Purification, characterization and immobilization of proteinase inhibitors from Stichodactyla helianthus

Delfín, Julieta; Díaz, Javier Santovenia; Antuch, Walfrido; Rodríguez, R; González, Yoel Martínez; Morera, Vivian; Martínez, Isabel Lorente; Ларионова, Н. И.; Padrón, Gabrìel; Chávez, María Á.

doi:10.1016/0041-0101(96)80902-0

Cited by 10 publications

(23 citation statements)

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“…Thus, they strongly inhibit trypsin-like enzymes, but also chymotrypsin and HNE, with comparatively lower affinity. In contrast, the interaction with PPE is usually very weak or not observed at all (18,21). This elastase specificity could be attributed to a more flexible S1 pocket in HNE that allows accommodation of a broad variety of P1 residues (11,(22)(23)(24).…”

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confidence: 80%

“…We reported previously the isolation as well as functional and structural characterization of the BPTI-Kunitz-type inhibitor ShPI-1 from the Caribbean sea anemone Stichodactyla helianthus (UniProt accession number P31713) (21,36). This molecule inhibits not only serine proteases but also cysteine and aspartic proteases such as papain and pepsin with K i values in the nanomolar range (21), qualifying ShPI-1 for biotechnological use (37).…”

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confidence: 99%

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Three-dimensional Structure of a Kunitz-type Inhibitor in Complex with an Elastase-like Enzyme

García-Fernández

Perbandt

Roggenbuck³

et al. 2015

Journal of Biological Chemistry

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Background: Kunitz-type inhibitors provide a suitable scaffold for novel elastase inhibitors. Results: The inhibitor ShPI-1 was modified for pancreatic elastase binding, and the crystal structure of the complex was elucidated and analyzed. Conclusion: The extended protease-inhibitor interactions provide a potential switch to direct inhibitor selectivity toward elastases. Significance: These results will help to design novel elastase inhibitors for the treatment of tissue destruction diseases.

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confidence: 80%

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confidence: 99%

Three-dimensional Structure of a Kunitz-type Inhibitor in Complex with an Elastase-like Enzyme

García-Fernández

Perbandt

Roggenbuck³

et al. 2015

Journal of Biological Chemistry

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“…The marine Caribbean fauna is characterized by its richness and diversity, which make it a very attractive natural source for the identification of novel biomolecules with biological and biomedical interests. The potential of marine invertebrates as a source of these biomolecules has been reported in previous studies, particularly those focused on endoproteases such as serine and cysteine proteases and their inhibitors, some with exceptional structural and functional properties (2,(12)(13)(14).…”

Section: Nvci Is a Novel Exogenous Proteinaceous Inhibitor Of Metallomentioning

confidence: 99%

Crystal Structure of Novel Metallocarboxypeptidase Inhibitor from Marine Mollusk Nerita versicolor in Complex with Human Carboxypeptidase A4

Covaleda

Rivero

Chávez

et al. 2012

Journal of Biological Chemistry

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Background: Only a few proteinaceous inhibitors of metallocarboxypeptidases have been characterized structurally in depth.Results: The structure of human carboxypeptidase A4 in complex with a Nerita versicolor inhibitor (NvCI) was derived at 1.7 Å. Conclusion: NvCI displays a different protein fold that inhibits carboxypeptidases in a substrate-like manner. Significance: We deciphered the structural determinants for picomolar inhibition constants for A-type carboxypeptidases, the most potent by now.

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“…Although the first toxins isolated from these cnidarians were neurotoxins (Béress & Béress 1974), cardiotoxins (Simpson et al 1990), and several cytolysins (Kem 1988), protease inhibitors have also been found (Delfín et al 1996). Indeed, although some anemone toxins have been extensively investigated during recent years, information regarding the biological activity of many of them is scarce.…”

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confidence: 99%

Isolation, Partial Purification and Characterization of Active Polypeptide from the Sea Anemone Bartholomea annulata

Sánchez‐Rodríguez¹,

Zugasti²,

Santamarı́a³

et al. 2006

Basic Clin Pharma Tox

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In the sea anemone Bartholomea annulata, four different types of cnidocysts, basitrichous isorhizas, microbasic p-mastigophores, microbasic amastigophores and spirocysts were identified. In relation to the efficacy of different substances to induce discharge of nematocysts we observe that distilled water induced more than 70% of microbasic pmastigophores to discharge, whereas spirocysts were discharged in a lesser extent (∑20%). The median lethal dose (LD 50 ) in mice was found after injection of 700.7 mg protein per kg of body weight from the crude extract. The protein with neurotoxic effect was isolated using low-pressure liquid chromatography. The neurotoxic activity was determined using sea crabs (Ocypode quadrata), injecting 15 mg of crude extract or isolated fraction into the third walking leg, and violent motor activity followed by progressive loss of sensibility to external stimuli, further leading to full paralysis were observed. The active fraction (called V) eluted at 43.9 min.Sea anemones as well as corals, hydrozoans, scyphozoans and cubozoans, are included in the Phylum Cnidaria, the only group in the animal kingdom with the ability to produce cnidocysts. Cnidocysts are among the largest and most complex intracellular secretion products known (Holstein & Tardent 1984). There are 28 types of morphologically distinct cnidocysts, which are divided into three subcategories: nematocysts (25 different types), spirocysts (2 types), and one type of ptychocysts (Mariscal 1974). From these three subcategories, only nematocysts inject toxins into prey, and thus they are considered as the most sophisticated lethal weapons in the animal kingdom (Tardent 1995).Nematocysts from sea anemones contain complex mixtures of biologically active compounds, mainly consisting of peptides and proteins (Béress 1982;Hessinger 1988;Kem 1988;Norton 1991). Although the first toxins isolated from these cnidarians were neurotoxins (Béress & Béress 1974), cardiotoxins (Simpson et al. 1990), and several cytolysins (Kem 1988), protease inhibitors have also been found (Delfín et al. 1996). Indeed, although some anemone toxins have been extensively investigated during recent years, information regarding the biological activity of many of them is scarce. In the particular case of Bartholomea annulata, the only report in the literature is the study by Santamaría et al. (2002). In this study, the authors evaluated the haemolytic and peroxidative responses by the crude extract in mice erythrocytes. In consideration of the information mentioned above, the aim of this work is to evaluate the biotoxic parameters of both the crude extract and the partially purified venom from B. annulata in different experimental models. Materials and MethodsIn order to identify the different types of cnidocysts present in tentacles of B. annulata, preparations were preserved with 4% formaldehyde, glycerine and 96% ethyl alcohol, and analyzed by light microscopy (20¿, 40¿ and 100¿). Cnidocysts from both fresh and frozen specimens were also observed i...

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Purification, characterization and immobilization of proteinase inhibitors from Stichodactyla helianthus

Cited by 10 publications

References 0 publications

Three-dimensional Structure of a Kunitz-type Inhibitor in Complex with an Elastase-like Enzyme

Three-dimensional Structure of a Kunitz-type Inhibitor in Complex with an Elastase-like Enzyme

Crystal Structure of Novel Metallocarboxypeptidase Inhibitor from Marine Mollusk Nerita versicolor in Complex with Human Carboxypeptidase A4

Isolation, Partial Purification and Characterization of Active Polypeptide from the Sea Anemone Bartholomea annulata

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