Dose-dependent changes in the levels of free and peptide forms of hydroxyproline in human plasma after collagen hydrolysate ingestion

Shigemura, Yasutaka; Kubomura, Daiki; Satō, Yoshio; Satô, Kenji

doi:10.1016/j.foodchem.2014.02.091

Cited by 56 publications

(45 citation statements)

References 25 publications

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“…Porcine skin gelatin hydrolysates (Huang, Hung, Jao, Tung, & Hsu, 2014) and salmon skin gelatin hydrolysates (Hsieh, Wang, Hung, Chen, & Hsu, 2015) have been proven to inhibit plasma DPP-IV in rats. Hyp-containing peptides were detected in human plasma after the ingestion of a collagen hydrolysate and exerted beneficial effects on human health (Shigemura, Kubomura, Sato, & Sato, 2014). This result indicates that Hyp-containing DPP-IV inhibitory peptides may resist gastrointestinal proteases/ peptidases and exert effects in vivo in human plasma.The results described herein demonstrate that peptides with a Pro residue at the penultimate position from deer skin hydrolysate contribute to the DPP-IV inhibition activity of deer collagen hydrolysates.…”

Section: Discussionmentioning

confidence: 84%

Screening and identification of DPP-IV inhibitory peptides from deer skin hydrolysates by an integrated approach of LC–MS/MS and in silico analysis

Jin

Yan

et al. 2015

Journal of Functional Foods

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Section: Discussionmentioning

confidence: 84%

Screening and identification of DPP-IV inhibitory peptides from deer skin hydrolysates by an integrated approach of LC–MS/MS and in silico analysis

Jin

Yan

et al. 2015

Journal of Functional Foods

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“…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). Moreover, the quantity and structure of such Hyp-containing peptides in human blood after oral administration of HC depends on the source; for example, Ala-Hyp-Gly and Ser-Hyp-Gly were detected only from fish scale gelatin hydrolysate, Ala-Hyp and Pro-Hyp-Gly from fish scale or fish skin gelatin hydrolysates, whereas Leu-Hyp, Ile-Hyp and Phe-Hyp appeared after ingestion of fish and to a lower level porcine skin originated HC (Ohara et al, 2007).…”

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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“…hCol1 is a mixture of type I collagen peptides of different molecular weights that are generated via enzymatic digestion of type I collagen extracted from animal connective tissues. The peptide mixture, which contains an abundance of hydroxyproline, proline and glycine, is absorbed dose-dependently following bolus oral delivery [13], with a series of di- and tri-peptides peaking in the circulation within one hour after consumption in humans [14]. hCol1 is considered safe as an oral supplement [15], and when consumed daily, beneficial effects have been observed in bone [16] and skin [17, 18].…”

Section: Introductionmentioning

confidence: 99%

Daily oral consumption of hydrolyzed type 1 collagen is chondroprotective and anti-inflammatory in murine posttraumatic osteoarthritis

et al. 2017

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Osteoarthritis (OA) is a degenerative joint disease for which there are no disease modifying therapies. Thus, strategies that offer chondroprotective or regenerative capability represent a critical unmet need. Recently, oral consumption of a hydrolyzed type 1 collagen (hCol1) preparation has been reported to reduce pain in human OA and support a positive influence on chondrocyte function. To evaluate the tissue and cellular basis for these effects, we examined the impact of orally administered hCol1 in a model of posttraumatic OA (PTOA). In addition to standard chow, male C57BL/6J mice were provided a daily oral dietary supplement of hCol1 and a meniscal-ligamentous injury was induced on the right knee. At various time points post-injury, hydroxyproline (hProline) assays were performed on blood samples to confirm hCol1 delivery, and joints were harvested for tissue and molecular analyses were performed, including histomorphometry, OARSI and synovial scoring, immunohistochemistry and mRNA expression studies. Confirming ingestion of the supplements, serum hProline levels were elevated in experimental mice administered hCol1. In the hCol1 supplemented mice, chondroprotective effects were observed in injured knee joints, with dose-dependent increases in cartilage area, chondrocyte number and proteoglycan matrix at 3 and 12 weeks post-injury. Preservation of cartilage and increased chondrocyte numbers correlated with reductions in MMP13 protein levels and apoptosis, respectively. Supplemented mice also displayed reduced synovial hyperplasia that paralleled a reduction in Tnf mRNA, suggesting an anti-inflammatory effect. These findings establish that in the context of murine knee PTOA, daily oral consumption of hCol1 is chondroprotective, anti-apoptotic in articular chondrocytes, and anti-inflammatory. While the underlying mechanism driving these effects is yet to be determined, these findings provide the first tissue and cellular level information explaining the already published evidence of symptom relief supported by hCol1 in human knee OA. These results suggest that oral consumption of hCol1 is disease modifying in the context of PTOA.

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Dose-dependent changes in the levels of free and peptide forms of hydroxyproline in human plasma after collagen hydrolysate ingestion

Cited by 56 publications

References 25 publications

Screening and identification of DPP-IV inhibitory peptides from deer skin hydrolysates by an integrated approach of LC–MS/MS and in silico analysis

Screening and identification of DPP-IV inhibitory peptides from deer skin hydrolysates by an integrated approach of LC–MS/MS and in silico analysis

Biological Effect of Hydrolyzed Collagen on Bone Metabolism

Daily oral consumption of hydrolyzed type 1 collagen is chondroprotective and anti-inflammatory in murine posttraumatic osteoarthritis

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