Characterization of lizard venom hyaluronidase and evidence for its action as a spreading factor

Tu, Anthony T.; Hendon, Robert R.

doi:10.1016/0305-0491(83)90086-x

Cited by 86 publications

(60 citation statements)

References 18 publications

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“…Hyaluronidase enzymes across animal taxa show lower levels of sequence diversity than other toxins, and no new activities have been reported for either venom or body forms. Those recruited most likely act primarily as diffusion factors, enhancing tissue permeability to allow a more efficient spreading of toxins or hemostatic factors (153).…”

Section: Hyaluronidasementioning

confidence: 99%

The Toxicogenomic Multiverse: Convergent Recruitment of Proteins Into Animal Venoms

Fry

Roelants

Champagne

et al. 2009

Annu. Rev. Genom. Hum. Genet.

709

778

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Throughout evolution, numerous proteins have been convergently recruited into the venoms of various animals, including centipedes, cephalopods, cone snails, fish, insects (several independent venom systems), platypus, scorpions, shrews, spiders, toxicoferan reptiles (lizards and snakes), and sea anemones. The protein scaffolds utilized convergently have included AVIT/colipase/prokineticin, CAP, chitinase, cystatin, defensins, hyaluronidase, Kunitz, lectin, lipocalin, natriuretic peptide, peptidase S1, phospholipase A 2 , sphingomyelinase D, and SPRY. Many of these same venom protein types have also been convergently recruited for use in the hematophagous gland secretions of invertebrates (e.g., fleas, leeches, kissing bugs, mosquitoes, and ticks) and vertebrates (e.g., vampire bats). Here, we discuss a number of overarching structural, functional, and evolutionary generalities of the protein families from which these toxins have been frequently recruited and propose a revised and expanded working definition for venom. Given the large number of striking similarities between the protein compositions of conventional venoms and hematophagous secretions, we argue that the latter should also fall under the same definition. 483

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Section: Hyaluronidasementioning

confidence: 99%

The Toxicogenomic Multiverse: Convergent Recruitment of Proteins Into Animal Venoms

Fry

Roelants

Champagne

et al. 2009

Annu. Rev. Genom. Hum. Genet.

709

778

View full text Add to dashboard Cite

show abstract

“…These enzymes supposedly serve as "spreading factors" by degrading HA, thereby facilitating the diffusion of other venom constituents. A few of these enzymes have been characterized to some extent (Tu & Hendon, 1983;Ramanaiah et al, 1990;Poh et al, 1992). In particular, the enzyme from bee venom has been investigated in detail.…”

Section: Hyases From Animal Venomsmentioning

confidence: 99%

Hyaluronidases - a group of neglected enzymes

Kreil¹

1995

Protein Sci.

325

219

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Hyaluronan is an important constituent of the extracellular matrix. This polysaccharide can be hydrolyzed by various hyaluronidases that are widely distributed in nature. The structure of some bacterial and animal enzymes of this type has recently been elucidated. It could be shown that the hyaluronidases from bee and hornet venom and the PH-20 hyaluronidase present on mammalian spermatozoa are homologous proteins.

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“…Hyaluronidase has also been identified in insect venom and snake venom. Presence of hyaluronidase in the venom enhances the spread of the toxin (18,19). Many hyaluronidases have been described based on their enzymatic action (14).…”

mentioning

confidence: 99%

Expression of hyaluronidase by tumor cells induces angiogenesis in vivo.

Liu

Pearlman

Diaconu

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

216

140

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Hyaluronic acid is a proteoglycan present in the extracellular matrix and is important for the maintenance of tissue architecture. Depolymerization of hyaluronic acid may facilitate tumor invasion. In addition, oligosaccharides of hyaluronic acid have been reported to induce angiogenesis. We report here that a hyaluronidase similar to the one on human sperm is expressed by metastatic human melanoma, colon carcinoma, and glioblastoma cell lines and by tumor biopsies from patients with colorectal carcinomas, but not by tissues from normal colon. Moreover, angiogenesis is induced by hyaluronidase+ tumor cells but not hyaluronidase-tumor cells and can be blocked by an inhibitor of hyaluronidase. Tumor cells thus use hyaluronidase as one of the "molecular saboteurs" to depolymerize hyaluronic acid to facilitate invasion. As a consequence, breakdown products of hyaluronic acid can further promote tumor establishment by inducing angiogenesis. Hyaluronidase on tumor cells may provide a target for anti-neoplastic drugs.

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Characterization of lizard venom hyaluronidase and evidence for its action as a spreading factor

Cited by 86 publications

References 18 publications

The Toxicogenomic Multiverse: Convergent Recruitment of Proteins Into Animal Venoms

The Toxicogenomic Multiverse: Convergent Recruitment of Proteins Into Animal Venoms

Hyaluronidases - a group of neglected enzymes

Expression of hyaluronidase by tumor cells induces angiogenesis in vivo.

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