Publications by authors named "Timothy Y Chang"
In previous work, we found that short sleep caused sensitivity to oxidative stress; here we set out to characterize the physiological state of a diverse group of chronically short-sleeping mutants during hyperoxia as an acute oxidative stress. Using RNA-sequencing analysis, we found that short-sleeping mutants had a normal transcriptional oxidative stress response relative to controls. In both short-sleeping mutants and controls, hyperoxia led to downregulation of glycolytic genes and upregulation of genes involved in fatty acid metabolism, reminiscent of metabolic shifts during sleep.
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- Secreted modular calcium-binding proteins (SMOCs) are evolutionary conserved proteins present in various organisms, including humans and worms, characterized by their calcium-binding and thyroglobulin domains.
- In C. elegans, the sole SMOC protein (CeSMOC-1) was shown to bind to the proteoglycan LON-2/glypican and the BMP homolog DBL-1, suggesting a complex interaction that influences BMP signaling pathways.
- The study revealed that CeSMOC-1 has dual regulatory roles: it negatively impacts BMP signaling through LON-2 and positively influences it via DBL-1, contributing to our understanding of SMOC protein functions in cellular signaling.
Secreted modular calcium binding (SMOC) proteins are conserved matricellular proteins found in organisms from to humans. SMOC homologs characteristically contain one or two extracellular calcium (EC) binding domain(s) and one or two thyroglobulin type-1 (TY) domain(s). SMOC proteins in and Xenopus have been found to interact with cell surface heparan sulfate protein glycans (HSPGs) to exert both positive and negative influences on the conserved bone morphogenetic protein (BMP) signaling pathway.
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