Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 20 de 145
Filtrar
Más filtros

País/Región como asunto
Tipo del documento
Intervalo de año de publicación
1.
J Sci Food Agric ; 104(9): 5244-5251, 2024 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-38308527

RESUMEN

BACKGROUND: Sturgeon is a popular aquaculture species in many countries. Its swim bladder is rich in collagen but has not yet been exploited scientifically. RESULTS: Collagen peptides (CPs) prepared from sturgeon swim bladder by trypsinolysis had an average molecular weight of 528.5 Da and consisted of 407 peptides, 16.1% of the content of which was GFPGADGSAGPK. The CPs at 25 mg mL-1 extended the lifespan of Caenorhabditis elegans by 22.6%, which was significantly higher than the extension achieved by other hydrolysis methods and source materials. They also improved fitness-related traits (body size, motor capacity, oxidative stress, cell apoptosis, and epidermal barrier function), indicating prolonged healthspan. Transcriptome analysis showed that the effect was mediated by the mitogen-activated protein kinase pathway, which enhanced stress resistance, the insulin/IGF-1 pathway, which inhibited protein aggregation, and the NHR-80/FAT-6 pathway, which regulated lipid metabolism. CONCLUSION: Collagen peptides from sturgeon swim bladder by trypsinolysis prolonged the lifespan and healthspan in C. elegans, and might be promising anti-aging agents. © 2024 Society of Chemical Industry.


Asunto(s)
Sacos Aéreos , Caenorhabditis elegans , Colágeno , Peces , Longevidad , Péptidos , Animales , Caenorhabditis elegans/efectos de los fármacos , Caenorhabditis elegans/genética , Caenorhabditis elegans/metabolismo , Caenorhabditis elegans/fisiología , Longevidad/efectos de los fármacos , Colágeno/metabolismo , Sacos Aéreos/química , Sacos Aéreos/metabolismo , Péptidos/farmacología , Péptidos/química , Peces/genética , Estrés Oxidativo/efectos de los fármacos , Proteínas de Peces/genética , Proteínas de Peces/metabolismo , Proteínas de Peces/química
2.
J Sci Food Agric ; 104(14): 8907-8915, 2024 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-38967325

RESUMEN

BACKGROUND: Sturgeon cartilage type II collagen peptides (SHCPs) can self-assemble and be used to prepare collagen peptide assemblies. Self-assembled peptides have great potential for applications in the food industry. In the present study, self-assembled peptides were prepared from sturgeon cartilage and then characterized. RESULTS: The SHCPs self-assembled and formed collagen peptide assemblies. After response surface experiment optimization, the optimal enzyme digestion process comprised 43.1 °C, 3.37 h and 0.96% enzyme addition, and the peptide yield was 78.46%. Physicochemical analysis showed that the SHCPs were amphiphilic, with an average molecular weight of 1081 Da, and were rich in hydrophobic amino acids. Peptide sequence identification showed that the peptides of SHCPs with polar amino acids followed by hydrophobic amino acids could be self-assembled through hydrogen bonding and hydrophobic interaction. Through turbidity experiments, Fourier transform infrared spectroscopy and scanning electron microscopy, we demonstrated that SHCPs can self-assemble into reticular and tubular structures under specific conditions. Furthermore, both the SHCPs-Ca and SHCPs-Mg assemblies were stabilized within a pH range consistent with that of the human gastrointestinal tract. CONCLUSION: The present study provides a simple and safe method for preparing novel self-assembled peptide materials from sturgeon by-products, providing a scientific basis for the exploitation of sturgeon cartilage and potentially reducing resource wastage. © 2024 Society of Chemical Industry.


Asunto(s)
Cartílago , Colágeno Tipo II , Proteínas de Peces , Peces , Interacciones Hidrofóbicas e Hidrofílicas , Péptidos , Animales , Cartílago/química , Proteínas de Peces/química , Péptidos/química , Colágeno Tipo II/química , Peso Molecular , Concentración de Iones de Hidrógeno , Secuencia de Aminoácidos , Espectroscopía Infrarroja por Transformada de Fourier , Enlace de Hidrógeno
3.
Molecules ; 28(19)2023 Sep 30.
Artículo en Inglés | MEDLINE | ID: mdl-37836729

