A trip of peptides to the brain
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(2020) 2:30
Food Production, Processing and Nutrition
REVIEW
Open Access
A trip of peptides to the brain Toshiro Matsui1,2* , Atsuko Yoshino1 and Mitsuru Tanaka2
Abstract Dietary di/tripeptides elicit preventive effects against lifestyle-related diseases such as hypertension, and hypercholesterolemia, etc. Although there have been evidential reports that the intake of protein hydrolysate improved impaired memory in human, limited studies on bioavailability, in particular, beyond the blood-brain barrier (BBB) of candidates in hydrolysate may prevent their extensive physiological studies. Thus, this review discusses the updated studies on BBB transport of peptides showing improved cognitive decline. Furthermore, their accumulation in the brain cerebral parenchyma is also introduced. Keywords: Peptide, Blood-brain barrier, Transport, Cognitive decline
Introduction The physiological role of peptides is deemed important from the aspect of preventive lifestyle-related diseases, such as hypertension, diabetes, and atherosclerosis (Mine et al. 2010). Clinical evidences prove their effective health benefits in humans, for example, the anti-hypertensive effect shown by daily intake of small (di/tri) peptides, which modulate promoting blood pressure (Hata et al. 1996; Kawasaki et al. 2000). Antihypertensive effect of peptides (e.g., Val-Tyr) is closely associated with the suppression of promoting systemic and local renin-angiotensin (RA) systems by inhibiting angiotensin I-converting enzyme (ACE) activity. In addition, the suppression of local RA systems by peptides in the aorta and kidney (Matsui et al. 2003; Dias et al. 2017) extensively leads us to study the potential of peptides in local organs. Researchers have clarified the action of diverse peptides in improving degraded vessel functions (Matsui et al., 2012). Dias et al. (2017) have also reviewed the physiological potential of a dipeptide, Val-Tyr [angiotensin (3–4)], in the kidney through the inhibition of Na+ reabsorption via the allosteric regulation of angiotensin-related receptors. Collectively, such * Correspondence: [email protected] 1 Department of Bioresources and Biosciences, Faculty of Agriculture, Graduate School of Kyushu University, 744 Motooka, Nishi-ku, Fukuoka 819-0395, Japan 2 Research and Development Center for Five-Sense Devices, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka 819-0395, Japan
reports strongly lead us to speculate that our body can accept peptides intestinally in intact form. An epoch-making study on peptide absorption has been reported by Fei et al. (1994), who successfully cloned a human peptide transporter 1 (PepT1) from the cDNA library of rabbit intestine. PepT1 can recognize the structure of peptide bonding corresponding to di/tripeptides. Transporters related to peptide transport as a super family of proton-coupled oligopeptide transporters (POT), also known as a solute carrier 15 (SLC15), have been identified as PepT1/2 and peptide-histidine transporters (PHT)1/2 (Daniel and Kottra, 2004). They are located
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