Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1998-6-16
pubmed:abstractText
The mechanism(s) by which insulin enhance prematurely the activity of brush border membrane (BBM) hydrolases in rat immature intestine is unknown. Therefore, we have compared the responses of four BBM enzymes [sucrase-isomaltase (SI), maltase, lactase-phloridzine hydrolase (LPH), and aminopeptidase] with exogenous insulin, the analog B-Asp10, IGF-I, and antireceptor MAb [insulin-receptor (IR) MAb] given to preweaning pups. Low doses of insulin caused a precocious induction of SI and of SI mRNA and stimulated maltase activity without effect on LPH nor on aminopeptidase activities. IGF-I given at the same dose as that of insulin had no detectable effect on these enzymes. Administration to sucklings of IR MAb prevented the effect of endogenous insulin by inhibiting the expression of SI and maltase without effect on LPH activity. B-Asp10, an insulin analogue that exhibits in vitro a 3.5-fold increase in receptor affinity with sustained signaling of the receptor tyrosine kinase, caused an overexpression of SI by 3.5-fold and of maltase by 1.5-fold compared with equivalent doses of normal insulin. The premature increases in SI activity, SI mRNA, and maltase activity in response to insulin were dose-dependent and were associated with dose-dependent increases in intracellular spermine and spermidine concentrations. In conclusion, these data suggest that the premature induction of SI by insulin is mediated by a dose-dependent signal initiated by binding of the hormone to its intestinal receptor, which after transduction into the cell indirectly triggers the transcription of the SI gene, possibly by changes in intracellular polyamine concentrations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Aminopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Insulin, http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor I, http://linkedlifedata.com/resource/pubmed/chemical/Lactase, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Sucrase, http://linkedlifedata.com/resource/pubmed/chemical/Sucrase-Isomaltase Complex, http://linkedlifedata.com/resource/pubmed/chemical/alpha-Glucosidases, http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase, http://linkedlifedata.com/resource/pubmed/chemical/insulin, Asp(B10)-
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0031-3998
pubmed:author
pubmed:issnType
Print
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
585-91
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:9585003-Aging, pubmed-meshheading:9585003-Aminopeptidases, pubmed-meshheading:9585003-Animals, pubmed-meshheading:9585003-Duodenum, pubmed-meshheading:9585003-Gene Expression Regulation, Enzymologic, pubmed-meshheading:9585003-Humans, pubmed-meshheading:9585003-Ileum, pubmed-meshheading:9585003-Insulin, pubmed-meshheading:9585003-Insulin-Like Growth Factor I, pubmed-meshheading:9585003-Intestinal Mucosa, pubmed-meshheading:9585003-Lactase, pubmed-meshheading:9585003-RNA, Messenger, pubmed-meshheading:9585003-Rats, pubmed-meshheading:9585003-Rats, Wistar, pubmed-meshheading:9585003-Receptor, Insulin, pubmed-meshheading:9585003-Recombinant Proteins, pubmed-meshheading:9585003-Signal Transduction, pubmed-meshheading:9585003-Sucrase, pubmed-meshheading:9585003-Sucrase-Isomaltase Complex, pubmed-meshheading:9585003-Transcription, Genetic, pubmed-meshheading:9585003-alpha-Glucosidases, pubmed-meshheading:9585003-beta-Galactosidase
pubmed:year
1998
pubmed:articleTitle
Premature stimulation of rat sucrase-isomaltase (SI) by exogenous insulin and the analog B-Asp10 is regulated by a receptor-mediated signal triggering SI gene transcription.
pubmed:affiliation
Department of Pediatrics, Faculty of Medicine, Catholic University of Louvain, Brussels, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't