Anti-HIV and anti-tumor activities of recombinant MAP30 from bitter melon

Lee‐Huang, Sylvia; Huang, Paul L.; Chen, Hao-Chia; Huang, Peng; Bourinbaiar, Aldar S.; Huang, Hong; Kung, Hsiang‐Fu

doi:10.1016/0378-1119(95)00186-a

Cited by 149 publications

(108 citation statements)

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“…At maturity, the fruit splits into three irregular valves that curl backwards and release numerous reddish-brown seeds. Biological actions of various extracts of the plants or its constituents include antidiabetic (Ahmed et al, 1998;Mastuda et al, 1999;Raza et al, 2000), anti ulcerogenic (Gürbüz et al, 2000), antimutagenic (Guevara et al, 1990), antioxidant (Scartezzini & Speroni, 2000), anti-tumour (Lee-Huang et al, 1995a), immunomodulatory (Spreafico et al, 1983). Two proteins known as α -and β -monorcharin which are present in the seeds, fruits and leaves have shown to inhibit the human immune deficiency virus (HIV) in vitro (Zhang, 1992;LeeHuang et al, 1995b).…”

Section: Introductionmentioning

confidence: 99%

Toxicological studies of Momordica charantia Linn Seed extracts in Male Mice

Patil

2011

Int. J. Morphol.

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Section: Introductionmentioning

confidence: 99%

Toxicological studies of Momordica charantia Linn Seed extracts in Male Mice

Patil

2011

Int. J. Morphol.

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“…Several medicinal properties of the bitter gourd have been studied by various researchers that include anti-diabetic [22][23][24], anti-ulcerogenic [25], anti-mutagenic [26], antioxidative [27], anti-tumour [28], immune-modulatory acivities [29] etc. In vitro studies reveals that the bitter gourd proteins (α -and β-monorcharin) have inhibitory effect against human immune deficiency virus (HIV).…”

Section: Pharmacological and Medicinal Usesmentioning

confidence: 99%

Nutritional, Pharmacological and Medicinal Properties of Momordica Charantia

Kumar¹,

Nallamuthu²

2015

IJNFS

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Abstract:Momordica charantia L. (Bitter gourd) is a flowering vine in the family of Cucurbitaceae. It contains an array of novel and biologically active phytochemicals including triterpenes, proteins and steroids. Medicinally, the plant has a long history of use by the indigenous people as a folk medicine. Bitter gourd is often used in Chinese cooking for its bitter flavor, typically in stir-fries, soups, and also as tea. Pakistan, Philippines, Panama and Nepal also use this bitter vegetable for culinary purposes in addition to India. Several medicinal properties of the bitter gourd have been studied by various researchers, such as anti-diabetic, anti-ulcerogenic, anti-mutagenic, antioxidant, anti-tumour, anti-lipolytic, analgesic, abortifacient, anti-viral, hypoglycemic and immunomodulatory. In vitro studies reveals that the bitter gourd proteins (α-and β-monorcharin) have inhibitory effect against HIV virus, and leaf extracts have broad-spectrum anti-microbial activity as well. Many in vivo studies have demonstrated the relatively low toxicity of all parts of the bitter gourd plant when ingested orally. This review also addresses taxonomy, phytochemical, culinary practices and pharmacological properties in detail. Over the years scientists have verified many of the traditional uses of this bitter plant that continues to be an important natural remedy in herbal medicine systems. Bitter gourd products such as concentrated fruit and seed extracts can be found in capsules and tablets, as well as in whole herb/vine powder forms and these supplements are becoming more widely available in many countries nowadays as prophylactic or therapeutic agents.

