HSP70 is upregulated after heat but not freezing stress in the freeze-tolerant cricket <i>Gryllus veletis</i>
Bibliographic record
Abstract
Abstract Heat shock proteins (HSPs) are well known to prevent and repair protein damage caused by various abiotic stressors, but their role in low temperature and freezing stress is not well-characterized compared to other thermal challenges. Ice formation in and around cells is hypothesized to cause protein damage, yet many species of insects can survive freezing, suggesting HSPs may be an important mechanism in freeze tolerance. Here, we studied HSP70 in a freeze-tolerant cricket Gryllus veletis to better understand the role of HSPs in this phenomenon. We measured expression of one heat-inducible HSP70 isoform at the mRNA level (using RT-qPCR), as well as the relative abundance of total HSP70 protein (using semi-quantitative Western blotting), in five tissues from crickets exposed to a survivable heat treatment (2 h at 40°C), a 6-week fall-like acclimation that induces freeze tolerance, and a survivable freezing treatment (1.5 h at -8°C). While HSP70 expression was upregulated by heat at the mRNA or protein level in all tissues studied (fat body, Malphigian tubules, midgut, femur muscle, nervous system ganglia), no tissue exhibited HSP70 upregulation within 2 – 24 h following a survivable freezing stress. During fall-like acclimation to mild low temperatures, we only saw moderate upregulation of HSP70 at the protein level in muscle, and at the RNA level in fat body and nervous tissue. Although HSP70 is important for responding to a wide range of stressors, our work suggests that this chaperone may be less critical in the preparation for, and response to, moderate freezing stress. Highlights Heat shock protein 70 (HSP70) may not contribute substantially to freeze tolerance Heat stress caused HSP70 mRNA and protein upregulation in the spring field cricket Acclimation prior to freezing was correlated with slight HSP70 upregulation HSP70 was not upregulated after freezing in this freeze-tolerant insect Further work is needed to determine whether freezing causes protein damage Graphical abstract
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How this classification was reachedexpand
Full frame machine prediction
Teacher imitationNot calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.
Distilled classifier scores by category (both heads)
| Category | Codex | Gemma |
|---|---|---|
| Metaresearch | 0.000 | 0.000 |
| Meta-epidemiology (narrow) | 0.000 | 0.000 |
| Meta-epidemiology (broad) | 0.000 | 0.000 |
| Bibliometrics | 0.000 | 0.000 |
| Science and technology studies | 0.000 | 0.000 |
| Scholarly communication | 0.000 | 0.000 |
| Open science | 0.000 | 0.000 |
| Research integrity | 0.000 | 0.000 |
| Insufficient payload (model declined to judge) | 0.001 | 0.000 |
Machine scores (provisional)
The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.
Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.
score_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from itClassification
machine, unvalidatedMachine predicted; a candidate call from one source (direct Gemma or distilled Codex), not a consensus.
How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".