collagenase

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Related to Collagenases: Interstitial collagenase

col·lag·e·nase

 (kə-lăj′ə-nās′, -nāz′, kŏl′ə-jə-)
n.
Any of various enzymes that catalyze the hydrolysis of collagen and gelatin.

collagenase

(ˈkɒlədʒəˌneɪz)
n
(Biochemistry) an enzyme that decomposes collagen
ThesaurusAntonymsRelated WordsSynonymsLegend:
Noun1.collagenase - any enzyme that catalyzes the hydrolysis of collagen and gelatin
enzyme - any of several complex proteins that are produced by cells and act as catalysts in specific biochemical reactions
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References in periodicals archive ?
The clostridial collagenase produced by BioSpecifics has a broad specificity towards collagen and is acknowledged as much more efficient than mammalian collagenases.
NASDAQ: BSTC), a biopharmaceutical company developing first in class collagenase-based products, today announced that positive data for XIAPEX (clostridial collagenase histolyticum for injection) were presented at the XVIth Annual Federation of European Societies for Surgery of the Hand (FESSH) Congress which took place in Oslo, Norway at the Oslo Congress Centre on May 26-28, 2011.
Collagenases break down the native collagen that holds animal tissues together, are made by a variety of microorganisms and by many different animal cells.
However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases.
The formulation, made up of two collagenases produced by the bacterium Clostridium histolyticurn, is injected into the cord at 4-week intervals, for a maximum of three injections, according to the manufacturer, Auxilium Pharmaceuticals Inc.
Behind collagen's breakdown were enzymes, such as collagenases.
Collagenase clostridium histolyticum is a combination of two purified collagenases (collagenase is an enzyme capable of breaking down collagen), derived from the bacterium Clostridium histolyticum.
The Clostridial collagenase produced by BioSpecifics has a broad specificity towards all types of collagen and is acknowledged as much more efficient than mammalian collagenases.
Strauss III, director of the Center for Research on Women's Health and Reproduction at the University of Pennsylvania in Philadelphia, and his colleagues focused on a family of enzymes called collagenases.
The second grant will fund a project related to the development of improved collagenases for tissue disassociation related to cellular therapy.
The goal of the study was to determine whether a specific peptide (a collagen fragment) up-regulated gene expression and protein production of collagenases in isolated normal human chondrocytes, and to determine which receptor and signaling pathways were involved in this up-regulation.
This special design may explain the effect of heparin on the determination of TEMP-2, because heparin might interact with proMMP-2 in the proMMP-2-TIMP-2 complex, as found in studies on interaction between heparin and collagenase (18).