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“…The RNase and non-specific depurination activities were found to be highest at low, non-physiological pH, suggesting that they are unlikely to be biologically significant. The DNase activity is, however, high at pH 7.5, and has been proposed as an alternative, physiologically relevant mechanism of cytotoxicity [9], with implications for various antiviral strategies [12,13]. Here, we present a detailed investigation into the putative DNase activity of RIPs.…”

mentioning

confidence: 96%

“…Stirpe and co-workers [5] suggested that the DNase activity associated with RIPs could be due to non-specific depurination of DNA and subsequent hydrolysis by a contaminating nuclease [5]. In contrast, Lee-Huang and others believe this activity to be an intrinsic property of all RIPs [10,13,15].DNase activity was once assigned to diphtheria toxin from Corynebacterium diphtheriae [16,17]. Again, this activity had low specific activity when compared with bone fide DNase I.…”

mentioning

confidence: 99%

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The deoxyribonuclease activity attributed to ribosome‐inactivating proteins is due to contamination

Day

Lord

Roberts

1998

European Journal of Biochemistry

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The mode of action of ribosome-inactivating proteins (RIPs) has, for many years, been considered to be depurination of a specific adenyl residue of ribosomal RNA, resulting in inhibition of protein synthesis. Recently, this view has been challenged by the observation that many RIP preparations have significant DNase activity in addition to their N-glycosidase activity. In this study, we have investigated the putative DNase activity of two RIPs, ricin and pokeweed antiviral protein (PAP), and show that, in both cases, the DNase activity is due to the presence of contaminating nucleases. The N-glycosidase and DNase activities of PAP were separately and specifically inactivated by chemical modification and heat. Gel filtration of ricin allowed physical separation of the two activities. Furthermore, neither recombinant PAP nor recombinant ricin A-chain purified from Escherichia coli displayed DNase activity.Keywords : deoxyribonuclease; ribosome-inactivating protein; RNA N-glycosidase.Ribosome-inactivating proteins (RIPs) are a group of structurally related proteins which depurinate a specific adenyl residue of 28-S ribosomal RNA (A4324 in rat, [1]). Depurination of this residue prevents binding of elongation factors, thereby inhibiting protein synthesis and resulting in cell death. RIPs can be divided into two classes: type I, which consist of a single subunit possessing RNA N-glycosidase activity, and type II, which have a type I-like catalytic subunit (A chain) linked to a cell-binding subunit (B chain). The B chains of plant toxins, e.g. ricin, are typically galactose/N-acetylgalactosamine-specific lectins and are linked to the A chain via a disulphide bond. Bacterial toxins that catalyse the same depurination reaction as RIPs, e.g. Shiga toxin, have a non-covalently bound glycolipidbinding B-chain pentamer.Most type-II RIPs are potent cytotoxins due to their ability to bind to and enter mammalian cells. Once inside the cell, the toxins exploit the cellular retrograde transport system to reach the endoplasmic reticulum from where they translocate into the cytosol by an as yet undetermined mechanism [2]. As holotoxins show no catalytic activity against ribosomes, separation of the A chain and B chain following intoxication is essential in order to exhibit a toxic effect.Type-I RIPs are, by comparison, only weakly cytotoxic when added exogenously to cells. A number of roles have been proposed for type-I RIPs, including defence mechanisms and promotion of senescence. Those which are active on con-specific ribosomes are typically stored in non-cytosolic compartments or as inactive precursors. Such RIPs are believed to be released into the cytosol following cellular damage, such as that caused by viral infection, resulting in local cell suicide around infected areas. An antifungal role has been proposed for RIPs that are inactive against con-specific ribosomes. Barley RIP is co-expressed with a chitinase, and [1, 3] β glucanase, which, while having intrinsic antifungal activity themselves, also facilitate RIP entry i...

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Anti-HIV and anti-tumor activities of recombinant MAP30 from bitter melon

Cited by 149 publications

References 14 publications

Toxicological studies of Momordica charantia Linn Seed extracts in Male Mice

Toxicological studies of Momordica charantia Linn Seed extracts in Male Mice

Nutritional, Pharmacological and Medicinal Properties of Momordica Charantia

The deoxyribonuclease activity attributed to ribosome‐inactivating proteins is due to contamination

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