Collagen Research

Collagen benefits are wide ranging because collagen is at the foundation of most structural tissues – so beauty benefits like skin wrinkle reduction go hand in hand with joint benefits like ligament and tendon support. Collagen research has been investigating the efficacy of collagen supplements for quite some time now. Undeniably, NeoCell collagen supplements work for a wide range of issues. The following are quotes from published research studies if you’d like to hear it from the researcher’s mouths themselves:

Collagen and Skin

Effects of collagen tripeptide supplement on skin properties: A prospective, randomized, controlled study
“We investigated to evaluate the effect of daily collagen peptide (CP) supplement on skin properties… Conclusions: Daily CP supplementation may improve skin hydration and elasticity…”
J Cosmet Laser Ther. 2013 Oct 16. Choi SY, Ko EJ, Lee YH, Kim BG, Shin HJ, Seo DB, Lee SJ, Kim BJ, Kim MN

Oral supplementation of specific collagen peptides has beneficial effects on human skin physiology: A double-blind, placebo-controlled study
“The objective of this research was to study the effectiveness of collagen hydrolysate (CH) composed of specific collagen peptides on skin biophysical parameters related to cutaneous aging…At the end of the study, skin elasticity in both CH dosage groups showed a statistically significant improvement in comparison to placebo. After 4 weeks of follow-up treatment, a statistically significantly higher skin elasticity level was determined in elderly women…No side effects were noted throughout the study.”
Skin Pharmacol Physiol. 2014;27(1):47-55. Proksch E, Segger D, Degwert J, Schunck M, Zague V, Oesser S.

Effects of collagen peptide ingestion on UV-B-induced skin damage
“The effect of daily ingestion of collagen peptide on the skin damage induced by repeated UV-B irradiation was examined. Ingestion of collagen peptide (0.2 g/kg/d) suppressed UV-B-induced decreases in skin hydration, hyperplasia of the epidermis, and decreases in soluble type I collagen. These results suggest that collagen peptide is beneficial as a dietary supplement to suppress UV-B-induced skin damage and photoaging.”
Biosci Biotechnol Biochem. 2009 Apr 23;73(4):930-2. Epub 2009 Apr 7. Tanaka M, Koyama Y, Nomura Y.

Collagen-derived dipeptide, proline-hydroxyproline, stimulates cell proliferation and hyaluronic acid synthesis in cultured human dermal fibroblasts
“Orally ingested collagen undergoes degradation to small di- or tripeptides, which are detected in circulating blood 2 h after ingestion. The influence of collagen-derived peptides on dermal extracellular matrix components and cell proliferation was studied using cultured human dermal fibroblasts. Of the various collagenous peptides tested here, the dipeptide proline-hydroxyproline (Pro-Hyp) enhanced cell proliferation (1.5-fold) and hyaluronic acid synthesis (3.8-fold)…These results suggest that Pro-Hyp stimulates both cell mitotic activity and hyaluronic acid synthesis…”
J Dermatol. 2010 Apr;37(4):330-8. Ohara H, Ichikawa S, Matsumoto H, Akiyama M, Fujimoto N, Kobayashi T, Tajima S.

Collagen hydrolysate intake increases skin collagen expression and suppresses matrix metalloproteinase 2 activity
“The effect of daily ingestion of collagen hydrolysate (CH) on skin extracellular matrix proteins was investigated…These results suggest that CH may reduce aging-related changes of the extracellular matrix by stimulating anabolic processes in skin tissue.”
J Med Food. 2011 Jun;14(6):618-24. Zague V, de Freitas V, da Costa Rosa M, de Castro GÁ, Jaeger RG, Machado-Santelli GM.

