Introduction

Silvipriya et al. (2015) have shared that collagen is the most abundant protein among the Anamalia, commonly referred to as the Animal Kingdom. As stated, being such a proliferous source, it may be extracted from a variety of means through varying methods, and of course – as you’ll soon find out – for numerous beneficial purposes. The work of Ranshaw et al. (2009) pertains largely to collagen as a bio-based technology, though also offering the words Greek derivatives; with kola and gen as gum and producing respectively. Within the extracellular connective tissue of the Anamalia (such as marine sources) the protein collagen is notably found and harnessed as its peptides (Ranshaw et al., 2009). Marine Collagen Peptides (MCPs) have been historically disregarded as a waste product within the fishing industry, causing a loss of valuable goods and health impact for potential human consumers, as well as the human ecology and economy more broadly. Alemán & Martínez-Alvarez (2013) explain that these biologically active peptides are enzymatically hydrolysed to unleash their remarkable potential. Marine biodiversity encompasses approximately 50% of the total biodiversity seen worldwide (Cheung et al., 2015), as such its preservation and understanding is vital.

Benefits and Effects

  • Collagen is becoming commonplace as a benefit to human skin. Proksch et al. (2014) found that oral administration of collagen hydrolysate (CH) exhibited significant improvements in skin elasticity after both 4 and 8 weeks of administration. Though, Proksch et al. (2014) found no substantial benefits for skin roughness, a slight assistance was noted for skin hydration. A meta-analysis by Choi et al. (2019) noted that over CH, collagen tripeptide and collagen dipeptide may show further anti-aging properties with there effect on dermal collagen density, skin elasticity, and hydration.
  • Studies utilizing the brown rat (rattus norvegicus) exhibit remarkable results toward anti-aging and extending life-span. Ben-Haim et al. (2018) note that MCPs fed to brown rats extended average and maximal life-span up to 10% and 11% respectively. Liang et al. (2010) noted that MCPs present a dose-dependant increase in life-span, wherein a reduction in both antioxidant enzymes and tumour occurrence as well as increase in lipid peroxidation were noted in sprague-dawley rats. Spindler (2012) validates the work of Liang et al. (2010) by noting that calorie restriction as such a factor for longevity may be excluded as a cause.
  • MCPs have been found to benefit diabetics and those with obesity profiles by triglyceride and glucose regulation via their direct influence on cholesterol, low-density lipoprotein (LDL), free-fatty acids, and fasting blood insulin as well as glycosylated hemoglobin (hemoglobin A1c) in human subjects (Zhu et al., 2010).
  • Reactive oxygen species (ROS) are key markers of oxidative stress; causing damage to lipids, proteins and DNA (Schieber & Chandel, 2014). ROS is a major cause of inflammation (Di et al., 2012). ROS production is linked to cell death and counteracts wound healing (Alemán & Martínez-Alvarez, 2013), whereas the antioxidant activity of MCPs ameliorates this such process (Yang et al., 2019). As such, MCPs aid in wound healing including their viability for caesarean delivery (C-section) recovery including wounds and scars more generally (Wang et al., 2015).
  • Antihypertensive peptides are becoming recognized as a defense against high blood pressure; in which the pressure within human arteries becomes excessive (Alemán & Martínez-Alvarez, 2013). Angiotensin-I Converting Enzyme (ACE) (more commonly known as ACE inhibitors), are a common drug therapy/first-line pharmaceutical treatment for high blood pressure and hypertension, yet Cheung et al. (2015) note that MCPs may have further validation within the pharmaceutical industry itself as more research is conducted on their benefits. Though the “metabolic, inflammatory, and genetic causes and atherothrombotic disease” (p. 1) mechanisms of type 2 diabetes mellitus (T2DM) have yet to be fully understood, the study by Zhu et al. (2017) found that MCPs exhibit beneficial effects on endothelial cells in rat models with T2DM. As such, and more commonly known, MCPs and eating fish in general has cardioprotective properties profusely.
  • Research has been done regarding the success of the casein protein glycomacropeptide (GMP) commonly derived from milk, wherein GMP aids in the creation of the hormone cholecystokinin known to potentially reduce obesity through increased satiety after such high protein intake (Khora, 2013). The research on MCPs mirrored functioning is ongoing.
  • The astounding work of Xu et la. (2015) found that following perinatal asphyxia (PA) MCPs are able to attenuate continuing learning and memory processes in animal models, demonstrating neuroprotective effects. This process is seen through a reduction in ROS and acetylcholinesterase (AChE) and an increase in hippocampus response element binding protein (p-CREB) and brain derived neurotrophic factor (BDNF) (Xu et la., 2015).
  • Alemán et al. (2011) have found that bioactive hydrolysates Alcalase and Esperase extracted from giant squid (dosidicus gigas) verified cytotoxic properties toward human cancer cells in vitro.

Administration

MCPs benefits are found in a dose- and temporal- dependent fashion, through oral administration.

No chronic toxic effect on rats was observed at administrations as high as “8.586 g/kg·bw/day for females and 6.658 g/kg·bw/day for males” at MCPs concentrated at 18% of total diet (Liang et al., 2012).

