Isolation and characterization of hyaluronidase a “spreading factor” from Indian cobra (Naja naja) venom

Girish, K. S.; Shashidharamurthy, Rangaiah; Nagaraju, S.; Gowda, T. Veerabasappa; Kemparaju, K.

doi:10.1016/j.biochi.2004.02.004

Cited by 112 publications

(106 citation statements)

References 32 publications

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“…edema, necrosis and hemorrhagic blistering commonly seen after H. hypnale bites (11,12,(43)(44)(45). In addition, hyaluronidase that presents substantially in the venom can synergistically potentiate the venom propagation and its local effects, contributing to severe local tissue destruction (46).…”

Section: Biological Properties Of H Hypnale and C Rhodostoma Venomsmentioning

confidence: 99%

Enzymatic and toxinological activities of Hypnale hypnale (hump-nosed pit viper) venom and its fractionation by ion exchange high performance liquid chromatography

Tan¹,

Sim²,

Gnanathasan³

et al. 2011

J. Venom. Anim. Toxins incl. Trop. Dis

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Abstract:Hypnale hypnale (hump-nosed pit viper) has been recently identified as one of the medically important venomous snakes in Sri Lanka and on the southwestern coast of India. The characterization of its venom is essential for understanding the pathophysiology of envenomation and for optimizing its management. In the present study, the biological properties of Hypnale hypnale venom and venom fractions obtained using Resource Q ion exchange chromatography were determined. The venom exhibited toxic activities typical of pit viper venom, comparable to that of its sister taxon, the Malayan pit viper (Calloselasma rhodostoma). Particularly noteworthy were its high activities of thrombin-like enzyme, proteases, phospholipase A 2 , L-amino acid oxidase and hyaluronidase. The thrombin-like enzyme was mainly acidic and distributed over several chromatography fractions, indicating its existence in multiple isoforms. The hemorrhagic and necrotic activities of the venom were likely associated with the proteolytic enzyme found mainly in the basic fraction. Phospholipase A 2 and phosphomonoesterase exist in both acidic and basic isoforms, while L-amino acid oxidase and hyaluronidase are highly acidic. The venom clotting activity on fibrinogens showed distinct species specificity in the following increasing order for clotting time: bovine < rabbit < goat < human < horse < < dog, and was comparable to that of C. rhodostoma venom. Its clot formation on human fibrinogen is gradual and prolonged, a phenomenon suggestive of consumptive coagulopathy as a complication observed clinically. At an intramuscular sublethal dose, the venom did not cause acute kidney injury in a rodent model, contrary to the positive control group treated with Daboia russelii venom. Nephrotoxicity may result from higher venom doses in the context of coagulopathy, as a complication provoked by venom hematoxicity.

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Section: Biological Properties Of H Hypnale and C Rhodostoma Venomsmentioning

confidence: 99%

Enzymatic and toxinological activities of Hypnale hypnale (hump-nosed pit viper) venom and its fractionation by ion exchange high performance liquid chromatography

Tan¹,

Sim²,

Gnanathasan³

et al. 2011

J. Venom. Anim. Toxins incl. Trop. Dis

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“…Hyaluronidase is crucial for the spread of bacterial infections, toxins, and venoms (19,20). The human genome contains six hyaluronidase genes, found on two chromosomes: 3p 21.3 (HYAL1, HYAL2, and HYAL3) and 7q 21.3 (HYAL4, PH20, and HYALP1; ref.…”