The protective effects of long-term oral administration of marine collagen hydrolysate from chum salmon on collagen matrix homeostasis in the chronological aged skin of Sprague-Dawley male rats
“To investigate the long-term effects of marine collagen hydrolysate (MCH) from Chum Salmon skin on the aberrant collagen matrix homeostasis in chronological aged skin…Based on immunohistochemistry and western blot analysis, collagen type I and III protein expression levels in MCH-treated groups significantly increased as compared with the aged control group. Furthermore, quantitative real-time polymerase chain reaction and western blot analysis showed MCH was able to increase the expressions of procollagen type I and III mRNA (COL1A2 and COL3A1)…Moreover, MCH could alleviate the oxidative stress in chronological aged skin…Therefore, MCH was demonstrated to have the protective effects on chronological skin aging due to the influence on collagen matrix homeostasis. And the antioxidative property of MCH might play an important role in the process.”
J Food Sci. 2010 Oct;75(8):H230-8. Liang J, Pei X, Zhang Z, Wang N, Wang J, Li Y.

Collagen hydrolysate intake improves the loss of epidermal barrier function and skin elasticity induced by UVB irradiation in hairless mice
“Ultraviolet B (UVB) irradiation induces serious damage to the skin. Collagen hydrolysate and collagen-derived peptides have effects on skin function in vivo and in vitro. Here, we investigated the loss of epidermal barrier function and skin elasticity induced by UVB irradiation in hairless mice fed collagen hydrolysate…Administration of collagen hydrolysate significantly decreased transepidermal water loss (TEWL) and epidermal thickness and increased stratum corneum water content. Repeated UVB irradiation decreased skin elasticity and dermal hyaluronic acid (HA) content in control mice, whereas collagen hydrolysate significantly suppressed both the increase in TEWL and the decrease in stratum corneum water content and improved skin elasticity and dermal HA content.”
Photodermatol Photoimmunol Photomed. 2013 Aug;29(4):204-11. Oba C, Ohara H, Morifuji M, Ito K, Ichikawa S, Kawahata K, Koga J.

Influence of aging on the quality of the skin of white women: the role of collagen
“Evaluate the influence of aging on the quality of the skin of white women, analyzing the dermal collagen…Histological analysis showed changes suggestive of skin aging (fragmentation and disorganization of collagen fibers), especially in patients over 60 years…There is reduction in collagen with increasing age, and an increase in its degradation, leading to fragmentation of the fibers.” Acta Cir Bras. 2012 Oct;27(10):736-40. Baroni Edo R, Biondo-Simões Mde L, Auersvald A, Auersvald LA, Montemor Netto MR, Ortolan MC, Kohler JN.

Effect of Prolyl-hydroxyproline (Pro-Hyp), a food-derived collagen peptide in human blood, on growth of fibroblasts from mouse skin
“We examined the effect of prolyl-hydroxyproline (Pro-Hyp), which occurs in human peripheral blood after ingestion of collagen peptide, on the migration and growth of mouse skin fibroblasts…These results suggest that Pro-Hyp might stimulate the growth of fibroblasts in the skin and consequently increase the number of fibroblasts migrating from the skin.”
J Agric Food Chem. 2009 Jan 28;57(2):444-9. Shigemura Y, Iwai K, Morimatsu F, Iwamoto T, Mori T, Oda C, Taira T, Park EY, Nakamura Y, Sato K.

Increasing effect of an oral intake of L-hydroxyproline on the soluble collagen content of skin and collagen fragments in rat serum
“We examined the effects of oral L-hydroxyproline (Hyp) on collagen in the body. After 2 weeks’ administration of Hyp (0.5 or 1 g/kg) to F344 male rats, the soluble collagen content of the skin had increased, and the serum concentration of collagen peptides was correlated with the skin content of soluble collagen. This result suggests that oral Hyp augmented collagen metabolism.”
Biosci Biotechnol Biochem. 2012;76(6):1242-4. Aoki M, Suto K, Komatsu M, Kamimura A, Morishita K, Yamasaki M, Takao T.
Collagen and Joints

Effects of ingestion of collagen peptide on collagen fibrils and glycosaminoglycans in the dermis
“In order to investigate the effects of collagen peptide ingestion on fibroblasts and the extracellular matrix in the dermis, collagen peptide was administered orally to pigs… Fibroblast density, and diameter and density of collagen fibrils were significantly larger in the collagen peptide group than in the lactalbumin and water control groups…These results suggest that ingestion of collagen peptide induces increased fibroblast density and enhances formation of collagen fibrils in the dermis in a protein-specific manner.”
J Nutr Sci Vitaminol (Tokyo). 2006 Jun;52(3):211-5. Matsuda N, Koyama Y, Hosaka Y, Ueda H, Watanabe T, Araya T, Irie S, Takehana K.

