Organic raw Rose hip is well known for their high vitamin C content, but are also a rich source of polyphenols, bioflavonoids and carotenoids. Rose hips naturally help fight inflammation, boost the immune system and are beneficial for maintaining overall health. Recent studies suggest that rose hips may be helpful in supporting the body in combating osteoarthritis, rheumatoid arthritis and Crohn's Disease. What makes rose hips so special is their naturally high vitamin C content is significantly enhanced by supporting bioflavonoids such as quercetin, rutin and hesperidin which increase absorption and amplify the overall benefit. Carotenoids found in rose hips include beta-carotene, lycopene, beta-chryptoxanthin, rubixanthin, zeaxanthin and lutein.
Raw Organic Rosehip preparations have been used for thousands of years in many different forms. As their name implies, they come from the rose plant. They are the bulbs that remain after the petals fall off. Rose hips have been used over the years for infections of all types; they have also been possibly used to for diarrhea, skin problems, colds & flu, sore throats, fatigue, kidney problems, inflammation, stress and nervousness. They have been proven to be a superb source of vitamin C, having a much higher content than citrus fruit. They also contain vitamins E and K, the B vitamins riboflavin and folate. Rose hips can help to possibly reduce skin wrinkling and strengthen the blood vessels reducing the body's ability to bruise. Taking rose hips gives your body the nutrients it needs to help stay young and healthy!
Some possible traditional uses of Raw Organic Rose Hip Powder may include:
● Possibly Boosting the overall immune system
● May Support the cardiovascular system
● Facilitating fat metabolism
● May protect tissues from free radical damage
● Excellent source of the fatty acid GOPO
● Assists the nervous system by converting certain amino acids into neurotransmitters
● Protects the joints & connective tissues
● May fight the cold & flu
● Protecting adrenal function
● Supporting kidney & urinary tract health
Constituents of Rose Hips include:
● Minerals: Calcium, Iron, Magnesium, Phosphorus, Potassium, Zinc, Copper, Manganese
● Vitamins: Vitamin C, Thiamin, Riboflavin, Niacin, Pantothenic Acid, Vitamin B-6, Folate, Choline, Betaine, Vitamin A (RAE), Beta & Alpha carotene, Cryptoxanthin beta Vitamin A (IU), Lutein & Zeaxanthin, Lycopene, Vitamin E, Beta Tocopherol, Gamma Tocopherol, Delta Tocopherol, Vitamin K
● Phytochemicals: Catechins, Flavonoids, Isoquercitrin, Leucoanthocyanins, Malic Acid, Pectins, Polyphenols, Quercetin, Tiliroside
This product is 100% natural and minimally processed. Taste, smell, texture, and color may vary from batch to batch. Due to its nature, this powder tends to clump. If clumping occurs, lay the bag on a flat surface and place a towel over the bag. Then pound on the bag until the clumps break up. The towel will help protect the bag from damage.
Mix 1 tablespoon with juice, yogurt, add to your favorite smoothie, or infuse in a tea.
To increase flavor and nutritional profile combine with our organic acerola powder.
Dog Rose, Hip Tree, Wild Brier, Dog Brier, Rose Haw, and Rose Hep
Organic Rose Hip.
Grown and dried in South Africa. Packaged with care in Florida, USA.
USDA Certified Organic
Z Natural Foods strives to offer the highest quality organically grown, raw, vegan, gluten free, non-GMO products available and exclusively uses low temperature drying techniques to preserve all the vital enzymes and nutrients. Our Raw Rose Hip Powder is certified organic and passes our strict quality assurance which includes testing for botanical identity, heavy metals, chemicals and microbiological contaminants. ZNaturalFoods.com offers Raw Organic Rose Hip Powder packaged in airtight stand-up, resealable foil pouches for optimum freshness. Once opened, just push the air out of the pouch before resealing it in order to preserve maximum potency. Keep your Organic Raw Rose Hip Powder in a cool, dark, dry place.
1. M. B. Goldring and S. R. Goldring, “Osteoarthritis,” Journal of Cellular Physiology, vol. 313, pp. 626–634, 2007.
2. Y. Henrotin, C. Sanchez, and M. Balligand, “Pharmaceutical and nutraceutical management of canine osteoarthritis: present and future perspectives,” Veterinary Journal, vol. 170, no. 1, pp. 113–123, 2005.
3. J. A. Buckwalter, J. Martin, and H. J. Mankin, “Synovial joint degeneration and the syndrome of osteoarthritis,” Instructional Course Lectures, vol. 49, pp. 481–489, 2000.
