4.5 Article Proceedings Paper

Programmed cell death in flight muscle histolysis of the house cricket

Journal

JOURNAL OF INSECT PHYSIOLOGY
Volume 53, Issue 1, Pages 30-39

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jinsphys.2006.09.012

Keywords

flight muscle histolysis; programmed cell death; juvenile hormone; dorsal longitudinal muscle; cricket

Funding

  1. NATIONAL CENTER ON MINORITY HEALTH AND HEALTH DISPARITIES [P20MD000233] Funding Source: NIH RePORTER
  2. NIMHD NIH HHS [P20 MD000233-010002, P20 MD000233, MD 00233] Funding Source: Medline

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We have characterized the process of flight muscle histolysis in the female house cricket, Acheta domesticus, through analysis of alterations of tissue wet weight, total protein content, and percent shortening of the dorsal longitudinal flight muscles (DLMs). Our objectives were to (1) define the normal course of histolysis in the cricket, (2) analyze the effects of juvenile hormone (JH) removal and replacement, (3) determine the effects of cycloheximide treatment, and (4) examine patterns of protein expression during histolysis. Our results suggest that flight muscle histolysis in the house cricket is an example of an active, developmentally regulated cell death program induced by an endocrine signal. Initial declines of total protein in DLMs indicated the JH signal that induced histolysis occurred by Day 2 and that histolysis was essentially complete by Day 3. Significant reductions in tissue weight and percent muscle shortening were observed in DLMs from Day 3 crickets. Cervical ligation of Day 1 crickets prevented histolysis but this inhibition could be reversed by continual topical treatments with methoprene (an active JH analog) although ligation of Day 2 crickets did not prevent histolysis. A requirement for active protein expression was demonstrated by analysis of synthesis block by cycloheximide and short-term incorporation of 35 S-methionine. Treatment with cycloheximide prevented histolysis. Autofluorographic imaging of DLM proteins separated by electrophoresis revealed apparent coordinated regulation of protein expression. (c) 2006 Elsevier Ltd. All rights reserved.

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