Novel gelatinolytic activities in rat organs

Kubota, Shin; Yokoyama, Yoshihiro; Toyohara, Haruhiko; Sakaguchi, Morihiko

doi:10.1080/15216549900201623

Cited by 4 publications

(3 citation statements)

References 6 publications

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“…The isolated cDNA was then expressed in Escherichia coil and the recombinant protein was found to degrade human type V collagen, which is one of the constituents of ECM 10 . Alternatively, a variety of gelatinolytic activities resulting from metalloproteinases have been detected in fish tissues, which were expressed at a higher level than those of rat tissues 11,12 . Together with these findings, it is suggested that MMP degrade ECM components, including collagen, in fish muscle and, consequently, trigger postmortem tenderization.…”

Section: Resultsmentioning

confidence: 99%

Possible implication of metalloproteinases in post-mortem tenderization of fish muscle

et al. 2001

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It is suspected that the proteolytic breakdown of extracellular matrix proteins is responsible for the postmortem tenderization of fish muscle during chilled storage. In order to identify the type(s) of proteinases involved in this phenomenon, the effect of proteinase inhibitors, EDTA (ethylenediamine tetraacetic acid), 1,10‐phenanthroline, ρ‐APMSF [(ρ‐amidinophenyl) methanesulfonyl fluoride hydrochloride] and E‐64 [L‐trans‐epoxysuccinyl‐leucylamido‐(4‐guanidinobutane)] on tenderization was investigated by using Japanese flounder. Proteinase inhibitor solution was injected into a blood vessel in a caudal portion of live flounder and the firmness of muscle was then evaluated as a shear force value at 0 h and 6 h after death. Metalloproteinase inhibitors, EDTA and 1,10‐phenanthroline, significantly suppressed postmortem tenderization. These findings suggest that metalloproteinases are candidates for proteinases involved in the postmortem tenderization of fish muscles. Although not significantly, p‐APMSF, a serine proteinase inhibitor, partially suppressed muscle tenderization, which suggests that serine proteinases are also implicated in postmortem tenderization. A cysteine proteinase inhibitor, E‐64, showed no effect, suggesting that cysteine proteinases are not involved.

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Section: Resultsmentioning

confidence: 99%

Possible implication of metalloproteinases in post-mortem tenderization of fish muscle

et al. 2001

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“…(1992) suggested that gelatinolytic serine proteinases secreted by human gastric carcinoma cell line may play a major role in the matrix degradation and subsequent tumor cell invasion, and these serine proteinases are called matrix serine proteinases. Kubota et al. (1999) suggested that gelatin‐degrading activities due to metalloproteinases and serine proteinases were constitutively expressed in various rat normal organs.…”

Section: Discussionmentioning

confidence: 99%

Gelatinolytic Serine Proteinases From the Wing Muscle of Red Stingray

Bae

Shimazoe

Yoshida

et al. 2010

Journal of Food Biochemistry

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Four gelatinolytic proteinases (A1, 97 kDa; A2, 66 kDa; A3, 30 kDa; A4, 23 kDa) were detected from the red stingray wing muscle by gelatin zymography. Among these proteinases, major gelatinolytic proteinases (A1, A2) were more purified and examined their characters. The optimum pH and temperature for the gelatinolytic activity of A1 and A2 were around pH 7 and pH 8, and maximal activity of A1 is at 30–50C, that of A2 is at 30C. Also, they were demonstrated to hydrolyze the gelatin from red stingray; protein bands were almost completely degraded after 6 h incubation at 37C and pH 7.5. Both enzymes were strongly inhibited by Pefabloc SC, which suggests that they belong to gelatinolytic serine protease. PRACTICAL APPLICATIONS Gelatinolytic enzyme hydrolyzes denatured collagen such as gelatin. The enzymes from red stingray may be utilized to produce gelatin peptide, which has been widely used as additive to enhance the elasticity, consistency and stability of food products. In addition, it is meaningful in that this study will give information to understand the gelatinolytic proteinases in ray species and could lead to a comparative study of the biochemical properties of gelatinolytic proteinases in elasmobranch and many other species.

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“…40,41 MMP activities are properly regulated in living fish, but they are activated and may lead to unwanted proteolysis in the intramuscular connective tissue after death. Because MMP activities assessed by gelatin zymography were significantly higher in various tissues and organs of yellowtail tissues than in those of rat tissues, 24,42 it seems likely that remarkable tenderization of fish muscle after death is partly ascribable to the higher activity level of MMP in fish muscle. Proteolytic breakdown of the extracellular matrix proteins in the intramuscular connective tissue by MMP is mainly responsible for the muscle tenderization during chilled storage.…”

Section: Activity Toward Crude Connective Tissue Preparation At Chillmentioning

confidence: 99%

Solubilization of type I collagen from fish muscle connective tissue by matrix metalloproteinase-9 at chilled temperature

et al. 2003

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Post‐mortem muscle tenderization during chilled storage is thought to result from loss of physical strength due to the disintegration of intramuscular connective tissue. Although metalloproteinases may be involved in the disintegration, details of the proteolytic processes occurring during chilled storage remain to be elucidated. To determine the involvement of matrix metalloproteinase‐9 (MMP‐9) in the post‐mortem disintegration of intramuscular connective tissue, we produced recombinant Japanese flounder MMP‐9 (jfMMP‐9) in COS‐7 cells. The recombinant jfMMP‐9 showed gelatinolytic activity in the zymographic analysis at chilled temperature, but no apparent proteolytic activity against the triple helical domain of types I and type V collagens. In contrast, recombinant jfMMP‐9 solubilized type I collagen from a crude connective tissue preparation at chilled temperature. This finding, together with the fact that a protein corresponding to MMP‐9 was immunologically detected in the muscle extract, indicates that MMP‐9 may be involved in the disintegration of the intramuscular connective tissue that induces the post‐mortem tenderization of fish muscle during chilled storage.

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Novel gelatinolytic activities in rat organs

Cited by 4 publications

References 6 publications

Possible implication of metalloproteinases in post-mortem tenderization of fish muscle

Possible implication of metalloproteinases in post-mortem tenderization of fish muscle

Gelatinolytic Serine Proteinases From the Wing Muscle of Red Stingray

Solubilization of type I collagen from fish muscle connective tissue by matrix metalloproteinase-9 at chilled temperature

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