Collagenolytic Enzymes and Their Naturally Occurring Inhibitors

Sellers, Anthony; Murphy, Gillian

doi:10.1016/b978-0-12-363709-3.50010-3

Cited by 104 publications

(49 citation statements)

References 201 publications

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“…Their molecular weights vary from 30 to 150 kDa. These enzymes have been widely studied from various mammalian tissues (Sellers and Murphy, 1981;Harris and Vater, 1982), as well as from bacteria (Bond and Van Wart, 1984;Matsuhita et al, 1994) and snake venom (Bjarnason and Fox, 1994).…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of a Collagenase from the Mackerel, Scomber japonicus

Park¹,

Lee²,

Byun³

et al. 2002

BMB Reports

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Collagenase from the internal organs of a mackerel was purified using acetone precipitation, ion-exchange chromatography on a DEAE-Sephadex A-50, gel filtration chromatography on a Sephadex G-100, ion-exchange chromatography on DEAE-Sephacel, and gel filtration chromatography on a Sephadex G-75 column. The molecular mass of the purified enzyme was estimated to be 14.8 kDa by gel filtration and SDS-PAGE. The purification and yield were 39.5-fold and 0.1% when compared to those in the starting-crude extract. The optimum pH and temperature for the enzyme activity were around pH 7.

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Section: Introductionmentioning

confidence: 99%

Purification and Characterization of a Collagenase from the Mackerel, Scomber japonicus

Park¹,

Lee²,

Byun³

et al. 2002

BMB Reports

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“…Metallo-collagenases, first discovered in tadpole tissue explants (Gross and Lapiere, 1962), are zinc-containing enzymes that also generally require calcium for their optimum activity and stability, and cleave the collagen helix at a specific locus under physiological conditions (Gawston and Murphy, 1981;Harris and Vater, 1982;Sellers and Murphy, 1981;Stricklin et al, 1977). These enzymes have been widely studied from various mammalian tissues (Harris and Vater, 1982;Sellers and Murphy, 1981) as well as from bacteria, such as Bacillus cereus (Makinen and Makinen, 1987), Clostridium histolyticum (Bond and Van Wart, 1984a, b;Peterkofsky, 1982), Achromobacter (Nguyen et al, 1988), Vibrio alginolyticus (Takeuchi et al, 1992) and Clostridium perfringens (Matsuhita et al, 1994), and snake venom (Bjarnason and Fox, 1994). These metallo-collagenases, extracellular enzymes, are involved in remodeling the extracellular matrix.…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of a Collagenolytic Protease from the Filefish, Novoden modestrus

Kim¹,

Park²,

Kim³

et al. 2002

BMB Reports

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A serine collagenolytic protease was purified from the internal organs of filefish, Novoden modestrus, by ammonium sulfate, ion-exchange chromatography on a DEAE-Sephadex A-50, ion-exchange rechromatography on a DEAE-Sephadex A-50, and gel filtration on a Sephadex G-150 column. The molecular mass of the filefish serine collagenase was estimated to be 27.0 kDa by gel filtration and SDS-PAGE. The purified collagenase was optimally active at pH 7.0-8.0 and 55 o C. The purified enzyme was rich in Ala, Ser, Leu, and Ile, but poor in Trp, Pro, Tyr, and Met. In addition, the purified collagenolytic enzyme was strongly inhibited by N-P-toluenesulfonyl-L-lysine chloromethyl ketone (TLCK), diisopropylfluorophosphate (DFP), and soybean trypsin inhibitor.

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“…These enzymes are usually found in a latent form and require activation before they can digest their substrates. Collagenase, the most widely studied mammalian metalloproteinase, can be activated by trypsin, mercurials aid chaotropic ions (Sellers & Murphy, 1981), but the processes by which activation is achieved in,vivo are unclear. A specific metalloproteinase inhibitor (TIMP) is found in the culture media of many tis$ues , and in the case of rabbit bone medium it was reported to combine with crude mercurial-activated collagenase to form a complex of similar size to latent collagenase .…”

mentioning

confidence: 99%

The interaction of purified rabbit bone collagenase with purified rabbit bone metalloproteinase inhibitor

Cawston¹,

Murphy²,

Mercer³

et al. 1983

Biochemical Journal

165

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1. Pure rabbit bone metalloproteinase inhibitor (TIMP) bound tightly to pure rabbit bone collagenase with an apparent Kd of 1.4 × 10(-10) M. 2. The molecular weight of the enzyme-inhibitor complex was found to be 54 000, but no enzyme activity could be recovered from the complex after treatment with either mercurials or proteinases. The complex thus differed from latent collagenase in terms of size, susceptibility to mercurials and behaviour on concanavalin A-Sepharose. 3. The interaction of the purified components was compared with that of crude collagenase and crude inhibitor in culture medium. Mercurial treatment partially reversed the inhibition in the crude system, but not when the purified components were used. 4. The significance of the results is discussed in relation to the extracellular control of the activity of collagenase.

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Collagenolytic Enzymes and Their Naturally Occurring Inhibitors

Cited by 104 publications

References 201 publications

Purification and Characterization of a Collagenase from the Mackerel, Scomber japonicus

Purification and Characterization of a Collagenase from the Mackerel, Scomber japonicus

Purification and Characterization of a Collagenolytic Protease from the Filefish, Novoden modestrus

The interaction of purified rabbit bone collagenase with purified rabbit bone metalloproteinase inhibitor

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