24-Week study on the use of collagen hydrolysate as a dietary supplement in athletes with activity-related joint pain
“To investigate the effect of collagen hydrolysate on activity-related joint pain in athletes who are physically active and have no evidence of joint disease…This was the first clinical trial of 24-weeks duration to show improvement of joint pain in athletes who were treated with the dietary supplement collagen hydrolysate. The results of this study have implications for the use of collagen hydrolysate to support joint health and possibly reduce the risk of joint deterioration in a high-risk group…the results suggest that athletes consuming collagen hydrolysate can reduce parameters (such as pain) that have a negative impact on athletic performance.”
Curr Med Res Opin. 2008 May;24(5):1485-96. Clark KL, Sebastianelli W, Flechsenhar KR, Aukermann DF, Meza F, Millard RL, Deitch JR, Sherbondy PS, Albert A.

Effect of collagen hydrolysate in articular pain: a 6-month randomized, double-blind, placebo controlled study
“Evaluation of the efficacy and safety of a food supplement made of collagen hydrolysate 1200 mg/day versus placebo during 6 months, in subjects with joint pain at the lower or upper limbs or at the lumbar spine…At 6 months, the proportion of clinical responders to the treatment, according to VAS scores, was significantly higher in the collagen hydrolysate (CH) group…No significant difference in terms of security and tolerability was observed between the two groups…This study suggests that collagen hydrolysate 1200 mg/day could increase the number of clinical responders (i.e. improvement of at least 20% on the VAS) compared to placebo.”
Complement Ther Med. 2012 Jun;20(3):124-30. Bruyère O, Zegels B, Leonori L, Rabenda V, Janssen A, Bourges C, Reginster JY.

Change in knee osteoarthritis cartilage detected by delayed gadolinium enhanced magnetic resonance imaging following treatment with collagen hydrolysate: A pilot randomized controlled trial
“Single center, prospective, randomized, placebo-controlled, double-blind, pilot trial of collagen hydrolysate for mild knee osteoarthritis (OA)…These preliminary results suggest that the dGEMRIC technique may be able to detect change in proteoglycan content in knee cartilage among individuals taking collagen hydrolysate after 24 weeks.”
Osteoarthritis Cartilage. 2011 Apr;19(4):399-405. McAlindon TE, Nuite M, Krishnan N, Ruthazer R, Price LL, Burstein D, Griffith J, Flechsenhar K.

A randomized controlled trial on the efficacy and safety of a food ingredient, collagen hydrolysate, for improving joint comfort
“Collagen, a major component of joint cartilage, is found in the diet, particularly in meat. Its hydrolysed form, collagen hydrolysate (CH), is well absorbed. CH may stimulate the joint matrix cells to synthesize collagen, so helping to maintain the structure of the joint and potentially to aid joint comfort. In a randomized, double-blind, controlled multicentre trial, 250 subjects with primary osteoarthritis of the knee were given 10 g CH daily for 6 months. There was a significant improvement in knee joint comfort as assessed by visual analogue scales to assess pain and the Womac pain subscale. Subjects with the greatest joint deterioration, and with least intake of meat protein in their habitual diets, benefited most. CH is safe and effective and warrants further consideration as a food ingredient.”
Int J Food Sci Nutr. 2009;60 Suppl 2:99-113. Benito-Ruiz P, Camacho-Zambrano MM, Carrillo-Arcentales JN, Mestanza-Peralta MA, Vallejo-Flores CA, Vargas-López SV, Villacís-Tamayo RA, Zurita-Gavilanes LA.