RESUMEN

Antler ossified tissue has been widely used for the extraction of bioactive peptides. In this study, collagen was prepared from antler ossified tissue via acetic acid and pepsin. Five different proteases were used to hydrolyze the collagen and the hydrolysate treated by neutrase (collagen peptide named ACP) showed the highest DPPH radical clearance rate. The extraction process of ACP was optimized by response surface methodology, and the optimal conditions were as follows: a temperature of 52 °C, a pH of 6.1, and an enzyme concentration of 3200 U/g, which resulted in the maximum DPPH clearance rate of 74.41 ± 0.48%. The peptides (ACP-3) with the strongest antioxidant activity were obtained after isolation and purification, and its DPPH free radical clearance rate was 90.58 ± 1.27%; at the same time, it exhibited good scavenging activity for ABTS, hydroxyl radical, and superoxide anion radical. The study investigated the protective effect of ACP-3 on oxidative damage in HaCaT cells. The findings revealed that all groups that received ACP-3 pretreatment exhibited increased activities of SOD, GSH-Px, and CAT compared to the model group. Furthermore, ACP-3 pretreatment reduced the levels of ROS and MDA in HaCaT cells subjected to H2O2-induced oxidative damage. These results suggest that collagen peptides derived from deer antler ossified tissue can effectively mitigate the oxidative damage caused by H2O2 in HaCaT cells, thereby providing a foundation for the utilization of collagen peptides in pharmaceuticals and cosmetics.


Asunto(s)
Cuernos de Venado , Ciervos , Animales , Humanos , Antioxidantes/farmacología , Peróxido de Hidrógeno/farmacología , Células HaCaT , Estrés Oxidativo , Péptidos/farmacología , Colágeno/farmacología
4.
Molecules ; 28(2)2023 Jan 16.
Artículo en Inglés | MEDLINE | ID: mdl-36677946

RESUMEN

Type I and V collagens are the major components of fibrillogenic proteins in fish skin, and their hydrolysis products possess hyaluronidase inhibitory activity. In this study, for the first time, type I and V collagens were isolated from the skin of shortbill spearfish and striped marlin. Type I (2α1[I]α2[I]) and type V (α1[V]α3[V]α2[V]) collagens composed of distinct α-peptide chains with comparable structures were investigated using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and UV spectrophotometric chromatography. After enzymatic digestion, the collagen peptides were purified by using ultrafiltration (30 KDa) and high-performance liquid chromatography (RP-HPLC) to yield CPI-F3 and CPV-F4 fractions with strong hyaluronidase inhibition rates (42.17% and 30.09%, respectively). Based on the results of simulated gastrointestinal fluid, temperature, and pH stability assays, CPI-F3 and CPV-F4 exhibited stability in gastric fluid and showed no significant changes under the temperature range from 50 to 70 °C (p > 0.05). The results of this first research on the bioactivity of type V collagen peptides provide valuable information for the biomedical industry and show the potential for future bioactivity investigations of type V collagen and its peptides.


Asunto(s)
Colágeno Tipo V , Hialuronoglucosaminidasa , Animales , Colágeno Tipo V/análisis , Colágeno/química , Péptidos/farmacología , Péptidos/análisis , Peces/metabolismo , Piel/metabolismo , Electroforesis en Gel de Poliacrilamida
5.
Mar Drugs ; 20(5)2022 May 14.
Artículo en Inglés | MEDLINE | ID: mdl-35621976

RESUMEN

For making full use of aquatic by-products to produce high value-added products, Siberian sturgeon (Acipenser baerii) cartilages were degreased, mineralized, and separately hydrolyzed by five kinds of proteases. The collagen hydrolysate (SCH) generated by Alcalase showed the strongest 2,2-diphenyl-1-picrylhydrazyl radical (DPPH·) and hydroxide radical (HO·) scavenging activity. Subsequently, thirteen antioxidant peptides (SCP1-SCP3) were isolated from SCH, and they were identified as GPTGED, GEPGEQ, GPEGPAG, VPPQD, GLEDHA, GDRGAEG, PRGFRGPV, GEYGFE, GFIGFNG, PSVSLT, IELFPGLP, LRGEAGL, and RGEPGL with molecular weights of 574.55, 615.60, 583.60, 554.60, 640.64, 660.64, 885.04, 700.70, 710.79, 602.67, 942.12, 714.82, and 627.70 Da, respectively. GEYGFE, PSVSLT, and IELFPGLP showed the highest scavenging activity on DPPH· (EC50: 1.27, 1.05, and 1.38 mg/mL, respectively) and HO· (EC50: 1.16, 0.97, and 1.63 mg/mL, respectively), inhibiting capability of lipid peroxidation, and protective functions on H2O2-damaged plasmid DNA. More importantly, GEYGFE, PSVSLT, and IELFPGLP displayed significant cytoprotection on HUVECs against H2O2 injury by regulating the endogenous antioxidant enzymes of superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) to decrease the contents of reactive oxygen species (ROS) and malondialdehyde (MDA). Therefore, the research provided better technical assistance for a higher-value utilization of Siberian sturgeon cartilages and the thirteen isolated peptides-especially GEYGFE, PSVSLT, and IELFPGLP-which may serve as antioxidant additives for generating health-prone products to treat chronic diseases caused by oxidative stress.


