

Ying Swan Ho

Agency for Science, Technology and Research

Victor Lin

University of North Texas

Hamed S. Hayatshahi

Reata Pharmaceuticals (United States)

Rohit Sampat

University of North Texas

Kyle A. Emmitte

University of North Texas

Abhishek Parab

Purdue University West Lafayette

Ashwini Zolekar

University of Illinois Chicago

Nigam M. Mishra

University of North Texas

Kai Lay Esther Peh

Bioprocessing Technology Institute

Cooperative Institutions

National University of Singapore

Agency for Science, Technology and Research

Genome Institute of Singapore

University of Adelaide

University of Melbourne

Duke-NUS Medical School

National Cancer Centre Singapore

Australian Research Council

Nanyang Technological University

National University Cancer Institute, Singapore

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Fatty acid oxidation is a druggable gateway regulating cellular plasticity for driving metastasis in breast cancer

Science Advances (2021)

Ser Yue Loo Li Ping Toh William Xie Elina Pathak Wilson Wei Sheng Tan

Cell state transitions control the functional behavior of cancer cells. Epithelial-to-mesenchymal transition (EMT) confers cancer stem cell-like properties, enhanced tumorigenicity and drug resistance to tumor cells, while mesenchymal-epithelial transition (MET) reverses these phenotypes. Using high-throughput chemical library screens, retinoids are found to be potent promoters of MET that inhibit tumorigenicity in basal-like breast cancer. Cell state transitions are defined by reprogramming of lipid metabolism. Retinoids bind cognate nuclear receptors, which target lipid metabolism genes, thereby redirecting fatty acids for β-oxidation in the mesenchymal cell state towards lipid storage in the epithelial cell state. Disruptions of key metabolic enzymes mediating this flux inhibit MET. Conversely, perturbations to fatty acid oxidation (FAO) rechannel fatty acid flux and promote a more epithelial cell phenotype, blocking EMT-driven breast cancer metastasis in animal models. FAO impinges on the epigenetic control of EMT through acetyl-CoA-dependent regulation of histone acetylation on EMT genes, thus determining cell states.

10.1126/sciadv.abh2443

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Citations (67)

N‐ Glycan matrix‐assisted laser desorption/ionization mass spectrometry imaging protocol for formalin‐fixed paraffin‐embedded tissues

Rapid Communications in Mass Spectrometry (2017)

Matthew T. Briggs Yin Ying Ho Gurjeet Kaur Martin K. Oehler Arun Everest‐Dass

Matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI-MSI) of the proteome of a tissue has been an established technique for the past decade. In the last few years, MALDI-MSI of the N-glycome has emerged as a novel MALDI-MSI technique. To assess the accuracy and clinical significance of the N-linked glycan spatial distribution, we have developed a method that utilises MALDI-MSI followed by liquid chromatography coupled to tandem mass spectrometry (LC/MS/MS) in order to assign glycan structures to the differentiating MALDI-MSI glycan masses released from the tissue glycoproteins.Our workflow presents a comprehensive list of instructions on how to (i) apply MALDI-MSI to spatially map the N-glycome across formalin-fixed paraffin-embedded (FFPE) clinical samples, (ii) structurally characterise N-glycans extracted from consecutive FFPE tissue sections by LC/MS/MS, and (iii) match relevant N-glycan masses from MALDI-MSI with confirmed N-glycan structures determined by LC/MS/MS.Our protocol provides groups that are new to this technique with instructions how to establish N-glycan MALDI-MSI in their laboratory. Furthermore, the method assigns N-glycan structural detail to the masses obtained in the MALDI-MS image. Copyright © 2017 John Wiley & Sons, Ltd.

Mass spectrometry imaging

Matrix (chemical analysis)

10.1002/rcm.7845

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Citations (25)

Applications of Mass Spectrometry Imaging to Cancer

Advances in cancer research (2017)

Georgia Arentz Parul Mittal Chao Zhang Yin Ying Ho Matthew T. Briggs

Mass spectrometry imaging

MALDI imaging

10.1016/bs.acr.2016.11.002

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Citations (61)

Evaluating the Efficacy of Subcellular Fractionation of Blast Cells Using Live Cell Labeling and 2D DIGE

Methods in molecular biology (2012)

Yin Ying Ho Megan A. S. Penno Michelle Perugini Ian A. Lewis Peter Hoffmann

Proteome

Cell fractionation

Surface protein

10.1007/978-1-61779-573-2_22

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Applications and analysis of hydrolysates in animal cell culture

Bioresources and Bioprocessing (2021)

Yin Ying Ho Hao Lu Zhi Feng Sherman Lim Hao Wei Lim Ying Swan Ho

Abstract Animal cells are used in the manufacturing of complex biotherapeutic products since the 1980s. From its initial uses in biological research to its current importance in the biopharmaceutical industry, many types of culture media were developed: from serum-based media to serum-free to protein-free chemically defined media. The cultivation of animal cells economically has become the ultimate goal in the field of biomanufacturing. Serum serves as a source of amino acids, lipids, proteins and most importantly growth factors and hormones, which are essential for many cell types. However, the use of serum is unfavorable due to its high price tag, increased lot-to-lot variations and potential risk of microbial contamination. Efforts are progressively being made to replace serum with recombinant proteins such as growth factors, cytokines and hormones, as well as supplementation with lipids, vitamins, trace elements and hydrolysates. While hydrolysates are more complex, they provide a diverse source of nutrients to animal cells, with potential beneficial effects beyond the nutritional value. In this review, we discuss the use of hydrolysates in animal cell culture and briefly cover the composition of hydrolysates, mode of action and potential contaminants with some perspectives on its potential role in animal cell culture media formulations in the future.