4. M. B. Goldring, “The role of the chondrocyte in osteoarthritis,” Arthritis and Rheumatism, vol. 43, no. 9, pp. 1916–1926, 2000.
5. M. Shakibaei, “Inhibition of chondrogenesis by integrin antibody in vitro,” Experimental Cell Research, vol. 240, no. 1, pp. 95–106, 1998.
6. L. Cao, V. Lee, M. E. Adams et al., “β1-Integrin-collagen interaction reduces chondrocyte apoptosis,” Matrix Biology, vol. 18, no. 4, pp. 343–355, 1999.
7. M. Shakibaei, T. John, P. De Souza, R. Rahmanzadeh, and H. J. Merker, “Signal transduction by β1 integrin receptors in human chondrocytes in vitro: collaboration with the insulin-like growth factor-I receptor,” Biochemical Journal, vol. 342, no. 3, pp. 615–623, 1999.
8. M. Shakibaei, G. Schulze-Tanzil, P. De Souza et al., “Inhibition of mitogen-activated protein kinase kinase induces apoptosis of human chondrocytes,” The Journal of Biological Chemistry, vol. 276, no. 16, pp. 13289–13294, 2001.
9. P. G. Todhunter, S. A. Kincaid, R. J. Todhunter et al., “Immunohistochemical analysis of an equine model of synovitis-induced arthritis,” American Journal of Veterinary Research, vol. 57, no. 7, pp. 1080–1093, 1996.
10. T. Aigner, K. Fundel, J. Saas et al., “Large-scale gene expression profiling reveals major pathogenetic pathways of cartilage degeneration in osteoarthritis,” Arthritis and Rheumatism, vol. 54, no. 11, pp. 3533–3544, 2006.
11. K. J. Smith, A. L. Bertone, S. E. Weisbrode, and M. Radmacher, “Gross, histologic, and gene expression characteristics of osteoarthritic articular cartilage of the metacarpal condyle of horses,” American Journal of Veterinary Research, vol. 67, no. 8, pp. 1299–1306, 2006.
12. K. von der Mark, T. Kirsch, A. Nerlich et al., “Type X collagen synthesis in human osteoarthritic cartilage: indication of chondrocyte hypertrophy,” Arthritis and Rheumatism, vol. 35, no. 7, pp. 806–811, 1992.
13. F. J. Blanco, R. Guitian, E. Vázquez-Martul, F. J. De Toro, and F. Galdo, “Osteoarthritis chondrocytes die by apoptosis: a possible pathway for osteoarthritis pathology,” Arthritis and Rheumatism, vol. 41, no. 2, pp. 284–289, 1998.
14. M. B. Goldring, “The role of cytokines as inflammatory mediators in osteoarthritis: lessons from animal models,” Connective Tissue Research, vol. 40, no. 1, pp. 1–11, 1999.
15. J. R. Robbins, B. Thomas, L. Tan, et al., “Immortalized human adult articular chondrocytes maintain cartilage-specific phenotype and responses to interleukin-1β,” Arthritis and Rheumatism, vol. 43, no. 10, pp. 2189–2201, 2000.
16. A. Kumar, Y. Takada, A. M. Boriek, and B. B. Aggarwal, “Nuclear factor-κB: its role in health and disease,” Journal of Molecular Medicine, vol. 82, no. 7, pp. 434–448, 2004.
17. K. Riehemann, B. Behnke, and K. Schulze-Osthoff, “Plant extracts from stinging nettle (Urtica dioica), an antirheumatic remedy, inhibit the proinflammatory transcription factor NF-κB,” FEBS Letters, vol. 442, no. 1, pp. 89–94, 1999.
18. S. Murakami, V. Lefebvre, and B. De Crombrugghe, “Potent inhibition of the master chondrogenic factor Sox9 gene by interleukin-1 and tumor necrosis factor-α,” The Journal of Biological Chemistry, vol. 275, no. 5, pp. 3687–3692, 2000.
19. D. M. Gerlag, L. Ransone, P. P. Tak et al., “The effect of a T cell-specific NF-κB inhibitor on in vitro cytokine production and collagen-induced arthritis,” Journal of Immunology, vol. 165, no. 3, pp. 1652–1658, 2000.
20. N. G. Murphy and R. B. Zurier, “Treatment of rheumatoid arthritis,” Current Opinion in Rheumatology, vol. 3, no. 3, pp. 441–448, 1991.
21. K. P. Khalsa, “Frequently asked questions (FAQ),” Journal of Herbal Pharmacotherapy, vol. 6, no. 1, pp. 77–87, 2006.
22. S. N. Willich, K. Rossnagel, S. Roll et al., “Rose hip herbal remedy in patients with rheumatoid arthritis—a randomised controlled trial,” Phytomedicine, vol. 17, no. 2, pp. 87–93, 2010.
