Autism Studies and Related Medical Conditions, January 2009 - TACA

times peer week) was effective in immediately decreasing gross motor activity and
stereotyped behaviour and caused a delayed increase of crying, smiling and rough-andtumble
play. This single case presents preliminary evidence that a therapeutically
valuable rebound reaction is possible and that the human opioid system modulates
social-affective processes. The possibility of psychological factors being instrumental in
achieving this effect is discussed as being suitable for future clinical trials.
Kurek M, Przybilla B, Hermann K, Ring J: A naturally occurring opioid peptide from
cow's milk, beta-casomorphine-7, is a direct histamine releaser in man.Int Arch Allergy
Immunol 1992;97(2):115-20.
Abstract: Department of Dermatology, Ludwig-Maximilian-University, Munich.
beta-Casomorphine-7, a naturally occurring product of cow's milk with opiate-like
activity, was studied for possible direct histamine liberation activities in humans. It was
found to cause concentration-dependent in vitro histamine release from peripheral
leukocytes of healthy adult volunteers. Intradermal injection of beta-casomorphine-7
induced a wheal and flare reaction in the skin similar to histamine or codeine. Oral
pretreatment with the H1 antagonist terfenadine significantly inhibited the skin
responses to beta-casomorphine-7. The intradermal injection of an opiate receptor
antagonist, naloxone, inhibited in vitro histamine release and skin reactions only in a
100-fold excess over beta-casomorphine-7. These findings suggest that betacasomorphine-7
can be regarded as a noncytotoxic, direct histamine releaser in
humans. The clinical relevance of these findings deserves further studies.
Fukudome S, Yoshikawa M: Opioid peptides derived from wheat gluten: their
isolation and characterization. Federation of European Biochemical Societies (FEBS)
1992; 296: 107-111.
Abstract:Research Control Department, Nisshin Flour Milling Co., Ltd., Tokyo, Japan.
Four opioid peptides were isolated from the enzymatic digest of wheat gluten. Their
structures were Gly-Tyr-Tyr-Pro-Thr, Gly-Tyr-Tyr-Pro,Tyr-Gly-Gly-Trp-Leu and Tyr-Gly-
Gly-Trp, which were named gluten exorphins A5, A4, B5 and B4, respectively. The
gluten exorphin A5 sequence was found at 15 sites in the primary structure of the high
molecular weight glutenin and was highly specific for delta-receptors. The structureactivity
relationships of gluten exorphins A were unique in that the presence of Gly at
their N-termini increased their activities. Gluten exorphin B5, which corresponds to
[Trp4,Leu5]enkephalin, showed the most potent activity among these peptides. Its IC50
values were 0.05 microM and 0.017 microM, respectively, on the GPI and the MVD
assays.
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