Why doesn’t Dr. Maggie Joint Formula Contain Hyaluronic Acid?

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What is Hyaluronic acid?

Hyaluronic acid, or HA as it is commonly abbreviated, is a clear sugary gooey molecule that occurs naturally in the skin’s structure, eyes, fluid, joints, and connective tissue throughout the body. It helps lubricate your joints and keep things full of moisture. Many patients, both human as well as our furry friends, have reported relief of joint discomfort while taking HA.

Molecular structure of hyaluronic acid

 

So Why Not Use Hyaluronic Acid in Dr. Maggie Joint Formula?

Although your body naturally creates Hyaluronic acid, recent research has proven that HA plays a role cancer metastasis. It is important to note that Hyaluronic Acid does not cause cancer, but rather aids in the metastasis of existing cancer cells in the body. It is possible that some undetected cancer cells could therefore multiply and metastasize while taking HA products, causing the patient to discover a cancer that may otherwise have gone unnoticed for some time. Because of this we don’t want any extra HA to be anywhere near cancer cells.

Hyaluronic Acid appears to make it easier for cancer to spread.

For a cancer tumor to expand its size and spread into adjacent territory, the cells have to move out into the extra cellular matrix. They do this by forming an arm of cytoplasm that reaches out, grabs onto a handhold in adjacent goop and than pulls the cell along after it. How does it latch onto this goop? Imagine it’s got a chunk of Velcro at the tip of the arm. In this analogy the Velcro is designed to latch onto a specific chemical which turns out to be hyaluronic acid. The ‘Velcro’ has been identified and named; it is a specific protein made by many cancer cells named CD44.

When a cancer cell with this CD44 protein grows and attempts to spread, HA helps it do so. If you add extra HA to a culture of CD44 positive breast cancer cells they grow and spread faster. In mice with breast cancer, if you add hyaluronidase, the enzyme that digests and breaks up HA, you slow the growth and progression of the cancer. This enzyme works so well at hindering cancer spread that research is being conducted using it as a treatment for cancer.

 

 

Dr. Maggie Opts For Safety

Although HA has been proven to be effective in relieving joint pain, we feel that given this background, not only should Hyaluronic acid should not be taken by anyone with cancer (in particular breast cancer, ovarian cancer or lung cancer), by extension, we prefer to err on the side of caution and use ingredients that have less potential to cause serious health issues. We would hate to find out that a pet with a yet undetected cancer took a HA containing supplement and had the cancer metastasize and spread at a rate it may not have.

See below for supporting research

Hyaluronic acid (HA) promotes tumor metastasis.

Hyaluronic Acid Synthase-1 Expression Regulates Bladder Cancer Growth, Invasion, and Angiogenesis through CD44

Roozbeh Golshani, Luis Lopez, Veronica Estrella, Mario Kramer, Naoko Iida, Vinata B. Lokeshwar
DOI: 10.1158/0008-5472.CAN-07-2140 Published 15 January 2008

Abstract

Hyaluronic acid (HA) promotes tumor metastasis and is an accurate diagnostic marker for bladder cancer. HA is synthesized by HA synthases HAS1, HAS2, or HAS3. We have previously shown that HAS1 expression in tumor tissues is a predictor of bladder cancer recurrence and treatment failure. In this study, we stably transfected HT1376 bladder cancer cells with HAS1-sense (HAS1-S), HAS1-antisense (HAS1-AS), or vector cDNA constructs. Whereas HAS1-S transfectants produced ∼1.7-fold more HA than vector transfectants, HA production was reduced by ∼70% in HAS1-AS transfectants. HAS1-AS transfectants grew 5-fold slower and were ∼60% less invasive than vector and HAS1-S transfectants. HAS1-AS transfectants were blocked in G2-M phase of the cell cycle due to down-regulation of cyclin B1, cdc25c, and cyclin-dependent kinase 1 levels. These transfectants were also 5- to 10-fold more apoptotic due to the activation of the Fas-Fas ligand–mediated extrinsic pathway. HAS1-AS transfectants showed a ∼4-fold decrease in ErbB2 phosphorylation and down-regulation of CD44 variant isoforms (CD44-v3, CD44-v6, and CD44-E) both at the protein and mRNA levels. However, no decrease in RHAMM levels was observed. The decrease in CD44-v mRNA levels was not due to increased mRNA degradation. Whereas CD44 small interfering RNA (siRNA) transfection decreased cell growth and induced apoptosis in HT1376 cells, HA addition modestly increased CD44 expression and cell growth in HAS1-AS transfectants, which could be blocked by CD44 siRNA. In xenograft studies, HAS1-AS tumors grew 3- to 5-fold slower and had ∼4-fold lower microvessel density. These results show that HAS1 regulates bladder cancer growth and progression by modulating HA synthesis and HA receptor levels. [Cancer Res 2008;68(2):483–91]

Footnotes

  • Received June 8, 2007.
  • Revision received August 18, 2007.
  • Accepted September 13, 2007.
  • ©2008 American Association for Cancer Research.

