A Pilot Study for the Detection of Cyclic Prolyl-Hydroxyproline (Pro-Hyp) in Human Blood after Ingestion of Collagen Hydrolysate.

Yasutaka Shigemura,Asahi Suzuki,Mihoko Kurokawa,Yoshio Sato,Yu Iwasaki,Kenji Sato,Mana Tateno

doi:10.3390/nu10101356

Yasutaka Shigemura, Asahi Suzuki + Show 5 more

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https://doi.org/10.3390/nu10101356

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Journal: Nutrients	Publication Date: Sep 22, 2018
Citations: 17	License type: CC BY 4.0

Affiliation: Tokyo Kasei University, Kyoto University

Abstract

Levels of short linear hydroxyproline (Hyp)-containing peptides, such as prolyl-hydroxyproline (Pro-Hyp), increase in human blood after the ingestion of collagen hydrolysate, which has been associated with beneficial effects for human skin and joints. The present study demonstrates the presence of a novel food-derived collagen peptide, cyclic Pro-Hyp, in human blood after the ingestion of collagen hydrolysate. The cyclic Pro-Hyp levels in plasma samples were estimated by liquid chromatography mass spectrometry (LC-MS). Cyclic Pro-Hyp levels significantly increased in the plasma after ingestion of collagen hydrolysate, reaching a maximum level after 2 h and then decreasing. The maximum level of cyclic Pro-Hyp in plasma ranged from 0.1413 to 0.3443 nmol/mL, representing approximately 5% of linear Pro-Hyp in plasma after ingestion of collagen hydrolysate. Addition of cyclic Pro-Hyp in medium at 7 nmol/mL significantly enhanced the growth rate of mouse skin fibroblasts on collagen gel more extensively compared to linear Pro-Hyp.

Highlights

IntroductionCollagen is the most abundant protein in the animal body and accounts for approximately 30%
Collagen is the most abundant protein in the animal body and accounts for approximately 30%of all human proteins
To examine the bio-activities of cyclic Pro-Hyp, we examined its effect on the growth of mouse skin fibroblasts on collagen gel (Figure 7)

Summary

Introduction

Collagen is the most abundant protein in the animal body and accounts for approximately 30%. This protein is present as a major extracellular matrix component in the skin, muscle, cartilage, bone, and tendons. The collagen molecule forms a triple helical structure and contains a unique amino acid, hydroxyproline (Hyp), which exists in collagen [1]. The heat-denatured form of collagen is called gelatin. Gelatin has a collapsed triple helical structure and has been used in foods, pharmaceuticals, cosmetics, and photographic film at the industrial scale. It has been suggested that ingestion of gelatin improves conditions of joints, skin, nails, and hair [2,3,4]

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