Asunto(s)
Antioxidantes , Citoprotección , Animales , Cartílago , Colágeno , Peces , Células Endoteliales de la Vena Umbilical Humana , Humanos , Peróxido de Hidrógeno/farmacología , Péptidos/química , Péptidos/farmacología
6.
Mar Drugs ; 19(12)2021 Nov 27.
Artículo en Inglés | MEDLINE | ID: mdl-34940675

RESUMEN

Bovine bone is rich in collagen and is a good material for collagen peptide preparation. Although thermolysin-like proteases (TLPs) have been applied in different fields, the potential of TLPs in preparing bioactive collagen peptides has rarely been evaluated. Here, we characterized a thermophilic TLP, A69, from a hydrothermal bacterium Anoxybacillus caldiproteolyticus 1A02591, and evaluated its potential in preparing bioactive collagen peptides. A69 showed the highest activity at 60 °C and pH 7.0. We optimized the conditions for bovine bone collagen hydrolysis and set up a process with high hydrolysis efficiency (99.4%) to prepare bovine bone collagen peptides, in which bovine bone collagen was hydrolyzed at 60 °C for 2 h with an enzyme-substrate ratio of 25 U/g. The hydrolysate contained 96.5% peptides that have a broad molecular weight distribution below 10000 Da. The hydrolysate showed good moisture-retention ability and a high hydroxyl radical (•OH) scavenging ratio of 73.2%, suggesting that the prepared collagen peptides have good antioxidative activity. Altogether, these results indicate that the thermophilic TLP A69 has promising potential in the preparation of bioactive collagen peptides, which may have potentials in cosmetics, food and pharmaceutical industries. This study lays a foundation for the high-valued utilization of bovine bone collagen.


Asunto(s)
Anoxybacillus , Antioxidantes/farmacología , Colágeno/farmacología , Metaloendopeptidasas/química , Péptidos/farmacología , Animales , Antioxidantes/química , Bovinos , Colágeno/química , Péptidos/química
7.
Skin Pharmacol Physiol ; 34(3): 115-127, 2021.
Artículo en Inglés | MEDLINE | ID: mdl-33774639

RESUMEN

INTRODUCTION: We aimed to investigate the effect of orally ingested collagen peptides (CPs) on skin condition and elucidate their mechanism of action. METHODS: A randomized, placebo-controlled, double-blind trial was conducted in 99 healthy Japanese women, aged 35-50 years. The subjects were randomized into 3 groups (33 subjects/group) to receive 1 or 5 g of CP or placebo once daily for 12 weeks. Skin water content, transepidermal water loss (TEWL), skin elasticity, and skin thickness were evaluated before treatment and after 4, 8, and 12 weeks of treatment. The level of natural moisturizing factor (NMF) constituents in the stratum corneum (SC) was quantified before treatment and after 12 weeks of treatment. RESULTS: Oral ingestion of CP increased the water content in the SC and epidermis and decreased TEWL. Furthermore, the NMF level in the SC was increased. However, skin elasticity and skin thickness remained unchanged. CONCLUSIONS: The improvement in skin water content following the oral ingestion of CP can be attributed to an increase in the level of NMF in the SC. TRIAL REGISTRATION: UMIN000030375 (retrospectively registered).


Asunto(s)
Colágeno/farmacología , Péptidos/farmacología , Piel/efectos de los fármacos , Adulto , Relación Dosis-Respuesta a Droga , Método Doble Ciego , Femenino , Humanos , Persona de Mediana Edad , Piel/metabolismo
8.
J Food Sci Technol ; 58(1): 377-382, 2021 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-33505082

RESUMEN

The purpose of this study is to examine the possibility of use in various fields such as cosmetics and food industry by extracting, separating, and purifying canola glycoprotein(hreinafter referred to as CNG) and comparing general characteristics and physiological activities with commercially available carrot glycoprotein(hreinafter referred to as CRG). The CNG had a protein content of 13.12%, which is higher than that of common vegetable glycoproteins, and much higher than the CRG of 2.36%. The molecular weight distribution of the CNG was 263-310 Da, which showed a lower molecular weight distribution than the 566-628 Da of the CRG. The total polyphenol content of the CNG was 29.89 mg/g, which was higher than that of the CRG measured at 1.76 mg g-1. The DPPP radical scavenging activity of CNG and carrot glycoprotein were 10.07 mg mL-1 and 7.76 mg mL-1, respectively, indicating that CNG had slightly higher electron donating ability than CRG. Total antioxidant activity of CNG was 26.84 mg AA eq/g and CRG was 10.53 mg AA eq/g.