Section: Introductionmentioning

confidence: 99%

HYAL1 Hyaluronidase in Prostate Cancer: A Tumor Promoter and Suppressor

Lokeshwar

Cerwinka²,

Isoyama³

et al. 2005

Cancer Research

153

160

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Hyaluronidases degrade hyaluronic acid, which promotes metastasis. HYAL1 type hyaluronidase is an independent prognostic indicator of prostate cancer progression and a biomarker for bladder cancer. However, it is controversial whether hyaluronidase (e.g., HYAL1) functions as a tumor promoter or as a suppressor. We stably transfected prostate cancer cells, DU145 and PC-3 ML, with HYAL1-sense (HYAL1-S), HYAL1-antisense (HYAL1-AS), or vector DNA. HYAL1-AS transfectants were not generated for PC-3 ML because it expresses little HYAL1. HYAL1-S transfectants produced V42 milliunits (moderate overproducers) or z80 milliunits hyaluronidase activity (high producers). HYAL1-AS transfectants produced <10% hyaluronidase activity when compared with vector transfectants (18-24 milliunits). Both blocking HYAL1 expression and high HYAL1 production resulted in a 4-to 5-fold decrease in prostate cancer cell proliferation. HYAL1-AS transfectants had a G 2 -M block due to decreased cyclin B1, cdc25c, and cdc2/p34 expression and cdc2/p34 kinase activity. High HYAL1 producers had a 3-fold increase in apoptotic activity and mitochondrial depolarization when compared with vector transfectants and expressed activated proapoptotic protein WOX1. Blocking HYAL1 expression inhibited tumor growth by 4-to 7-fold, whereas high HYAL1 producing transfectants either did not form tumors (DU145) or grew 3.5-fold slower (PC-3 ML). Whereas vector and moderate HYAL1 producers generated muscle and blood vessel infiltrating tumors, HYAL1-AS tumors were benign and contained smaller capillaries. Specimens of high HYAL1 producers were 99% free of tumor cells. This study shows that, depending on the concentration, HYAL1 functions as a tumor promoter and as a suppressor and provides a basis for anti-hyaluronidase and high-hyaluronidase treatments for cancer. (Cancer Res 2005; 65(17): 7782-9)

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“…Hyaluronidase known as spreading factor results in membrane degradation of hyaluron lead to easy spreading of other toxic enzymes. The degradation of extracellular matrix is a continuous process and antivenom fails to neutralize the local tissue damages (Homma and Tu, 1970;Girish et al, 2004). Lethal toxicity and pharmacological activity is combined action of all these toxic enzymes.…”

Section: Discussionmentioning

confidence: 99%

In vitro neutralization of Eachis carinatus and Naja naja venom by Canthium parviflorum and its GC-MS analysis

Shrikanth

Janardhan

2016

Bangladesh J Pharmacol

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Canthium parviflorum is used in the traditional therapy to treat snakebite victims. In the present study, partially purified methanol root extract of C. parviflorum was used for the neutralization of Eachis carinatus and Naja naja venom. The extract inhibited in vitro phosphomonoesterase, phosphodiesterase, acetylcholinesterase, hyaluronidase, protease, phospholipase A2 and 5’nucleotidase activities of both venoms. One of the promising band exhibited neutralization of all the in vitro enzyme activities and was further subjected to GC-MS analysis which revealed the presence of eight active phytocompounds. These phytochemicals might be responsible for in vitro enzyme neutralization. Methanol extract possesses potent active phytochemicals against the site specific toxins and hydrolytic enzymes analyzed.Video Clip of Methodology:<a href="https://youtube.com/v/oSLdFcfaJxU">Phospholipase A2 assay</a>: 1 min 36 sec

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Isolation and characterization of hyaluronidase a “spreading factor” from Indian cobra (Naja naja) venom

Cited by 112 publications

References 32 publications

Enzymatic and toxinological activities of Hypnale hypnale (hump-nosed pit viper) venom and its fractionation by ion exchange high performance liquid chromatography

Enzymatic and toxinological activities of Hypnale hypnale (hump-nosed pit viper) venom and its fractionation by ion exchange high performance liquid chromatography

HYAL1 Hyaluronidase in Prostate Cancer: A Tumor Promoter and Suppressor

<i>In vitro</i> neutralization of <i>Eachis carinatus</i> and <i>Naja naja</i> venom by <i>Canthium parviflorum</i> and its GC-MS analysis

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