Snake fetuin: Isolation and structural analysis of new fetuin family proteins from the sera of venomous snakes

Aoki, Narumi; Deshimaru, Masanobu; Kihara, Koichi; Terada, Shigeyuki

doi:10.1016/j.toxicon.2009.05.018

Cited by 16 publications

(21 citation statements)

References 29 publications

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“…AB058635 and AB200168 respectively, were cloned previously, and their complete nucleotide sequences were analyzed to determine the primary structures of these proteins. 22,30) When their nucleotide sequences were aligned and compared, their nucleotide substitutions were observed much more frequently in the mature protein-coding regions than in the 5 0 -and 3 0 -untranslated regions, or in the signal peptide-coding regions (Fig. 1).…”

Section: Resultsmentioning

confidence: 99%

“…22,30) HSF inhibits certain types of snake venom-derived MPs and suppresses their hypodermal hemorrhage-inducing activity. 15,16,30) In addition, it possesses binding capacity to SSPs, suggesting that it serves as a carrier protein for low-molecular-weight functional proteins in habu snake blood.…”

Section: Discussionmentioning

confidence: 99%

“…[19][20][21] Indeed, in our additional study of habu serum, we isolated an HSF-like protein (HLP) with fetuin-like calcium-binding activity. 22) In the case of the mamushi snake (Gloydius blomhoffi), three isoforms of fetuin family proteins were isolated: one MP inhibitor, MSF, and two calcification inhibitors, MLP1 and MLP2. 22,23) These findings imply an evolutionary scenario in which the fetuin ancestor gene was multiplied through gene duplication, followed by an accumulation of mutations, so that some of the resulting fetuin paralogs acquired venom protease-inhibiting activity.…”

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confidence: 99%

“…22) In the case of the mamushi snake (Gloydius blomhoffi), three isoforms of fetuin family proteins were isolated: one MP inhibitor, MSF, and two calcification inhibitors, MLP1 and MLP2. 22,23) These findings imply an evolutionary scenario in which the fetuin ancestor gene was multiplied through gene duplication, followed by an accumulation of mutations, so that some of the resulting fetuin paralogs acquired venom protease-inhibiting activity. Indeed, we have observed an unusually high accumuy To whom correspondence should be addressed.…”

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confidence: 99%

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Accelerated Evolution of Fetuin Family Proteins inProtobothrops flavoviridis(Habu Snake) Serum and the Discovery of an L1-Like Genomic Element in the Intronic Sequence of a Fetuin-Encoding Gene

Tanaka

Oyama

Hori

et al. 2013

Bioscience, Biotechnology, and Biochemistry

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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Accelerated Evolution of Fetuin Family Proteins inProtobothrops flavoviridis(Habu Snake) Serum and the Discovery of an L1-Like Genomic Element in the Intronic Sequence of a Fetuin-Encoding Gene

Tanaka

Oyama

Hori

et al. 2013

Bioscience, Biotechnology, and Biochemistry

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“…Interestingly, three HSF-like proteins (HLP) showing neither antihemorrhagic nor antiproteolytic activities against SVMPs have been reported in the sera of two snakes (HLP-A and HLP-B, from Gloydius blomhoffii brevicaudus, and HLP, from Protobothrops flavoviridis) (Aoki et al 2009). Despite their homology, only HLP-B was characterized as a true snake fetuin, i.e., a serum protein capable of binding minerals, thus preventing systemic calcification.…”

Section: Structural Characterizationmentioning

confidence: 99%

Natural Inhibitors of Snake Venom Metallopeptidases

Neves-Ferreira¹,

Valente²,

Domont³

et al. 2015

Toxins and Drug Discovery

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Protein inhibitors of peptidases are widely distributed among animals, plants, and microorganisms. They are important regulatory molecules that function to avoid proteolysis in various biological systems. From the plasma of animals that are naturally resistant to snake envenomation, a special class of peptidase inhibitors has been identified. These inhibitors have antihemorrhagic properties and form inactive noncovalent complexes with snake venom metallopeptidases. In nonresistant animals, these toxic metallopeptidases induce microvascular damage and are responsible for systemic and local hemorrhage, key events in the pathogenesis of viperid envenomation. The inhibitors isolated from mammalian plasma are grouped into the MEROPS I43 family of immunoglobulin-related proteins; those from reptiles show a typical cystatin-like fold and belong to the MEROPS I25C subfamily. The inhibitors show a reversible tight-binding reaction mechanism of inhibition, although due to a lack of three-dimensional information for the enzyme-inhibitor complexes, the structural features that govern the interaction are largely unknown. This review is intended to highlight the latest advances in the field, analyzing future perspectives in the area of natural immunity against snake venom. The discussion will focus on how endogenous protein inhibitors can be used as structural templates, providing valuable insights into the molecular determinants of selective metallopeptidase inhibition. The wide range of natural toxin inhibitors may constitute a rich source of information leading to new possibilities in intervention not only against snake venom metallopeptidases but also against other metzincins, such as mammalian MMPs and ADAMs.

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