Effect of exorphins on gastrointestinal function, hormonal release, and appetite

Morley, John E.; Levine, Allen S.; Yamada, Tadataka; Gebhard, Roger L.; Prigge, William F.; Shafer, Rex B.; Goetz, Frederick C.; Silvis, Stephen E.

doi:10.1016/0016-5085(83)90374-8

Cited by 84 publications

(26 citation statements)

References 37 publications

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“…et al, 1981). These peptides of exogenous origin behave like endorphins and so have been named 'exorphins' (Zioudrou et al, 1979) or 'formones' (= food hormones) (Morley et al, 1983). If these active molecules do indeed enter the circulation during assimilation in vivo of gluten or casein, this could have clinically significant consequences.…”

Section: Possible Implications Of Absorption Of Intact Peptidesmentioning

confidence: 98%

Entry of Peptides of Dietary Origin into the Circulation

Gardner

1983

Nutr Health

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Current theories of protein digestion and absorption state that free amino acids are the only significant form in which amino-N crosses the intestine and enters the systemic circulation. Nevertheless, there is now abundant evidence that intact peptides escaping digestion (or undergoing only partial digestion) and even whole protein molecules can enter the circulation in health and disease. Since peptides are now believed to play a major role in neural and endocrine regulation and in view of the fact that intestinal digestive activity can be reduced and intestinal 'permeability' increased in a variety of pathological conditions, the possibility that absorbed intact peptides can exert biological activities in peripheral tissues and can elicit symptoms in susceptible individuals now requires critical evaluation. These considerations may provide a physiological rationale for changing the source(s) of dietary protein in cases where food allergies/dietary sensitivities are suspected.

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Section: Possible Implications Of Absorption Of Intact Peptidesmentioning

confidence: 98%

Entry of Peptides of Dietary Origin into the Circulation

Gardner

1983

Nutr Health

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“…With increased knowledge of the physiological and pharmacological properties of many peptides, protein hydrolysates have taken on a new role. Recent advances in this area substantiate the specific contributions of protein digestion products to, for example, intestinal motility and transit,5 hormonal secretion,6 opioid activity7 and calcium absorption 8…”

Section: Introductionmentioning

confidence: 94%

Kinetics of peptide fraction release during in vitro digestion of casein

et al. 2004

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The charges and sizes of peptides released during in vitro casein digestion were investigated. Casein was hydrolysed sequentially by pepsin and pancreatin and, during hydrolysis, the products of digestion were removed by dialysis. The undigested residues were separated by ion-exchange chromatography into basic-neutral (BN), lightly acid (LA) and acid (A) fractions. Each of these fractions was further resolved by sequential ultrafiltration (MWCO 10 and 1 kDa) into two retentates (>10 and 10-1 kDa) and one permeate (<1 kDa). The polypeptides (>10 kDa) produced by pepsin hydrolysis were degraded into small molecules during the first 2 h of pancreatin hydrolysis; less than 100 mg g −1 of the total N remained undigested. Most of the material produced was in the BN10-1 (ie basic-neutral, 10-1 kDa) fraction, with three times as much N as the A10-1 fractions. As digestion progressed a decrease in the proportion of N in the residues retained by the dialysis membrane was observed. This decrease was particularly rapid in the BN10-1 fraction. Large proportions of leucine (Leu), lysine (Lys), arginine (Arg), phenylalanine (Phe) and tyrosine (Tyr) were found as peptides smaller than 1 kDa, both in the dialysates and retentates, while glutamine (Glu), threonine (Thr), serine (Ser) and asparagine (Asp) appeared mostly in the A10-1 and A >10 fractions. After 6 h of pancreatin hydrolysis most of the proline (Pro) content was in the BN10-1 fractions. The mechanisms behind and the implications of these results are discussed.

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“…Wheat gluten has a unique amino acid composition: glutamyl residues account for about 40% of the amino acids (Kasarda et al, 1984). It is demonstrated that wheat gluten hydrolysate (WGH) contains various functional peptides which have opioidergic activity (Morley et al, 1983;Schusdziarra et al, 1981) or inhibitory effect on angiotensin-I converting enzyme (Motoi and Kodama, 2003). Moreover, WGH is reported to have the inhibitory effect on muscle damage after exercise (Sawaki et al, 2004) and liver cirrhosis (Horigushi et al, 2004;Suzuki et al, 2012).…”

Section: Introductionmentioning

confidence: 95%