9.
Molecules ; 25(4)2020 Feb 12.
Artículo en Inglés | MEDLINE | ID: mdl-32059436

RESUMEN

Oral administration of bovine collagen peptide (CP) combined with calcium citrate (CC) has been found to inhibit bone loss in ovariectomized rats. However, the protective effects of CP and CP-CC against bone loss have not been investigated in a tail-suspension simulated microgravity (SMG) rat model. Adult Sprague-Dawley rats (n = 40) were randomly divided into five groups (n = 8): a control group with normal gravity, a SMG control group, and three SMG groups that underwent once-daily gastric gavage with CP (750 mg/kg body weight), CC (75 mg/kg body weight) or CP-CC (750 and 75 mg/kg body weight, respectively) for 28 days. After sacrifice, the femurs were analyzed by dual-energy X-ray absorptiometry, three-point bending mechanical tests, microcomputed tomography, and serum bone metabolic markers. Neither CP nor CP-CC treatment significantly inhibited bone loss in SMG rats, as assessed by dual-energy X-ray absorptiometry and three-point bending mechanical tests. However, both CP and CP-CC treatment were associated with partial prevention of the hind limb unloading-induced deterioration of bone microarchitecture, as demonstrated by improvements in trabecular number and trabecular separation. CP-CC treatment increased serum osteocalcin levels. Dietary supplementation with CP or CP-CC may represent an adjunct strategy to reduce the risk of fracture in astronauts.


Asunto(s)
Enfermedades Óseas Metabólicas/tratamiento farmacológico , Citrato de Calcio/farmacología , Colágeno/farmacología , Péptidos/farmacología , Animales , Densidad Ósea/efectos de los fármacos , Enfermedades Óseas Metabólicas/diagnóstico por imagen , Enfermedades Óseas Metabólicas/metabolismo , Enfermedades Óseas Metabólicas/patología , Bovinos , Colágeno/química , Fémur/diagnóstico por imagen , Fémur/efectos de los fármacos , Fémur/patología , Suspensión Trasera/métodos , Humanos , Ovariectomía , Péptidos/química , Ratas , Ratas Sprague-Dawley , Cola (estructura animal)/diagnóstico por imagen , Cola (estructura animal)/efectos de los fármacos , Cola (estructura animal)/fisiopatología , Microtomografía por Rayos X
10.
Mar Drugs ; 17(8)2019 Jul 31.
Artículo en Inglés | MEDLINE | ID: mdl-31370332

RESUMEN

The effect of collagen peptides (CPs) in intestinal mucosal protection has been approved in both cell and animal models. However, its structure-activity relationship and efficient peptide sequences are unclear, which hinders the in-depth study of its action mechanism and relative nutraceuticals and pharmaceuticals development. In this work, size exclusion chromatography, cation-exchange chromatography, and RP-HPLC were used to separate Alaska pollock skin-derived collagen hydrolysates based on their molecular weight, charge property, and hydrophobicity. The intestinal epithelial barrier function (IEBF) protective effect of separated peptide fractions were evaluated by tumor necrosis factor (TNF)-α-induced Caco-2 cell model. Results indicated that lower molecular weight (500-1000 Da) and higher hydrophilicity of CPs were related to better IEBF protective effect. Two high-efficiency IEBF protective peptide sequences, GPSGPQGSR and GPSGLLGPK with the corresponding molecular weights of 841.41 Da and 824.38 Da, were subsequently identified by UPLC-QToF-MS/MS. Their IEBF protective ability are comparable or even better than the currently used intestinal health supplements glutamine and arginine. The present findings suggested that the hydrophilic CPs, with molecular weight between 500 Da to 1000 Da, should be preferred in IEBF protective peptides preparation. GPSGPQGSR and GPSGLLGPK might have the potential of being IEBF protective ingredients used in intestinal health supplements and drugs.


Asunto(s)
Colágeno/farmacología , Gadiformes , Mucosa Intestinal/efectos de los fármacos , Péptidos/farmacología , Alaska , Animales , Células CACO-2 , Colágeno/química , Colágeno/aislamiento & purificación , Suplementos Dietéticos , Humanos , Interacciones Hidrofóbicas e Hidrofílicas , Mucosa Intestinal/citología , Mucosa Intestinal/metabolismo , Peso Molecular , Péptidos/química , Péptidos/aislamiento & purificación , Permeabilidad/efectos de los fármacos , Relación Estructura-Actividad , Espectrometría de Masas en Tándem
11.
Int J Mol Sci ; 21(1)2019 Dec 28.
Artículo en Inglés | MEDLINE | ID: mdl-31905705