Hyaluronidase in Prostate Cancer

  1. Vinata B. Lokeshwar‡¶, 
  2. Diego Rubinowicz‡, 
  3. Grethchen L. Schroeder‡,
  4. Eva Forgacs‖, 
  5. John D. Minna‖, 
  6. Norman L. Block‡, 
  7. Mehrdad Nadji**and
  8. Bal L. Lokeshwar‡ +Author Affiliations

From the Department of Urology, Cell Biology and Anatomy, and **Pathology, University of Miami School of Medicine, Miami, Florida 33101 and the Hamon Center for Therapeutic Oncology Research, University of Texas Southwestern Medical Center, Dallas, Texas 75390-8593

Abstract

Hyaluronic acid (HA), a glycosaminoglycan, regulates cell adhesion and migration. Hyaluronidase (HAase), an endoglycosidase, degrades HA into small angiogenic fragments. Using an enzyme-linked immunosorbent assay-like assay, we found increased HA levels (3–8-fold) in prostate cancer (CaP) tissues when compared with normal (NAP) and benign (BPH) tissues. The majority (∼75–80%) of HA in prostate tissues was found to exist in the free form. Primary CaP fibroblast and epithelial cells secreted 3–8-fold more HA than respective NAP and BPH cultures. Only CaP epithelial cells and established CaP lines secreted HAase and the secretion increased with tumor grade and metastasis. The pH activity profile and optimum (4.2; range 4.0–4.3) of CaP HAase was identical to the HYAL1-type HAase present in human serum and urine. Full-length HYAL1 transcript and splice variants were detected in CaP cells by reverse transcriptase-polymerase chain reaction, cloning, and sequencing. Immunoblotting confirmed secretion of a ∼60-kDa HYAL1-related protein by CaP cells. Immunohistochemistry showed minimal HA and HYAL1 staining in NAP and BPH tissues. However, a stromal and epithelial pattern of HA and HYAL1 expression was observed in CaP tissues. While high HA staining was observed in tumor-associated stroma, HYAL1 staining in tumor cells increased with tumor grade and metastasis. The gel-filtration column profiles of HA species in NAP, BPH, and CaP tissues were different. While the higher molecular mass and intermediate size HA was found in all tissues, the HA fragments were found only in CaP tissues. In particular, the high-grade CaP tissues, which showed both elevated HA and HYAL1 levels, contained angiogenic HA fragments. The stromal-epithelial HA and HYAL1 expression may promote angiogenesis in CaP and may serve as prognostic markers for CaP.

 

Tumor-associated Hyaluronic Acid

Tumor-associated Hyaluronic Acid: A New Sensitive and Specific Urine Marker for Bladder Cancer

Vinata B. Lokeshwar, Can Öbek, Mark S. Soloway, Norman L. Block Published 15 February 1997

Abstract

Hyaluronic acid (HA), a glycosaminoglycan, is known to promote tumor cell adhesion and migration, and its small fragments stimulate angiogenesis. We compared levels of HA in the urine of normal individuals and patients with bladder cancer or other genitourinary conditions, using a sensitive ELISA-like assay. Among the 144 specimens analyzed, the urinary HA levels of bladder cancer patients with G1 (255 ± 41.7 ng/mg), G2 (291.8 ± 68.3 ng/mg) and G3 (428.4 ± 67 ng/mg) tumors are 4–9-fold elevated as compared to those of normal individuals (44.7 ± 6.2 ng/mg) and patients with other genitourinary conditions (69.5 ± 6.8 ng/mg; P < 0.001). Urinary HA measurement by the ELISA-like assay shows a sensitivity of 91.9% and specificity of 92.8% to detect bladder cancer. Thus, urinary HA measurement is a simple, noninvasive yet highly sensitive and specific method for bladder cancer detection. The increase in urinary HA concentration is a direct correlate of the elevated tumor-associated HA levels, because the HA levels are also elevated (3–5-fold) in bladder tumor tissues (P < 0.001). The profiles of urinary HA species of normal individuals and bladder cancer patients are different. Although only the intermediate-size HA species are found in the urine of normal and low-grade bladder tumor patients, the urine of high-grade bladder cancer patients contains both the high molecular mass and the small angiogenic HA fragments. These urinary HA fragments stimulate a mitogenic response (2.4-fold) in primary human microvessel endothelial cells, suggesting that the small HA fragments may regulate tumor angiogenesis by modulating endothelial cell functions.

Footnotes

  • 1This work was supported by the Stanley Glaser Award (to V. B. L.), The Weeks Endowment Fund (to V. B. L. and N. L. B.), the Vehbi Koc Foundation, and the Scientific and Technical Research Council of Turkey (to C. Ö.).
  • 2To whom requests for reprints should be addressed, at Department of Urology (M-800), University of Miami School of Medicine, P. O. Box 016960, Miami, FL 33101. Phone: (305) 243-6321; Fax: (305) 243-6893; E-mail: blokeshw@ummednet.med.miami.edu.
Trina Links-Gowe
Trina Links-Gowe

Trina Links-Gowe is the Brand Manager of NaturPet Inc., maker of Dr. Maggie and NaturPet natural pet health products. Trina is passionate about both human and animal health and about using nature’s remedies to treat common ailments and conditions.

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