Limited heat-shock protein 72 induction in Caco-2 cells by L-glutamine.

Abstract:

BACKGROUND/AIMS:L-glutamine (L-gln) is a conditionally essential amino acid which is consumed by certain tissues like the intestine in large amounts as energy source during critical illness. Apart from nutritive action, recent data suggest a link to heat-shock protein (hsp) induction. We investigated the effect of L-gln on hsp72 expression in the intestinal cell line Caco-2 under basal and heat-shock conditions and compared it with related amino acids. METHODS:Total cellular protein was extracted and separated by SDS-PAGE. Immunoblots were performed with anti-hsp72 followed by chemiluminescence detection and densitometric scanning. RESULTS:Following heat shock, hsp72 protein expression increased by 72 and 53% at 2 and 4 mmol/l L-gln, respectively, compared to heat shock alone (p < 0.05). Under basal conditions a limited increase occurred only at 8 mmol/l L-gln (p < 0.01). Levels remained unaffected when related amino acids including alanine, glutamate or glycine were supplemented under basal and heat-shock conditions. Similarly, the nonmetabolizable glutamine analogue DON or the toxic metabolite L-pyroglutamate did not induce hsp72. CONCLUSION:We conclude that the glutamine-mediated effect may be specifically attributed to the metabolic action of L-gln.

journal_name

Digestion

journal_title

Digestion

authors

Lindemann G,Grohs M,Stange EF,Fellermann K

doi

10.1159/000048844

subject

Has Abstract

pub_date

2001-01-01 00:00:00

pages

81-6

issue

2

eissn

0012-2823

issn

1421-9867

pii

48844

journal_volume

64

pub_type

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