Biomanufacturing

Biopharmaceutical

10.1186/s40643-021-00443-w

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Citations (44)

A Glycosyltransferase from Nicotiana alata Pollen Mediates Synthesis of a Linear (1,5)-α-L-Arabinan When Expressed in Arabidopsis

PLANT PHYSIOLOGY (2016)

Edwin R. Lampugnani Yin Ying Ho Isabel Møller Poh-Ling Koh John F. Golz

The walls of Nicotiana alata pollen tubes contain a linear arabinan composed of (1,5)-α-linked arabinofuranose residues. Although generally found as a side chain on the backbone of the pectic polysaccharide rhamnogalacturonan I, the arabinan in N. alata pollen tubes is considered free, as there is no detectable rhamnogalacturonan I in these walls. Carbohydrate-specific antibodies detected arabinan epitopes at the tip and along the shank of N. alata pollen tubes that are predominantly part of the primary layer of the bilayered wall. A sequence related to ARABINAN DEFICIENT1 (AtARAD1), a presumed arabinan arabinosyltransferase from Arabidopsis (Arabidopsis thaliana), was identified by searching an N alata pollen transcriptome. Transcripts for this ARAD1-like sequence, which we have named N. alata ARABINAN DEFICIENT-LIKE1 (NaARADL1), accumulate in various tissues, most abundantly in the pollen grain and tube, and encode a protein that is a type II membrane protein with its catalytic carboxyl terminus located in the Golgi lumen. The NaARADL1 protein can form homodimers when transiently expressed in Nicotiana benthamiana leaves and heterodimers when coexpressed with AtARAD1 The expression of NaARADL1 in Arabidopsis led to plants with more arabinan in their walls and that also exuded a guttation fluid rich in arabinan. Chemical and enzymatic characterization of the guttation fluid showed that a soluble, linear α-(1,5)-arabinan was the most abundant polymer present. These results are consistent with NaARADL1 having an arabinan (1,5)-α-arabinosyltransferase activity.

10.1104/pp.15.02005

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Citations (22)

Direct identification of A-to-I editing sites with nanopore native RNA sequencing

Nature Methods (2022)

Tram Anh Thi Nguyen Jia Wei Joel Heng Pornchai Kaewsapsak Eng Piew Louis Kok Dominik Stanojević

Nanopore

Identification

10.1038/s41592-022-01513-3

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Citations (80)

Exploring Biologically Relevant Pathways in Frailty

The Journals of Gerontology Series A (2011)

Yin Ying Ho Amy M. Matteini B. Beamer Linda F. Fried Qian‐Li Xue

Background.Frailty is a late-life syndrome of vulnerability to adverse health outcomes characterized by a phenotype that includes muscle weakness, fatigue, and inflammatory pathway activation. The identification of biologically relevant pathways that influence frailty is challenged by its biological complexity and the necessity in separating disease states from the syndrome of frailty. As with longevity research, genetic analyses may help to provide insights into biologically relevant pathways that contribute to frailty.

Biological pathway

Genetic Association

10.1093/gerona/glr061

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Citations (55)

A chemokine-binding domain in the tumor necrosis factor receptor from variola (smallpox) virus

Proceedings of the National Academy of Sciences (2006)

Alı́ Alejo M. Begoña Ruiz-Argüello Yin Ying Ho Vincent P. Smith Margarida Saraiva

Variola virus (VaV) is the causative agent of smallpox, one of the most devastating diseases encountered by man, that was eradicated in 1980. The deliberate release of VaV would have catastrophic consequences on global public health. However, the mechanisms that contribute to smallpox pathogenesis are poorly understood at the molecular level. The ability of viruses to evade the host defense mechanisms is an important determinant of viral pathogenesis. Here we show that the tumor necrosis factor receptor (TNFR) homologue CrmB encoded by VaV functions not only as a soluble decoy TNFR but also as a highly specific binding protein for several chemokines that mediate recruitment of immune cells to mucosal surfaces and the skin, sites of virus entry and viral replication at late stages of smallpox. CrmB binds chemokines through its C-terminal domain, which is unrelated to TNFRs, was named smallpox virus-encoded chemokine receptor (SECRET) domain and uncovers a family of poxvirus chemokine inhibitors. An active SECRET domain was found in another viral TNFR (CrmD) and three secreted proteins encoded by orthopoxviruses. These findings identify a previously undescribed chemokine-binding and inhibitory domain unrelated to host chemokine receptors and a mechanism of immune modulation in VaV that may influence smallpox pathogenesis.

Variola virus

Viral Pathogenesis

10.1073/pnas.0510462103

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Citations (140)

Molecular mechanism of the assembly of (1,3;1,4)-β-D-glucan in Italian ryegrass (Lolium multiflorum) suspension-cultured cells

Yin Ying Ho

Lolium multiflorum

Suspension

Suspension culture

Lolium

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