RESUMEN

Prolyl-hydroxyproline (Pro-Hyp) and hydroxyprolyl-glycine (Hyp-Gly) appear in human blood after ingestion of collagen hydrolysate and trigger growth of fibroblasts attached on collagen gel, which has been associated with beneficial effects upon ingestion of collagen hydrolysate, such as improvement of skin and joint conditions. In the present study, inconsistent results were obtained by using different lots of fetal bovine serum (FBS). Fibroblasts proliferated in collagen gel without adding Pro-Hyp and Hyp-Gly and did not respond to addition of Pro-Hyp and Hyp-Gly, which raises doubts about conclusions from prior research. Unexpectedly high levels of hydroxyprolyl peptides, including Pro-Hyp, however, were present in the FBS (approximately 100 µM), and also in other commercially available forms of FBS (70-80 µM). After removal of low molecular weight (LMW, < 6000 Da) compounds from the FBS by size exclusion chromatography, Pro-Hyp and Hyp-Gly again triggered growth of fibroblasts attached on collagen and increased the number of fibroblasts migrated from mouse skin. These results indicate the presence of bioactive hydroxyprolyl peptides in commercially available FBS, which can mask effects of Pro-Hyp and Hyp-Gly supplementation; our work confirms that Pro-Hyp and Hyp-Gly do play crucial roles in proliferation of fibroblasts.


Asunto(s)
Proliferación Celular , Dipéptidos/farmacología , Fibroblastos/efectos de los fármacos , Animales , Bovinos , Células Cultivadas , Colágeno/farmacología , Fibroblastos/fisiología , Masculino , Ratones , Ratones Endogámicos BALB C , Suero/química , Piel/citología
12.
Biosci Biotechnol Biochem ; 82(5): 893-895, 2018 May.
Artículo en Inglés | MEDLINE | ID: mdl-29447076

RESUMEN

We examined whether baPWV could be affected by pork collagen peptide (CP) ingestion. Seventy subjects were randomized into two groups (2.5 g/day CP and 2.5 g/day placebo). A significant reduction in baPWV was observed in the CP group compared to the placebo group. This study demonstrated that pork CP may contribute to the prevention of atherosclerosis in elderly.

13.
Mar Drugs ; 16(12)2018 Nov 23.
Artículo en Inglés | MEDLINE | ID: mdl-30477144

RESUMEN

Recently, the bioactive properties of marine collagen and marine collagen hydrolysates have been demonstrated. Although there is some literature assessing the general chemical features and biocompatibility of collagen extracts from marine sponges, no data are available on the biological effects of sponge collagen hydrolysates for biomedical and/or cosmetic purposes. Here, we studied the in vitro toxicity, antioxidant, wound-healing, and photoprotective properties of four HPLC-purified fractions of trypsin-digested collagen extracts-marine collagen hydrolysates (MCHs)-from the marine sponge C. reniformis. The results showed that the four MCHs have no degree of toxicity on the cell lines analyzed; conversely, they were able to stimulate cell growth. They showed a significant antioxidant activity both in cell-free assays as well as in H2O2 or quartz-stimulated macrophages, going from 23% to 60% of reactive oxygen species (ROS) scavenging activity for the four MCHs. Finally, an in vitro wound-healing test was performed with fibroblasts and keratinocytes, and the survival of both cells was evaluated after UV radiation. In both experiments, MCHs showed significant results, increasing the proliferation speed and protecting from UV-induced cell death. Overall, these data open the way to the use of C. reniformis MCHs in drug and cosmetic formulations for damaged or photoaged skin repair.


Asunto(s)
Organismos Acuáticos , Depuradores de Radicales Libres/farmacología , Péptidos/farmacología , Poríferos , Protectores Solares/farmacología , Cicatrización de Heridas/efectos de los fármacos , Animales , Colágeno/química , Evaluación Preclínica de Medicamentos , Fibroblastos , Depuradores de Radicales Libres/química , Depuradores de Radicales Libres/aislamiento & purificación , Humanos , Peróxido de Hidrógeno/metabolismo , Queratinocitos , Ratones , Péptidos/química , Péptidos/aislamiento & purificación , Células RAW 264.7 , Envejecimiento de la Piel/efectos de los fármacos , Envejecimiento de la Piel/efectos de la radiación , Protectores Solares/química , Protectores Solares/aislamiento & purificación , Rayos Ultravioleta/efectos adversos
14.
Mar Drugs ; 16(9)2018 Aug 30.
Artículo en Inglés | MEDLINE | ID: mdl-30200239

