Insect fat body cell morphology and response to cold stress is modulated by acclimation

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F18%3A43897537" target="_blank" >RIV/60076658:12310/18:43897537 - isvavai.cz</a>

Alternative codes found

RIV/60077344:_____/18:00495783

Result on the web

<a href="http://jeb.biologists.org/content/221/21/jeb189647" target="_blank" >http://jeb.biologists.org/content/221/21/jeb189647</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1242/jeb.189647" target="_blank" >10.1242/jeb.189647</a>

Result language

angličtina

Original language name

Insect fat body cell morphology and response to cold stress is modulated by acclimation

Original language description

Mechanistic understanding about the nature of cellular cryoinjury and mechanisms by which some animals survive freezing while others do not is currently lacking. Here, we exploited the broadly manipulable freeze tolerance of larval malt flies (Chymomyza costata) to uncover cell and tissue morphological changes associated with freeze mortality. Diapause induction, cold acclimation and dietary proline supplementation generate malt fly variants ranging from weakly to extremely freeze tolerant. Using confocal microscopy and immunostaining of the fat body, Malpighian tubules and anterior midgut, we described tissue and cytoskeletal (F-actin and alpha-tubulin) morphologies among these variants after exposure to various cold stresses (from chilling at -5 degrees C to extreme freezing at -196 degrees C), and upon recovery from cold exposure. Fat body tissue appeared to be the most susceptible to cryoinjury: freezing caused coalescence of lipid droplets, loss of a-tubulin structure and apparent aggregation of F-actin. A combination of diapause and cold acclimation substantially lowered the temperature at which these morphological disruptions occurred. Larvae that recovered from a freezing challenge repaired F-actin aggregation but not lipid droplet coalescence or alpha-tubulin structure. Our observations indicate that lipid coalescence and damage to alpha-tubulin are non-lethal forms of freeze injury, and suggest that repair or removal (rather than protection) of actin proteins is a potential mechanism of acquired freeze tolerance.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

<a href="/en/project/GA16-06374S" target="_blank" >GA16-06374S: Nature of cold injury and its repair in insects.</a><br>

Continuities

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2018

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Experimental Biology

ISSN

0022-0949

e-ISSN

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Volume of the periodical

221

Issue of the periodical within the volume

21

Country of publishing house

GB - UNITED KINGDOM

Number of pages

8

Pages from-to

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UT code for WoS article

000449824800024

EID of the result in the Scopus database

2-s2.0-85055855042