Hydrolysis of synthetic peptides by collagenase

Nagai, Yutaka; Sakakibara, Shumpei; Noda, Haruhiko; Akabori, Shirô

doi:10.1016/0006-3002(60)90531-x

Cited by 66 publications

(18 citation statements)

References 3 publications

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“…Although assays of tumour peptidase with Pz-substrate by Keiditsch and Strauch (1970) corresponded closely with results obtained by the method of Nagai et al (1966) using 14C-labelled collagen as substrate, collagen peptidase and collagenase when isolated and purified are not identical. A similar distribution of the enzymes suggesting a close functional relationship was also recorded by Robertson and Williams (1969) in an invasive rat epithelioma where collagen-peptidase and true collagenolytic activity were found in corresponding regions of the tumour periphery.…”

supporting

confidence: 68%

“…FOLLOWING study of collagenase enzymes with synthetic peptides by Nagai et al (1960), introduction of the chromophore substrate p-phenyl-azo-benzyloxycarbonyl-pro-leu-gly-pro-D.arginine by Wunsch and Heidrich (1963) enabled collagen-peptidase activity, specific for apolar peptide sequences analogous to those of the collagen molecule, to be identified and assayed in mouse and chick embryo and in human HeLa cells by Strauch (1967), Strauch and Vencelj (1967) and Strauch et al (1968). Although assays of tumour peptidase with Pz-substrate by Keiditsch and Strauch (1970) corresponded closely with results obtained by the method of Nagai et al (1966) using 14C-labelled collagen as substrate, collagen peptidase and collagenase when isolated and purified are not identical.…”

mentioning

confidence: 99%

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Inhibition of collagen peptidase in HeLa cells and human tumours by compounds including drugs used in cancer therapy

Boggust¹,

McGauley²

1978

Br J Cancer

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Summary.-Collagen-peptidase activity in extracts of HeLa cells and human tumours is inactivated by Razoxane (ICRF-159), cyclophosphamide, 5-fluorouracil, thiotepa, aprotinin, EDTA and phenanthroline. As this activity, in association with other enzymes, may contribute to tissue lysis in cancers, chemical intervention may reduce invasiveness and modify the processes of infiltration and metastasis. Accordingly, some drugs used in therapy or for the prevention of metastasis may produce their observed effects by a combination of factors including enzyme inhibition.

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supporting

confidence: 68%

mentioning

confidence: 99%

Inhibition of collagen peptidase in HeLa cells and human tumours by compounds including drugs used in cancer therapy

Boggust¹,

McGauley²

1978

Br J Cancer

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“…The same tetrapeptide Pro-Leu-Gly-Pro with a free amino group was cleaved neither by the collagenase from Clostridium [5,14] nor by the Achromobacter enzyme. Yagisawa et al [5] reported this peptide to be a non-competitive inhibitor of collagenase from Clostridium.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of Collagenase from Achromobacter iophagus by Synthetic Peptides

Svensson

Siffert

Keil

1975

European Journal of Biochemistry

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Peptides of the general structure Pro‐Leu‐X‐Pro have been synthesized, with proline in l or d‐form and with either glycine or sarcosine in the position of X. Their inhibitory action on the cleavage of the peptide Cbz‐Gly‐Pro‐Leu‐Gly‐Pro by pure collagenase from Achromobacter iophagus was studied. Competitive inhibition was found in all cases, the most efficient by Pro‐Leu‐MeGly‐Pro. One product of cleavage of the synthetic substrate, Cbz‐Gly‐Pro‐Leu, also inhibits the enzyme.

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“…The former peptide was described as one of the most suitable substrates for collagenase (10), and the latter was claimed to be a specific substrate attacked only by collagenases (15). Compared to Cl.…”

mentioning

confidence: 99%

Detection and production of extracellular collagenolytic enzyme from Zygosaccharomyces rouxii.

Taing

Hashinaga

1996

J. Gen. Appl. Microbiol.

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Microbial collagenases are proteinases that are capable of hydrolyzing native collagen in vitro under physiological conditions ( 7) . Production of collagenase or collagenase-like proteases from various bacteria have been reported by many workers. Among the collagenase-producing bacteria, Clostridium histolyticum is the most studied microorganism and crude or purified collagenase from this bacteria are now available commercially. There have been works published on collagenase from the mold Trichophyton shoenleinii (13) and Aspergillus oryzae (12). However, reports on the presence of collagenolytic activity in yeasts are very rare. In the book, "The Yeasts: A Taxonomic Study," it is stated that with the exception of Cryptococcus species, few yeasts have the ability to liquefy gelatin which is a denatured form of collagen (5). Through our identification of sugartolerant yeasts isolated from high-sugar foods, we found a few strains of Zygosaccharomyces rouxii that possessed the activity of gelatin liquefaction. Although the enzyme active against gelatin may not be active against collagen, as pointed out by Merkel et al. (9), we were prompted by our results and regarded that it would be beneficial to investigate the presence of collagenolytic enzyme from a different source. This paper reports the isolation of crude enzyme from a gelatin-liquefaction strain of yeast and determination of its activity against various substrates including insoluble collagen. We dealt also with the cultural conditions that affected the production of the enzyme. Comparison was made between the yeast enzyme and Cl. histolyticum collagenase.Sugar-tolerant yeasts including 19 strains of Z. rouxii and one strain of Torulaspora delbrueckii, isolated from high-sugar foods were used for screening

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Hydrolysis of synthetic peptides by collagenase

Cited by 66 publications

References 3 publications

Inhibition of collagen peptidase in HeLa cells and human tumours by compounds including drugs used in cancer therapy

Inhibition of collagen peptidase in HeLa cells and human tumours by compounds including drugs used in cancer therapy

Inhibition of Collagenase from Achromobacter iophagus by Synthetic Peptides

Detection and production of extracellular collagenolytic enzyme from Zygosaccharomyces rouxii.

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