References

Attwood, C. (2017). Raw fish meat on brown chopping board photo [photo]. Retrieved from https://unsplash.com/photos/kC9KUtSiflw

Alemán, A., & Martínez-Alvarez, O. (2013). Marine collagen as a source of bioactive molecules: A review. The Natural Products Journal, 3(2), 105-114.

Alemán, A., Pérez-Santín, E., Bordenave-Juchereau, S., Arnaudin, I., Gómez-Guillén, M. C., & Montero, P. (2011). Squid gelatin hydrolysates with antihypertensive, anticancer and antioxidant activity. Food Research International, 44(4), 1044-1051.

Ben-Haim, M. S., Kanfi, Y., Mitchell, S. J., Maoz, N., Vaughan, K. L., Amariglio, N., … & Cohen, H. Y. (2018). Breaking the ceiling of human maximal life span. The Journals of Gerontology: Series A, 73(11), 1465-1471.

Cheung, R. C. F., Ng, T. B., & Wong, J. H. (2015). Marine peptides: Bioactivities and applications. Marine drugs, 13(7), 4006-4043.

Chen, X. L., Peng, M., Li, J., Tang, B. L., Shao, X., Zhao, F., … & Zhang, Y. Z. (2017). Preparation and functional evaluation of collagen oligopeptide-rich hydrolysate from fish skin with the serine collagenolytic protease from Pseudoalteromonas sp. SM9913. Scientific reports, 7(1), 1-13.

Choi, F. D., Sung, C. T., Juhasz, M. L., & Mesinkovsk, N. A. (2019). Oral collagen supplementation: A systematic review of dermatological applications. Journal of drugs in dermatology: JDD, 18(1), 9-16.

Di, A., Gao, X. P., Qian, F., Kawamura, T., Han, J., Hecquet, C., … & Malik, A. B. (2012). The redox-sensitive cation channel TRPM2 modulates phagocyte ROS production and inflammation. Nature immunology, 13(1), 29.

Khora, S. S. (2013). Marine fish-derived bioactive peptides and proteins for human therapeutics. International Journal of Pharmacy and Pharmaceutical Sciences, 5(3), 31-37.

Liang, J., Pei, X. R., Zhang, Z. F., Wang, N., Wang, J. B., & Li, Y. (2012). A chronic oral toxicity study of marine collagen peptides preparation from chum salmon (Oncorhynchus keta) skin using Sprague-Dawley rat. Marine Drugs, 10(1), 20-34.

Liang, J., Pei, X. R., Wang, N., Zhang, Z. F., Wang, J. B., & Li, Y. (2010). Marine collagen peptides prepared from chum salmon (Oncorhynchus keta) skin extend the life span and inhibit spontaneous tumor incidence in sprague-dawley rats. Journal of medicinal food, 13(4), 757-770.

Proksch, E., Segger, D., Degwert, J., Schunck, M., Zague, V., & Oesser, S. (2014). Oral supplementation of specific collagen peptides has beneficial effects on human skin physiology: a double-blind, placebo-controlled study. Skin pharmacology and physiology, 27(1), 47-55.

Ramshaw, J. A., Peng, Y. Y., Glattauer, V., & Werkmeister, J. A. (2009). Collagens as biomaterials. Journal of Materials Science: Materials in Medicine, 20(1), 3.

Schieber, M., & Chandel, N. S. (2014). ROS function in redox signaling and oxidative stress. Current biology, 24(10), R453-R462.

Silvipriya, K. S., Kumar, K. K., Bhat, A. R., Kumar, B. D., John, A., & Lakshmanan, P. (2015). Collagen: Animal sources and biomedical application. Journal of Applied Pharmaceutical Science, 5(3), 123-127.

Spindler, S. R. (2012). Review of the literature and suggestions for the design of rodent survival studies for the identification of compounds that increase health and life span. Age, 34(1), 111-120.

Wang, J., Xu, M., Liang, R., Zhao, M., Zhang, Z., & Li, Y. (2015). Oral administration of marine collagen peptides prepared from chum salmon (Oncorhynchus keta) improves wound healing following cesarean section in rats. Food & Nutrition Research, 59(1), 26411.

Xu, L., Dong, W., Zhao, J., & Xu, Y. (2015). Effect of marine collagen peptides on physiological and neurobehavioral development of male rats with perinatal asphyxia. Marine drugs, 13(6), 3653-3671.

Yang, F., Jin, S., & Tang, Y. (2019). Marine Collagen Peptides Promote Cell Proliferation of NIH-3T3 Fibroblasts via NF-κB Signaling Pathway. Molecules, 24(22), 4201.

Zhu, C. F., Li, G. Z., Peng, H. B., Zhang, F., Chen, Y., & Li, Y. (2010). Treatment with marine collagen peptides modulates glucose and lipid metabolism in Chinese patients with type 2 diabetes mellitus. Applied Physiology, Nutrition, and Metabolism, 35(6), 797-804.

Zhu, C., Zhang, W., Liu, J., Mu, B., Zhang, F., Lai, N., … & Li, Y. (2017). Marine collagen peptides reduce endothelial cell injury in diabetic rats by inhibiting apoptosis and the expression of coupling factor 6 and microparticles. Molecular Medicine Reports, 16(4), 3947-3957.

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