Dataset Information

Alkali-salinity NaHCO3-responsive mechanisms in leaves from halophyte Puccinellia tenuiflora revealed from physiological and comparative proteomic analysis

ABSTRACT: Alkali-salinity is a major abiotic stress that limits plant growth and productivity. Studying mechanisms of alkali-salinity tolerance in halophytic plants will provide valuable information for underlying plant alkali-salinity tolerance. Puccinellia tenuiflora is considered as an ideal model plant for studying the alkali-salinity tolerant mechanisms in plants. In this study, the NaHCO3-responsive molecular mechanisms in P. tenuiflora leaves were investigated using a combined physiological and proteomic approaches. Our results implied some specific NaHCO3-responsive mechanisms in leaves from P. tenuiflora. They are (1) reduction of photosynthesis attributed to the decrease of the abundance of Calvin cycle enzymes, (2) accumulation of Na+ and K+ caused ion-specific stress, (3) accumulation of proline, soluble sugar and betaine enhanced the ability of osmotic regulation, (4) diverse reactive oxygen species (ROS) scavenging mechanisms under different NaHCO3 concentrations, and (5) alternative protein synthesis and processing strategies in chloroplast and cytoplasm. All these provide important evidence for understanding NaHCO3-responsive mechanisms in P. tenuiflora.

INSTRUMENT(S): 4800 Proteomics Analyzer

ORGANISM(S): Puccinellia Tenuiflora

TISSUE(S): Plant Cell, Leaf

SUBMITTER: Shaojun Dai

LAB HEAD: zepeng

PROVIDER: PXD002351 | Pride | 2022-02-23

REPOSITORIES: Pride

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Project description:Lipoprotein lipase (LPL) is responsible for the intravascular catabolism of triglyceride-rich lipoproteins and plays a central role in whole-body energy balance and lipid homeostasis. As such, LPL is subject to tissue-specific regulation in different physiological conditions, but the mechanisms of this regulation remain incompletely characterized. Previous work revealed that LPL comprises a set of proteoforms with different isoelectric points, but their regulation and functional significance have not been studied thus far. Here we studied the distribution of LPL proteoforms in different rat tissues and their regulation under physiological conditions. First, analysis by two-dimensional electrophoresis and Western blot showed different patterns of LPL proteoforms (i.e., different pI or relative abundance of LPL proteoforms) in different rat tissues under basal conditions, which could be related to the tissue-specific regulation of the enzyme. Next, the comparison of LPL proteoforms from heart and brown adipose tissue between adults and 15-day-old rat pups, two conditions with minimal regulation of LPL in these tissues, yielded virtually the same tissue-specific patterns of LPL proteoforms. In contrast, the pronounced down-regulation of LPL activity observed in white adipose tissue during fasting is accompanied by a prominent reconfiguration of the LPL proteoform pattern. Furthermore, refeeding reverts this down-regulation of LPL activity and restores the pattern of LPL proteoforms in this tissue. Importantly, this reversible proteoform-specific regulation during fasting and refeeding indicates that LPL proteoforms are functionally diverse. Further investigation of potential differences in the functional properties of LPL proteoforms showed that all proteoforms exhibit lipolytic activity and have similar heparin-binding affinity, although other functional aspects remain to be investigated. Overall, this study demonstrates the ubiquity, differential distribution and specific regulation of LPL proteoforms in rat tissues and underscores the need to consider the existence of LPL proteoforms for a complete understanding of LPL regulation under physiological conditions.

Dataset Information

Alkali-salinity NaHCO3-responsive mechanisms in leaves from halophyte Puccinellia tenuiflora revealed from physiological and comparative proteomic analysis

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