23. X. Tao, H. Schulze-Koops, L. Ma, J. Cai, Y. Mao, and P. E. Lipsky, “Effects of Tripterygium wilfordii Hook F extracts on induction of cyclooxygenase 2 activity and prostaglandin E2 production,” Arthritis and Rheumatism, vol. 41, no. 1, pp. 130–138, 1998.
24. N. Lin, T. Sato, and A. Ito, “Triptolide, a novel diterpenoid triepoxide from Tripterygium wilfordii Hook. f., suppresses the production and gene expression of pro-matrix metalloproteinases 1 and 3 and augments those of tissue inhibitors of metalloproteinases 1 and 2 in human synovial fibroblasts,” Arthritis and Rheumatism, vol. 44, no. 9, pp. 2193–2200, 2001.
25. L. W. Whitehouse, M. Znamirowska, and C. J. Paul, “Devil's Claw (Harpagophytum procumbens): no evidence for anti-inflammatory activity in the treatment of arthritic disease,” Canadian Medical Association Journal, vol. 129, no. 3, pp. 249–251, 1983.
26. C. L. Shen, K. J. Hong, and S. W. Kim, “Effects of ginger (Zingiber officinale Rosc.) on decreasing the production of inflammatory mediators in sow osteoarthrotic cartilage explants,” Journal of Medicinal Food, vol. 6, no. 4, pp. 323–328, 2003.
27. L. C. Mishra, B. B. Singh, and S. Dagenais, “Scientific basis for the therapeutic use of Withania somnifera (ashwagandha): a review,” Alternative Medicine Review, vol. 5, no. 4, pp. 334–346, 2000. View at Scopus
28. E. Ernst, “Complementary and alternative medicine in rheumatology,” Best Practice and Research, vol. 14, no. 4, pp. 731–749, 2000.
29. L. Long, K. Soeken, and E. Ernst, “Herbal medicines for the treatment of osteoarthritis: a systematic review,” Rheumatology, vol. 40, no. 7, pp. 779–793, 2001.
30. J. E. Chrubasik, B. D. Roufogalis, H. Wagner, and S. A. Chrubasik, “A comprehensive review on nettle effect and efficacy profiles, Part I: herba urticae,” Phytomedicine, vol. 14, no. 6, pp. 423–435, 2007.
31. G. Schulze-Tanzil, P. De Souza, B. Behnke, S. Klingelhoefer, A. Scheid, and M. Shakibaei, “Effects of the antirheumatic remedy Hox alpha—a new stinging nettle leaf extract—on matrix metalloproteinases in human chondrocytes in vitro,” Histology and Histopathology, vol. 17, no. 2, pp. 477–485, 2002.
32. M. Shakibaei and P. De Souza, “Differentiation of mesenchymal limb bud cells to chondrocytes in alginate beads,” Cell Biology International, vol. 21, no. 2, pp. 75–86, 1997.
33. M. Shakibaei, T. John, G. Schulze-Tanzil, I. Lehmann, and A. Mobasheri, “Suppression of NF-κB activation by curcumin leads to inhibition of expression of cyclo-oxygenase-2 and matrix metalloproteinase-9 in human articular chondrocytes: implications for the treatment of osteoarthritis,” Biochemical Pharmacology, vol. 73, no. 9, pp. 1434–1445, 2007.
34. S. Miyamoto, M. Maki, M. J. Schmitt, M. Hatanaka, and I. M. Verma, “Tumor necrosis factor α-induced phosphorylation of IκBα is a signal for its degradation but not dissociation from NF-κB,” Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 26, pp. 12740–12744, 1994.
35. A. Vinitsky, C. Michaud, J. C. Powers, and M. Orlowski, “Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex,” Biochemistry, vol. 31, no. 39, pp. 9421–9428, 1992.
36. R. O. Sanderson, C. Beata, R. M. Flipo et al., “Systematic review of the management of canine osteoarthritis,” Veterinary Record, vol. 164, no. 14, pp. 418–424, 2009. View at Scopus
37. T. P. N. Talorete, M. Bouaziz, S. Sayadi, and H. Isoda, “Influence of medium type and serum on MTT reduction by flavonoids in the absence of cells,” Cytotechnology, vol. 52, no. 3, pp. 189–198, 2006.
38. M. Shakibaei, P. De Souza, and H. J. Merker, “Integrin expression and collagen type II implicated in maintenance of chondrocyte shape in monolayer culture: an immunomorphological study,” Cell Biology International, vol. 21, no. 2, pp. 115–125, 1997.
