Quantification of hydroxyprolyl-glycine (Hyp-Gly) in human blood after ingestion of collagen hydrolysate

Sugihara, Fumihito; Inoue, Naoki; Kuwamori, Masanori; Taniguchi, Makoto

doi:10.1016/j.jbiosc.2011.09.024

Cited by 38 publications

(31 citation statements)

References 9 publications

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“…Apart from these, studies that focused on the effects of oral intake in both animal and human models have revealed an efficient absorption and metabolism of hydroxyproline containing peptides. Possible bioactivity of these sequences has also been reported [15,16] with their ability to bypass gut digestion [17].…”

Section: Introductionmentioning

confidence: 86%

Antioxidant and Angiotensin 1 Converting Enzyme Inhibitory Functions from Chicken Collagen Hydrolysates

Soladoye¹,

Saldo²,

Peiró³

et al. 2014

J Nutr Food Sci

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Section: Introductionmentioning

confidence: 86%

Antioxidant and Angiotensin 1 Converting Enzyme Inhibitory Functions from Chicken Collagen Hydrolysates

Soladoye¹,

Saldo²,

Peiró³

et al. 2014

J Nutr Food Sci

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“…In addition, small amounts of other di-and tripeptides such as Ala-Hyp, Ala-Hyp-Gly, Leu-Hyp, Ile-Hyp, Phe-Hyp, Pro-Hyp-Gly, (Iwai et al, 2005) and Gly-Pro-Hyp can be detected (Ichikawa et al, 2010;Watanabe-Kamiyama et al, 2010). Another peptide, Hyp-Gly, was more recently discovered in human plasma upon collagen ingestion (Shigemura et al, 2011;Sugihara, Inoue, Kuwamori, & Taniguchi, 2012). It is noticeable that the average plasma concentration of those peptides is dose-dependent: Hyp-containing peptides reach maximum levels of 6.43, 20.17 and 32.84 nmol/mL following ingestion of 30.8, 153.8 and 384.6 mg doses of HC, respectively (Shigemura et al, 2011;Shigemura, Kubomura, Sato, & Sato, 2014).…”

Section: Bioavailabilitymentioning

confidence: 99%

Biological Effect of Hydrolyzed Collagen on Bone Metabolism

Daneault

Coxam

Wittrant

2015

Critical Reviews in Food Science and Nutrition

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Osteoporosis is a chronic and asymptomatic disease characterized by low bone mass and skeletal microarchitectural deterioration, increased risk of fracture, and associated comorbidities most prevalent in the elderly. Due to an increasingly aging population, osteoporosis has become a major health issue requiring innovative disease management. Proteins are important for bone by providing building blocks and by exerting specific regulatory function. This is why adequate protein intake plays a considerable role in both bone development and bone maintenance. More specifically, since an increase in the overall metabolism of collagen can lead to severe dysfunctions and a more fragile bone matrix and because orally administered collagen can be digested in the gut, cross the intestinal barrier, enter the circulation, and become available for metabolic processes in the target tissues, one may speculate that a collagen-enriched diet provides benefits for the skeleton. Collagen-derived products such as gelatin or hydrolyzed collagen (HC) are well acknowledged for their safety from a nutritional point of view; however, what is their impact on bone biology? In this manuscript, we critically review the evidence from literature for an effect of HC on bone tissues in order to determine whether HC may represent a relevant alternative in the design of future nutritional approaches to manage osteoporosis prevention.

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“…Collagen peptides (CP) are produced by the hydrolysis of gelatin (heat-denatured collagen) by proteases and are commonly utilized as a component of nutraceuticals (8). It has been demonstrated that, following the digestion of orally administered CP in the intestine, di- and tri-peptides, particularly Prolyl-hydroxyproline (Pro-Hyp), as well as amino acids, accumulate in human peripheral blood and these peptides remain in the blood for a relatively long time (3–4 h) (9–11). Pro-Hyp is considered to be a biologically active substance, as it induces hyaluronic acid synthesis in cultured synovial cells (12) and suppresses the hypertrophic differentiation of chondrocytes, which is involved in the pathogenesis of OA (13).…”

Section: Introductionmentioning

confidence: 99%

Evaluation of the effect of oral administration of collagen peptides on an experimental rat osteoarthritis model

Isaka

Someya

Nakamura

et al. 2017

Experimental and Therapeutic Medicine

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Collagen is an extracellular matrix protein present in the skin, tendon, cartilage and bone. Collagen peptides (CP) are produced by the hydrolysis of gelatin (heat-denatured collagen) by proteases and are utilized as a component of nutraceuticals. The current study investigated the effect of CP on the articular cartilage of OA by evaluating the serum levels of biomarkers (CTX–II for type II collagen degradation and CPII for type II collagen synthesis), histopathological changes (Mankin score, based on the toluidine blue staining of proteoglycans), and immunohistochemical staining of matrix metalloproteinase (MMP)-13 and type II collagen, using a rat experimental osteoarthritis (OA) model. Anterior cruciate ligament transection (ACLT) was performed on the right knee joint to surgically induce OA. Animals were divided into four groups: Control group (Control), sham-operated group (Sham), ACLT group without collagen peptide (ACLT group) and ACLT group with oral administration of CP (CP group). ACLT induced histological damages and significantly increased the Mankin score (P<0.05). However, CP administration markedly suppressed the Mankin score, although this difference was not significant. In addition, serum CTX-II levels were significantly decreased in CP group compared with those in the ACLT group (P<0.05). By contrast, serum CPII levels did not differ significantly among the four groups. Moreover, immunohistochemical staining of type II collagen and MMP-13 (an important type II collagen-degrading enzyme) indicated that the amount of type II collagen increased, whereas the number of MMP-13 positive chondrocytes decreased in the CP group compared with ACLT group. These observations suggest that CP has the potential to exert chondroprotective action on OA by inhibiting MMP-13 expression and type II collagen degeneration.

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Quantification of hydroxyprolyl-glycine (Hyp-Gly) in human blood after ingestion of collagen hydrolysate

Cited by 38 publications

References 9 publications

Antioxidant and Angiotensin 1 Converting Enzyme Inhibitory Functions from Chicken Collagen Hydrolysates

Antioxidant and Angiotensin 1 Converting Enzyme Inhibitory Functions from Chicken Collagen Hydrolysates

Biological Effect of Hydrolyzed Collagen on Bone Metabolism

Evaluation of the effect of oral administration of collagen peptides on an experimental rat osteoarthritis model

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