Effects of Pro-Hyp, a collagen hydrolysate-derived peptide, on hyaluronic acid synthesis using in vitro cultured synovium cells and oral ingestion of collagen hydrolysates in a guinea pig model of osteoarthritis
“Oral administration of collagen hydrolysates increased the amount of proteoglycans in the epiphyses. It also reduced the morphological changes associated with osteoarthritic cartilage destruction of the knee joint. The results suggest that collagen hydrolysates have therapeutic potential for treatment of osteoarthritis.”
Biosci Biotechnol Biochem. 2010;74(10):2096-9. Ohara H, Iida H, Ito K, Takeuchi Y, Nomura Y.

Control of rheumatoid arthritis by oral tolerance
“This randomized, double-blind, controlled trial examined the therapeutic effect of bovine type II collagen (CII) tablets in rheumatoid arthritis…Treatment with 0.5 mg/day of bovine CII is well tolerated and produces small, but significant, disease improvement in RA…There were no side effects associated with CII treatment.”
Arthritis Rheum. 2001 Sep;44(9):1993-7. Choy EH, Scott DL, Kingsley GH, Thomas S, Murphy AG, Staines N, Panayi GS.
Collagen and Bone

Role of collagen hydrolysate in bone and joint disease
“Pharmaceutical-grade collagen hydrolysate (PCH) is obtained by hydrolysis of pharmaceutical gelatin…Collagen hydrolysate is of interest as a therapeutic agent of potential utility in the treatment of osteoarthritis and osteoporosis. Its high level of safety makes it attractive as an agent for long-term use in these chronic disorders.”
Semin Arthritis Rheum. 2000 Oct;30(2):87-99. Moskowitz RW.

Absorption and effectiveness of orally administered low molecular weight collagen hydrolysate in rats
“We investigated the absorption mechanism of low molecular weight collagen hydrolysate (LMW-CH) and its effects on osteoporosis in rats…Our findings show that LMW-CH exerts a beneficial effect on osteoporosis by increasing the organic substance content of bone.”
J Agric Food Chem. 2010 Jan 27;58(2):835-41. doi: 10.1021/jf9031487. Watanabe-Kamiyama M, Shimizu M, Kamiyama S, Taguchi Y, Sone H, Morimatsu F, Shirakawa H, Furukawa Y, Komai M.

Hydrolyzed collagen intake increases bone mass of growing rats trained with running exercise
“We examined the effects of 11 weeks of HC intake and running exercise on bone mass and strength in growing rats…The present study demonstrated that moderate HC intake (where the diet contains 20% protein, of which 30% is HC) increased bone mass during growth period and further promoted the effect of running exercise.”
J Int Soc Sports Nutr. 2013 Aug 6;10(1):35. Takeda S, Park JH, Kawashima E, Ezawa I, Omi N.
Collagen and Body Composition

Effects of whey and fortified collagen hydrolysate protein supplements on nitrogen balance and body composition in older women
“We compared the nitrogen balance of two protein supplements varying in type but not amount of protein content using a crossover study design…Therefore, a concentrated, fortified, hydrolyzed collagen protein supplement maintained nitrogen balance and preserved lean body mass during 15 days of consumption of a relatively low-protein diet.”
J Am Diet Assoc. 2009 Jun;109(6):1082-7. doi: 10.1016/j.jada.2009.03.003. Hays NP, Kim H, Wells AM, Kajkenova O, Evans WJ.

 

Leave a Reply

Fill in your details below or click an icon to log in:

WordPress.com Logo

You are commenting using your WordPress.com account. Log Out / Change )

Twitter picture

You are commenting using your Twitter account. Log Out / Change )

Facebook photo

You are commenting using your Facebook account. Log Out / Change )

Google+ photo

You are commenting using your Google+ account. Log Out / Change )

Connecting to %s

%d bloggers like this: