Hyaluronidase
From Wikipedia, the free encyclopedia
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Hyaluronidase
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| Systematic (IUPAC) name | |
| Sheep hyaluronidase | |
| Identifiers | |
| CAS number | |
| ATC code | B06 |
| PubChem | ? |
| DrugBank | |
| Chemical data | |
| Formula | C2455H3775N617O704S21 |
| Mol. mass | 53870.9 g/mol |
| Pharmacokinetic data | |
| Bioavailability | ? |
| Metabolism | ? |
| Half life | ? |
| Excretion | ? |
| Therapeutic considerations | |
| Pregnancy cat. |
C |
| Legal status | |
| Routes | subcutaneous |
The hyaluronidases (EC 3.2.1.35) are a family of enzymes that degrade hyaluronic acid.
In humans, there are six associated genes, including HYAL1, HYAL2, HYAL3, and PH-20/SPAM1.[1]
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[edit] Use as a drug
By catalyzing the hydrolysis of hyaluronic acid, a major constituent of the interstitial barrier, hyaluronidase lowers the viscosity of hyaluronic acid, thereby increasing tissue permeability. It is, therefore, used in medicine in conjunction with other drugs in order to speed their dispersion and delivery. The most common application is in ophthalmic surgery, in which it is used in combination with local anesthetics. It also increases the absorption rate of parenteral fluids given by hypodermoclysis, and is an adjunct in subcutaneous urography for improving resorption of radiopaque agents. Hyalurodinase is also used for extravasation of hyperosmolar solutions. Usually a 0.2 ml of the drug is injected around the area of extravasation. A total of 1 ml is used.
Brand names of animal-derived hyaluronidase include HydaseTM (developed and manufactured by PrimaPharm Inc., distributed by Akorn Inc.) which has been FDA approved as a "Thimerosal free" animal-derived hyaluronidase, Vitrase (ISTA Pharmaceuticals), Amphadase (Amphastar Pharmaceuticals) and Wydase. Wydase, however, is no longer manufactured.
On December 2, 2005, the FDA approved a synthetic (recombinant or rDNA) "human" hyaluronidase, Hylenex (Halozyme Therapeutics).[2]
[edit] Pathogenic production
Some bacteria, such as Staphylococcus aureus, Streptococcus pyogenes,[3] and Clostridium perfringens,[4] produce hyaluronidase as a means for greater mobility through the body's tissues and as an antigenic disguise that prevents their being recognized by phagocytes of the immune system.
[edit] Role in fertilization
In most mammalian fertilization, hyaluronidase is released by the acrosome of the sperm cell after it has reached the oocyte, by digesting proteins in the zona pellucida, thus enabling conception.
[edit] References
- ^ Csoka AB, Frost GI, Stern R (December 2001). "The six hyaluronidase-like genes in the human and mouse genomes". Matrix biology : journal of the International Society for Matrix Biology 20 (8): 499–508. PMID 11731267. http://linkinghub.elsevier.com/retrieve/pii/S0945-053X(01)00172-X.
- ^ "Halozyme Therapeutics and Baxter Healthcare Corporation Announce FDA Approval of Hylenex". http://www.baxter.com/about_baxter/news_room/news_releases/2005/12-05-05-hylenex.html. Retrieved on 2008-11-07.
- ^ Starr CR, Engleberg NC (January 2006). "Role of hyaluronidase in subcutaneous spread and growth of group A streptococcus". Infection and immunity 74 (1): 40–8. doi:. PMID 16368955. PMC: 1346594. http://iai.asm.org/cgi/pmidlookup?view=long&pmid=16368955.
- ^ Zukaite V, Biziulevicius GA (March 2000). "Acceleration of hyaluronidase production in the course of batch cultivation of Clostridium perfringens can be achieved with bacteriolytic enzymes". Letters in applied microbiology 30 (3): 203–6. PMID 10747251. http://www.blackwell-synergy.com/openurl?genre=article&sid=nlm:pubmed&issn=0266-8254&date=2000&volume=30&issue=3&spage=203.
[edit] External links
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