Collagenase enzymes from Clostridium: characterization of individual enzymes

Lwebuga‐Mukasa, Jamson S.; Harper, Elvin; Taylor, Palmer

doi:10.1021/bi00666a031

Cited by 54 publications

(26 citation statements)

References 32 publications

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“…Accordingly, it has been suggested that AChE molecules reside within the synaptic cleft substance (BETZ & SAKMANN, 1973) where they are bound to an unidentified filamentous component of the basement membrane matrix (RASH & ELLISMAN, 1974). Recently it has been reported that collagenase-induced release of AChE from electroplax tissue of Torpedo calfornica is accompanied by release of hydroxyproline containing peptides (LWEBUGA-MUKASA et al, 1976). Further, the authors state that "there are distinct similarities between the tail unit of AChE and basement membrane components" and provide strong support to the possibility of an association between AChE and the basement membrane.…”

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confidence: 97%

EFFECT OF DENERVATION AND OF AXOPLASMIC TRANSPORT BLOCKAGE ON THE IN VITRO RELEASE OF MUSCLE ENDPLATE ACETYLCHOLINESTERASE

Inestrosa

Ramírez

Fernández

1977

Journal of Neurochemistry

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Abstract— Cat geniohyoid muscle samples containing endplate regions, when incubated in vitro at 37°C in phosphate buffer (pH 73, release acetylcholinesterase (AChE; EC 3.1.1.7) to the bathing medium. By treating the muscle samples with collagenase (EC 3.4.4.19), it was confirmed that most of the AChE released came from the endplates. Enzyme liberation was studied 10 days after either local injection of 10mM‐cokhicine into the hypoglossal nerve or following nerve transection. Results showed that the rate of release is increased by denervation, but is not affected by axoplasmic transport blockage. It is postulated that the cellular contact between nerve and muscle—altered by denervation but not by interruption of axoplasmic transport—is an essential factor in maintaining the localization of end‐plate AChE within the synaptic cleft substance. This does not invalidate the possible participation of ACh and muscle activity in such enzyme localization.

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confidence: 97%

EFFECT OF DENERVATION AND OF AXOPLASMIC TRANSPORT BLOCKAGE ON THE IN VITRO RELEASE OF MUSCLE ENDPLATE ACETYLCHOLINESTERASE

Inestrosa

Ramírez

Fernández

1977

Journal of Neurochemistry

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“…2) To date bacterial collagenases have been purified from various species, such as C. histolyticum, [3][4][5][6] C. perfringens, 7) Pseudomonas marinoglutinosa, 8) V. alginolyticus, [9][10][11] and Streptomyces sp., [12][13][14][15][16] and partially characterized. The V. parahaemolticus collagenase was obtained by expression of the gene in Escherichia coli and partially characterized.…”

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Purification and Characterization of a Major Collagenase fromStreptomyces parvulus

Sakurai

Inoue

Nishii

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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“…Its purification by various techniques resulted in identification of from two to seven different collagenase fractions (16,17,20,23,27,40). Despite extensive studies by a number of workers, there is no general consensus as to the number of enzymes and their properties.…”

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Cloning and nucleotide sequence analysis of the colH gene from Clostridium histolyticum encoding a collagenase and a gelatinase

et al. 1994

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The colH gene encoding a collagenase was cloned from Clostridium histolyticum JCM 1403. Nucleotide sequencing showed a major open reading frame encoding a 116-kDa protein of 1,021 amino acid residues. The deduced amino acid sequence contains a putative signal sequence and a zinc metalloprotease consensus sequence, HEXXH. A 116-kDa collagenase and a 98-kDa gelatinase were copurified from culture supernatants of C. histolyticum. While the former degraded both native and denatured collagen, the latter degraded only denatured collagen. Peptide mapping with V8 protease showed that all peptide fragments, except a few minor ones, liberated from the two enzymes coincided with each other. Analysis of the N-terminal amino acid sequence of the two enzymes revealed that their first 24 amino acid residues were identical and coincided with those deduced from the nucleotide sequence. These results indicate that the 98-kDa gelatinase is generated from the 116-kDa collagenase by cleaving of the C-terminal region, which could be responsible for binding or increasing the accessibility of the collagenase to native collagen fibers. The role of the C-terminal region in the functional and evolutional aspects of the collagenase was further studied by comparing the amino acid sequence of the C. histolyticum collagenase with those of three homologous enzymes: the collagenases from Clostridium perfringens and Vibrio alginolyticus and Achromobacter lyticus protease I.

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Collagenase enzymes from Clostridium: characterization of individual enzymes

Cited by 54 publications

References 32 publications

EFFECT OF DENERVATION AND OF AXOPLASMIC TRANSPORT BLOCKAGE ON THE IN VITRO RELEASE OF MUSCLE ENDPLATE ACETYLCHOLINESTERASE

EFFECT OF DENERVATION AND OF AXOPLASMIC TRANSPORT BLOCKAGE ON THE IN VITRO RELEASE OF MUSCLE ENDPLATE ACETYLCHOLINESTERASE

Purification and Characterization of a Major Collagenase fromStreptomyces parvulus

Cloning and nucleotide sequence analysis of the colH gene from Clostridium histolyticum encoding a collagenase and a gelatinase

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