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Gundry, R. L.

Publications and source records attributed to Gundry, R. L..

3 recordsLinked to original sources

Culture-Associated Changes in the Human Cardiac Fibroblast Surfaceome: A Proteomic Resource for Cell Surface Marker and Target Discovery

Cardiac fibroblasts (CF) are central to cardiac homeostasis and fibrosis, but the lack of reliable cell surface markers limits their direct isolation, characterization, and selective targeting in human myocardium. Most CF studies use cultured cells, yet how the cell surface changes during culture remains poorly defined. We used mass spectrometry-based surfaceome profiling in five sequential substudies of human CF, spanning failing and non-failing hearts, fresh and cryopreserved myocardium, and laboratory-isolated and commercially sourced cells. Culture was associated with extensive changes in surface protein abundance, which were largest between P0 and P1 and were reproduced in CF from fresh and cryopreserved tissue. These changes included increases in proteins associated with fibroblast activation and matrix production, and changes in proteins used as CF markers and pharmacologic targets. Whole cell proteomics showed that these changes extended beyond the cell surface. Because culture history shapes cultured CF, we examined 30 years of CF literature, revealing widespread use of later, mixed, or unreported passages and incomplete reporting of culture conditions. To aid future studies, we developed CFxplorer (CFxplorer.net), an interactive resource that integrates this literature analysis, passage-resolved protein trajectories, and a Human CF Surfaceome Atlas of 1,577 cell surface N-glycoproteins detected across 234 CF samples, with extracellular peptide evidence and biological and pharmacologic annotations to help prioritize candidate surface markers and targets for validation. Collectively, this study expands the human CF surfaceome, defines how it changes during culture, and shows that the properties of cultured CF should be verified, not assumed, before use in experiments.

cell biology↗

CIRFESS: An interactive resource for querying the set of theoretically detectable peptides for cell surface and extracellular enrichment proteomic studies

Cell surface transmembrane, extracellular, and secreted proteins are high value targets for immunophenotyping, drug development, and studies related to intercellular communication in health and disease. As the number of specific and validated affinity reagents that target this subproteome are limited, mass spectrometry (MS)-based approaches will continue to play a critical role in enabling discovery and quantitation of these molecules. Given the technical considerations that make MS-based cell surface proteome studies uniquely challenging, it can be difficult to select an appropriate experimental approach. To this end, we have integrated multiple prediction strategies and annotations into a single online resource, Compiled Interactive Resource for Extracellular and Surface Studies (CIRFESS). CIRFESS enables rapid interrogation of the human proteome to reveal the cell surface proteome theoretically detectable by current approaches and highlights where current prediction strategies provide concordant and discordant information. We applied CIRFESS to identify the percentage of various subsets of the proteome which are expected to be captured by targeted enrichment strategies, including two established methods and one that is possible but not yet demonstrated. These results will inform the selection of available proteomic strategies and development of new strategies to enhance coverage of the cell surface and extracellular proteome. CIRFESS is available at www.cellsurfer.net/cirfess.

bioinformatics↗

Reference glycan structure libraries of primary human cardiomyocytes and pluripotent stem cell-derived cardiomyocytes reveal cell-type and culture stage-specific glycan phenotypes

Cell surface glycoproteins play critical roles in maintaining cardiac structure and function in health and disease and the glycan-moiety attached to the protein is critical for proper protein folding, stability and signaling. However, despite mounting evidence that glycan structures are key modulators of heart function and must be considered when developing cardiac biomarkers, we currently do not have a comprehensive view of the glycans present in the normal human heart. In the current study, we used porous graphitized carbon liquid chromatography interfaced with mass spectrometry (PGC-LC-MS) to generate glycan structure libraries for primary human heart tissue homogenate, cardiomyocytes (CM) enriched from human heart tissue, and human induced pluripotent stem cell derived CM (hiPSC-CM). Altogether, we established the first reference structure libraries of the cardiac glycome containing 265 N- and O-glycans. Comparing the N-glycome of CM enriched from primary heart tissue to that of heart tissue homogenate, 21 structures significantly differed, and the high mannose class is increased in enriched CM. Moreover, by comparing primary CM to hiPSC-CM collected during 20-100 days of differentiation, dynamic changes in the glycan profile throughout in vitro differentiation were observed and differences between primary and hiPSC-CM were revealed. Namely, >30% of the N-glycome significantly changed across these time-points of differentiation and only 23% of the N-glycan structures were shared between hiPSC-CM and primary CM. These observations are an important complement to current genomic, transcriptomic, and proteomic profiling and reveal new considerations for the use and interpretation of hiPSC-CM models for studies of human development, disease, and drug testing. Finally, these data are expected to support future regenerative medicine efforts by informing targets for evaluating the immunogenic potential of hiPSC-CM and harnessing differences between immature, proliferative hiPSC-CM and adult primary CM.

biochemistry↗