39. A. Mobasheri, S. D. Carter, P. Martín-Vasallo, and M. Shakibaei, “Integrins and stretch activated ion channels; putative components of functional cell surface mechanoreceptors in articular chondrocytes,” Cell Biology International, vol. 26, no. 1, pp. 1–18, 2002.
40. S. M. Albelda and C. A. Buck, “Integrins and other cell adhesion molecules,” The FASEB Journal, vol. 4, no. 11, pp. 2868–2880, 1990. View at Scopus
41. J. P. Schmitz, D. D. Dean, Z. Schwartz et al., “Chondrocyte cultures express matrix metalloproteinase mRNA and immunoreactive protein; stromelysin-1 and 72 kDa gelatinase are localized in extracellular matrix vesicles,” Journal of Cellular Biochemistry, vol. 61, no. 3, pp. 375–391, 1996.
42. D. H. Manicourt, N. Fujimoto, K. Obata, and E. J. M. A. Thonar, “Levels of circulating collagenase, stromelysin-1, and tissue inhibitor of matrix metalloproteinases 1 in patients with rheumatoid arthritis: relationship to serum levels of antigenic keratan sulfate and systemic parameters of inflammation,” Arthritis and Rheumatism, vol. 38, no. 8, pp. 1031–1039, 1995.
43. G. Keyszer, I. Lambiri, R. Nagel et al., “Circulating levels of matrix metalloproteinases MMP-3 and MMP-1, tissue inhibitor of metalloproteinases 1 (TIMP-1), and MMP-1/TIMP-1 complex in rheumatic disease. Correlation with clinical activity of rheumatoid arthritis versus other surrogate markers,” The Journal of Rheumatology, vol. 26, no. 2, pp. 251–258, 1999. View at Scopus
44. I. C. Chikanza and L. Fernandes, “Novel strategies for the treatment of osteoarthritis,” Expert Opinion on Investigational Drugs, vol. 9, no. 7, pp. 1499–1510, 2000. View at Scopus
45. E. Nédélec, A. Abid, C. Cipolletta et al., “Stimulation of cyclooxygenase-2-activity by nitric oxide-derived species in rat chondrocyte: lack of contribution to loss of cartilage anabolism,” Biochemical Pharmacology, vol. 61, no. 8, pp. 965–978, 2001.
46. C. Csaki, N. Keshishzadeh, K. Fischer, and M. Shakibaei, “Regulation of inflammation signalling by resveratrol in human chondrocytes in vitro,” Biochemical Pharmacology, vol. 75, no. 3, pp. 677–687, 2008.
47. C. Csaki, A. Mobasheri, and M. Shakibaei, “Synergistic chondroprotective effects of curcumin and resveratrol in human articular chondrocytes: inhibition of IL-1beta-induced NF-kappaB-mediated inflammation and apoptosis,” Arthritis Research & Therapy, vol. 11, no. 6, article R165, 2009.
48. K. Yamamoto, T. Arakawa, N. Ueda, and S. Yamamoto, “Transcriptional roles of nuclear factor κB and nuclear factor-interleukin-6 in the tumor necrosis factor α-dependent induction of cyclooxygenase-2 in MC3T3-E1 cells,” The Journal of Biological Chemistry, vol. 270, no. 52, pp. 31315–31320, 1995.
49. M. Hebbar, J.-P. Peyrat, L. Hornez, P.-Y. Hatron, E. Hachulla, and B. Devulder, “Interleukin-1 induction of collagenase 3 (matrix metalloproteinase 13) gene expression in chondrocytes requires p38, c-Jun N-terminal kinase, and nuclear factor κB: differential regulation of collagenase 1 and collagenase 3,” Arthritis and Rheumatism, vol. 43, no. 4, pp. 801–811, 2000.
50. K. W. McIntyre, D. J. Shuster, K. M. Gillooly et al., “A highly selective inhibitor of IκB kinase, BMS-345541, blocks both joint inflammation and destruction in collagen-induced arthritis in mice,” Arthritis and Rheumatism, vol. 48, no. 9, pp. 2652–2659, 2003.
51. I. Kou and S. Ikegawa, “SOX9-dependent and -independent transcriptional regulation of human cartilage link protein,” The Journal of Biological Chemistry, vol. 279, no. 49, pp. 50942–50948, 2004.
61. C. A. Séguin and S. M. Bernier, “TNFalpha suppresses link protein and type II collagen expression in chondrocytes: role of MEK1/2 and NF-kappaB signaling pathways,” Journal of Cellular Physiology, vol. 197, no. 3, pp. 356–369, 2003. View at Scopus