RESUMEN

This study investigated the anti-obesity effects of collagen peptide derived from skate skin on lipid metabolism in high-fat diet (HFD)-fed mice. All C57BL6/J male mice were fed a HFD with 60% kcal fat except for mice in the normal group which were fed a chow diet. The collagen-fed groups received collagen peptide (1050 Da) orally (100, 200, or 300 mg/kg body weight per day) by gavage, whereas the normal and control groups were given water (n = 9 per group). The body weight gain and visceral adipose tissue weight were lower in the collagen-fed groups than in the control group (p < 0.05). Plasma and hepatic lipid levels were significantly reduced by downregulating the hepatic protein expression levels for fatty acid synthesis (sterol regulatory element binding protein-1 (SREBP-1), fatty acid synthase (FAS), and acetyl-CoA carboxylase (ACC)) and cholesterol synthesis (SREBP-2 and 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR)) and upregulating those for ß-oxidation (peroxisome proliferator-activated receptor alpha (PPAR-α) and carnitine palmitoyltransferase 1 (CPT1)) and synthesis of bile acid (cytochrome P450 family 7 subfamily A member 1 (CYP7A1)) (p < 0.05). In the collagen-fed groups, the hepatic protein expression level of phosphorylated 5' adenosine monophosphate-activated protein kinase (p-AMPK) and plasma adiponectin levels were higher, and the leptin level was lower (p < 0.05). Histological analysis revealed that collagen treatment suppressed hepatic lipid accumulation and reduced the lipid droplet size in the adipose tissue. These effects were increased in a dose-dependent manner. The findings indicated that skate collagen peptide has anti-obesity effects through suppression of fat accumulation and regulation of lipid metabolism.


Asunto(s)
Colágeno/farmacología , Metabolismo de los Lípidos/efectos de los fármacos , Obesidad/tratamiento farmacológico , Péptidos/farmacología , Rajidae , Tejido Adiposo/efectos de los fármacos , Tejido Adiposo/patología , Animales , Colágeno/aislamiento & purificación , Colágeno/uso terapéutico , Dieta Alta en Grasa/efectos adversos , Modelos Animales de Enfermedad , Relación Dosis-Respuesta a Droga , Evaluación Preclínica de Medicamentos , Humanos , Masculino , Ratones , Ratones Endogámicos C57BL , Obesidad/etiología , Obesidad/metabolismo , Obesidad/patología , Péptidos/aislamiento & purificación , Péptidos/uso terapéutico , Piel
15.
Mar Drugs ; 16(12)2018 Dec 03.
Artículo en Inglés | MEDLINE | ID: mdl-30513923

RESUMEN

Aging-associated changes of skin conditions are a major concern for maintaining quality of life. Therefore, the improvement of skin conditions by dietary supplementation is a topic of public interest. In this study, we hypothesized that a composite supplement containing fish derived-collagen peptide and ornithine (CPO) could improve skin conditions by increasing plasma growth hormone and/or insulin-like growth factor-1 (IGF-1) levels. Twenty-two healthy Japanese participants were enrolled in an 8-week double-blind placebo-controlled pilot study. They were assigned to either a CPO group, who were supplemented with a drink containing CPO, or an identical placebo group. We examined skin conditions including elasticity and transepidermal water loss (TEWL), as well as plasma growth hormone and IGF-1 levels. Skin elasticity and TEWL were significantly improved in the CPO group compared with the placebo group. Furthermore, only the CPO group showed increased plasma IGF-1 levels after 8 weeks of supplementation compared with the baseline. Our results might suggest the novel possibility for the use of CPO to improve skin conditions by increasing plasma IGF-1 levels.


Asunto(s)
Suplementos Dietéticos , Proteínas de Peces/administración & dosificación , Factor I del Crecimiento Similar a la Insulina/análisis , Envejecimiento de la Piel/efectos de los fármacos , Piel/efectos de los fármacos , Adulto , Colágeno/administración & dosificación , Método Doble Ciego , Elasticidad/efectos de los fármacos , Femenino , Voluntarios Sanos , Humanos , Japón , Masculino , Persona de Mediana Edad , Ornitina/administración & dosificación , Péptidos/administración & dosificación , Proyectos Piloto , Calidad de Vida
16.
Int J Mol Sci ; 19(11)2018 Nov 11.
Artículo en Inglés | MEDLINE | ID: mdl-30423867

RESUMEN

Collagen peptide (CP) has beneficial effects on functions of the skin, such as skin barrier function and skin elasticity, in vivo. However, there are few studies investigating the mechanism underlying the potential effects of CP in skin epidermal moisturization after ultraviolet B (UVB) irradiation. In this study, we examined whether orally-administered CP affects the loss of skin hydration induced by UVB irradiation in hairless mice. SKH-1 hairless mice were orally administered CP at two doses (500 and 1000 mg/kg) for nine weeks, and the dorsal skin was exposed to UVB. The potential effects of CP were evaluated by measuring the transepidermal water loss (TEWL), skin hydration, wrinkle formation, and hyaluronic acid expression in the dorsal mice skin. We found that oral administration of CP increased skin hydration and decreased wrinkle formation compared to the UVB-irradiated group. Treatment of CP increased the mRNA and protein expression of hyaluronic acid synthases (HAS-1 and -2) concomitant with an increased hyaluronic acid production in skin tissue. The expression of hyaluronidase (HYAL-1 and 2) mRNA was downregulated in the CP-treated group. In addition, the protein expression of skin-hydrating factors, filaggrin and involucrin, was upregulated via oral administration of CP. In summary, these results show that oral administration of CP increases hyaluronic acid levels, which decreases during UVB photoaging. Therefore, we suggest that CP can be used as a nutricosmetic ingredient with potential effects on UVB-induced skin dehydration and moisture loss in addition to wrinkle formation.


