Document Detail


Sphingomyelinase activity in mother's milk is essential for juvenile development: a case from lactating tsetse flies.
MedLine Citation:
PMID:  22517621     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Sphingosine is a structural component of sphingolipids. The metabolism of phosphoethanolamine ceramide (sphingomyelin) by sphingomyelinase (SMase), followed by the breakdown of ceramide by ceramidase (CDase) yields sphingosine. Female tsetse fly is viviparous and generates a single progeny within her uterus during each gonotrophic cycle. The mother provides her offspring with nutrients required for development solely via intrauterine lactation. Quantitative PCR showed that acid smase1 (asmase1) increases in mother's milk gland during lactation. aSMase1 was detected in the milk gland and larval gut, indicating this protein is generated during lactation and consumed by the larva. The higher levels of SMase activity in larval gut contents indicate that this enzyme is activated by the low gut pH. In addition, cdase is expressed at high levels in the larval gut. Breakdown of the resulting ceramide is likely accomplished by the larval gut-secreted CDase, which allows absorption of sphingosine. We used the tsetse system to understand the critical role(s) of SMase and CDase during pregnancy and lactation and their downstream effects on adult progeny fitness. Reduction of asmase1 by short interfering RNA negatively impacted pregnancy and progeny performance, resulting in a 4-5-day extension in pregnancy, 10%-15% reduction in pupal mass, lower pupal hatch rates, impaired heat tolerance, reduced symbiont levels, and reduced fecundity of adult progeny. This study suggests that the SMase activity associated with tsetse lactation and larval digestion is similar in function to that of mammalian lactation and represents a critical process for juvenile development, with important effects on the health of progeny during their adulthood.
Authors:
Joshua B Benoit; Geoffrey M Attardo; Veronika Michalkova; Peter Takác; Jana Bohova; Serap Aksoy
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2012-07-19
Journal Detail:
Title:  Biology of reproduction     Volume:  87     ISSN:  1529-7268     ISO Abbreviation:  Biol. Reprod.     Publication Date:  2012 Jul 
Date Detail:
Created Date:  2012-07-23     Completed Date:  2012-11-30     Revised Date:  2013-07-02    
Medline Journal Info:
Nlm Unique ID:  0207224     Medline TA:  Biol Reprod     Country:  United States    
Other Details:
Languages:  eng     Pagination:  17, 1-10     Citation Subset:  IM    
Affiliation:
Division of Epidemiology and Public Health, Yale School of Public Health, Yale University, New Haven, Connecticut 06520, USA. joshua.benoit@yale.edu
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MeSH Terms
Descriptor/Qualifier:
Animals
Base Sequence
Ceramidases / antagonists & inhibitors,  genetics,  metabolism
Drosophila / genetics
Female
Gene Knockdown Techniques
Genes, Insect
Hydrogen-Ion Concentration
Insect Proteins / antagonists & inhibitors,  genetics,  metabolism*
Lactation / genetics,  metabolism
Larva / growth & development
Milk / enzymology*
Models, Biological
Phylogeny
Pregnancy
RNA, Small Interfering / genetics
Species Specificity
Sphingomyelin Phosphodiesterase / antagonists & inhibitors,  genetics,  metabolism*
Symbiosis
Tsetse Flies / enzymology*,  genetics,  growth & development*,  microbiology
Wigglesworthia / isolation & purification
Grant Support
ID/Acronym/Agency:
AI081774/AI/NIAID NIH HHS; F32AI093023/AI/NIAID NIH HHS; R01 AI081774/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Insect Proteins; 0/RNA, Small Interfering; EC 3.1.4.-/acid sphingomyelinase-1; EC 3.1.4.12/Sphingomyelin Phosphodiesterase; EC 3.5.1.23/Ceramidases
Comments/Corrections

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