Asunto(s)
Colágeno/administración & dosificación , Colágeno/uso terapéutico , Deshidratación/tratamiento farmacológico , Ácido Hialurónico/biosíntesis , Péptidos/administración & dosificación , Péptidos/uso terapéutico , Piel/efectos de la radiación , Rayos Ultravioleta , Administración Oral , Animales , Colágeno/farmacología , Epidermis/efectos de los fármacos , Epidermis/patología , Epidermis/efectos de la radiación , Hialuronoglucosaminidasa/genética , Hialuronoglucosaminidasa/metabolismo , Masculino , Ratones Pelados , Péptidos/farmacología , ARN Mensajero/genética , ARN Mensajero/metabolismo , Envejecimiento de la Piel/efectos de los fármacos , Envejecimiento de la Piel/efectos de la radiación , Tilapia , Pérdida Insensible de Agua
17.
Molecules ; 23(12)2018 Dec 10.
Artículo en Inglés | MEDLINE | ID: mdl-30544714

RESUMEN

A total of 13 batches of collagen peptide samples were extracted, isolated, and purified from chicken sternal cartilage under various process parameters. The fingerprint profiles of 13 batches of collagen peptides were established by high-performance liquid chromatography (HPLC). In addition, the amino acid profiles and molecular weight distributions of collagen peptides were investigated. The in vitro antioxidant activities of the peptide samples were measured using the 2,2'-Azinobis (3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS) assay, the 2,2-diphenyl-1-picrylhydrazyl (DPPH) assay, the ferric-reducing antioxidant power (FRAP) assay and an assay of the oxidative damage induced by hydrogen peroxide (H2O2) in the degenerative cartilage cells from the knee joint of rat C518 (C518 cell line). The anti-inflammatory activities of the peptide samples were assessed by measuring the inflammatory responses induced by lipopolysaccharides (LPSes) in C518 cells. Subsequently, the spectrum-effect relationships between HPLC fingerprints and the antioxidant and anti-inflammatory activities of collagen peptides were investigated using grey relational analysis (GRA). Fifteen common peaks were obtained from the HPLC fingerprints of collagen peptides. Each collagen peptide sample had a characteristic set of amino acid types and contents. All of the hydrolysates of the collagen peptides were primarily composed of fractions II (500⁻1000 Da) and III (1000⁻3000 Da). Collagen peptides exhibited good scavenging activity on ABTS radical, DPPH radical, and ferric-reducing antioxidant power. Collagen peptides were also effective against H2O2-induced cellular oxidative damage in C518 cells. The antioxidant activity of collagen peptides was due to the low molecular weight and the presence of antioxidant and hydrophobic amino acid residues within its sequence. Collagen peptides significantly inhibited the secretion of inflammatory cytokines IL-1ß, TNF-α, and PGE2 in C518 cells. The anti-inflammatory activity of collagen peptides may include increased synthesis of the key components of extracellular matrix (ECM) and inhibited apoptosis of chondrocytes. The GRA results showed that peaks 2, 3, and 8 were the main components contributing to the antioxidant activity of the collagen peptides, whereas peaks 11 and 14 were the main components contributing to the anti-inflammatory activity of the collagen peptides. The components of peaks 8 and 14 were identified as GPRGPPGPVGP and VAIQAVLSLYASGR by UPLC-MS/MS. Those identified collagen peptides offer a potential therapeutic strategy for the treatment of osteoarthritis (OA) due to their antioxidative stress and due to them disturbing the catabolism and anabolism processes in arthrodial cartilage.


Asunto(s)
Antiinflamatorios/farmacología , Antioxidantes/farmacología , Condrocitos/citología , Colágeno/química , Peróxido de Hidrógeno/efectos adversos , Péptidos/farmacología , Animales , Antiinflamatorios/química , Antioxidantes/química , Línea Celular , Pollos , Condrocitos/efectos de los fármacos , Condrocitos/metabolismo , Cromatografía Líquida de Alta Presión , Citocinas/efectos de los fármacos , Citocinas/metabolismo , Modelos Animales de Enfermedad , Humanos , Estrés Oxidativo/efectos de los fármacos , Péptidos/química , Ratas
18.
J Sci Food Agric ; 98(5): 1944-1950, 2018 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-28914450

RESUMEN

BACKGROUND: Daily ingestion of collagen hydrolysate for a long period improves skin and joint conditions. It has been speculated that the beneficial effects are exerted by food-derived hydroxyproline (Hyp) peptides, which are detected in human blood after single ingestions. In the present study, to investigate the effect of long-term ingestion of collagen hydrolysate on Hyp peptides profile in blood, the concentrations of Hyp-peptides in human blood before and after daily ingestion for a long period were examined. RESULTS: Hyp-peptides increased to a maximum level at 1 h after ingestion and reverted to their initial levels within 24 h during experimental period. Pro-Gly and Hyp-peptides such as Pro-Hyp-Gly, Pro-Hyp, Ile-Hyp, Leu-Hyp, Hyp-Gly, Glu-Hyp and Ala-Hyp were identified in the blood after ingestion of collagen hydrolysate at 4.5 g day-1 for 4 weeks. For the whole period, Pro-Hyp was the leading compound. The compositional rate of Hyp-Gly showed a tendency to increase, while that of Pro-Hyp tended to decrease after daily ingestion. CONCLUSION: The present results indicate that daily ingestion of collagen hydrolysate for a long period can change compositional rate of Hyp peptides in human blood. This fact suggests that long-term ingestion of collagen hydrolysate might change exo- or endo-type protease activity in the digestive tract, which may consequently promote beneficial effects. © 2017 Society of Chemical Industry.


Asunto(s)
Colágeno/química , Colágeno/metabolismo , Péptidos/sangre , Hidrolisados de Proteína/química , Adulto , Animales , Femenino , Gelatina/química , Gelatina/metabolismo , Humanos , Persona de Mediana Edad , Péptidos/química , Hidrolisados de Proteína/metabolismo , Piel/química , Porcinos , Adulto Joven
19.
J Food Sci Technol ; 55(6): 2310-2317, 2018 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-29892131

RESUMEN

Milkfish (Chanos chanos), which is resistant to water quality changes is the fourth largest aquaculture commodity. Abandoned wastes of fish scale and bones aggravate environmental pollution. In this study, the effect of collagen peptides isolated from milkfish scales (MSCP) by pepsin-soluble collagen method on cell viability was investigated. The antioxidant, anti-inflammatory, and DNA-protective activities of MSCP were also evaluated. Results revealed that more than 95% of viable cells were retained in human keratinocytes after addition of 100 mg/mL MSCP. Measurement of DPPH· and ABTS· + radical scavenging activities and cellular reactive oxygen species revealed the high antioxidant activities of MSCP. MSCP demonstrated anti-inflammatory activities by reducing lipoxygenase activity and nitric oxide (NO·) radicals. Moreover, DNA electrophoresis assay indicated that MSCP treatment can directly protect against cyclobutane di-pyrimidine production and DNA single-strand breaks, which are harmful effects of UV radiation and H2O2. Given its antioxidant, anti-inflammatory, and DNA-protective activities, MSCP has potential applications in cosmeceuticals and supplementary health food.

20.
Br J Nutr ; 117(1): 1-11, 2017 01.
Artículo en Inglés | MEDLINE | ID: mdl-28091360

RESUMEN

Ingestion of collagen peptide (CP) elicits beneficial effects on the body, including improvement in blood lipid profiles, but the underlying mechanisms remain unclear. The purpose of this study was to investigate the effects of CP ingestion on the liver, which controls lipid metabolism in the body. Male BALB/cCrSlc mice were bred with the AIN-93M diet containing 14 % casein or the AIN-93M-based low-protein diet containing 10 % casein or a diet containing 6 % casein+4 % CP for 10 weeks (n 12/group). Total, free and esterified cholesterol levels in the blood decreased in the CP group. DNA microarray analysis of the liver revealed that expressions of genes related to lipid metabolic processes such as the PPAR signalling pathway and fatty acid metabolism increased in the CP group compared with the 10 % casein group. The expressions of several genes involved in steroid metabolic process, including Cyp7a1 and Cyp8b1, were decreased, despite being targets of transcriptional regulation by PPAR. These data suggest that lipid metabolism in the liver is altered by CP ingestion, and the decrease in blood cholesterol levels in the CP group is not due to enhancement of the steroid metabolic process. On the other hand, expressions of genes related to the unfolded protein response (UPR) significantly decreased at the mRNA level, suggesting that CP ingestion lowers endoplasmic reticulum stress. Indeed, protein levels of phosphorylated inositol-requiring enzyme 1 decreased after CP ingestion. Taken together, CP affects the broader pathways in the liver - not only lipid metabolism but also UPR.


Asunto(s)
Colágeno/farmacología , Regulación de la Expresión Génica/efectos de los fármacos , Metabolismo de los Lípidos/fisiología , Hígado/metabolismo , Respuesta de Proteína Desplegada/efectos de los fármacos , Administración Oral , Animales , Colágeno/administración & dosificación , Metabolismo de los Lípidos/genética , Masculino , Ratones
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA