Myo-inositol has been established as an important growth-promoting factor of mammalian cells and animals. The role of myo-inositol as a lipotropic factor has been proven, in addition to its involvement as co-factors of enzymes and as messenger molecules in signal transduction. Myo-inositol deficiency leads to intestinal lipodystrophy in animals and “inositol-less death” in some fungi. Of late, diverse uses of myo-inositol and its derivatives have been discovered in medicinal research. These compounds are used in the treatment of a variety of ailments from diabetes to cancer, and continued research in this direction promises a new future in therapeutics. In different diseases, inositols implement different strategies for therapeutic actions such as tissue specific increase or decrease in inositol products, production of inositol phosphoglycans (IPGs), conversion of myo-inositol (MI) to D-chiro-inositol (DCI), modulation of signal transduction, regulation of reactive oxygen species (ROS) production, etc. Though inositol pharmacology is a relatively lesser-known field, recent years of research has generated a critical mass of information on the subject. This review aims to summarize our current understanding on the role of inositol derivatives in ameliorating the symptoms of different diseases.

No abstract

Background: Isaria tenuipes is one of the potent species in the members of the genus Isaria, which is well reported to possess multiple bioactive substances of therapeutic importance. Therefore, an in vitro experimental study was carried to evaluate the bioactivities of the crude methanolic extract from the mycelium of this fungus. Methods: The fungus was authenticated through morphological characters and the species discrepancy was resolved using the nuclear rDNA ITS sequence. The methanolic extract was fingerprinted by FTIR. The antioxidant components in terms of total phenols and flavonoids were determined as gallic acid and quercetin equivalents respectively. Antioxidant activities of the methanolic extract was assessed using 1, 1-diphenyl-2-picrylhydrazyl (DPPH), 2, 2 /-azinobis-(3-ethylbenzthiazoline-6-sulphonic acid) radical cation (ABTS 0+), Fe 2+ chelating activity, and hydroxyl radical scavenging assays. Cytotoxicity of the extract was determined by [3-(4, 5-dimethylthiazol-2-yl)-2, 5diphenyltetrazolium bromide] (MTT) assay on three cancer cell lines: HeLa, HepG2, and PC3. Apoptosis was further studied by propidium iodide (PI) and Annexin-V/PI staining flow cytometric analysis. Anti-proliferation capacity was studied by colony-forming assay.

Evident myo-inositol-1-phosphate phosphatase (MIPP) activity has been detected both in the vegetative as well as in the spore-bearing organs of some selected pteridophytes having wide phylogenetic diversity. The basic characterization of this enzyme was carried out using the cosmopolitan fern Dryopteris filix-mas. The enzyme was partially purified from the cytosol fraction obtained from the reproductive pinnules of the plant to about 41-fold over the initial homogenate following low-speed centrifugation, streptomycin sulfate precipitation, 25-70% ammonium sulfate fractionation, CM Sephadex C-50 chromatography and finally gel-filtration on Ultrogel AcA 34. The apparent molecular weight of the native MIPP was estimated to be 94 kDa. The enzyme activity increased linearly with respect to protein concentration to about 150 µg and with respect to time up to 75 min. The temperature optimum was found at 40ºC. However, the enzyme showed good activity over the temperature range of 30-50ºC. This enzyme used D/L-myo-inositol-1-phosphate as its principal substrate (95-100%), however, about 16% activity was recorded when D-myo-inositol-3-phosphate substituted as substrate. Furthermore, weak (3%) activity of this MIPP was observed with 2-glycerophosphate as substrate. The apparent K m for pteridophytic MIPP was 0.083 mM. The enzyme was functional in a narrow pH range of 7.5 to 8.5. The activity of this MIPP enzyme was remarkably inhibited by the presence of a monovalent cation, lithium, and even moderately so at a low concentration such as 1 mM. On the other hand, magnesium, a divalent cation, enhanced activity at least up to 10 mM. Calcium diminished MIPP activity at concentrations over 4 mM. Key words: Dryopteris filix-mas, myo-inositol-1-phosphate phosphatase, pteridophytes, reproductive pinnulesOcorrência da fosfatase do mio-inositol-1-fosfato em pteridófitas: características da enzima a partir de pínulas reprodutivas de Dryopteris filix-mas (L.) Schott: Tem-se detectado atividade da fosfatase do mio-inositol-1-fosfato (FMIF) tanto em órgãos vegetativos como em estruturas esporulantes de algumas pteridófitas com ampla diversidade filogenética. Neste estudo, procedeu-se à caracterização básica dessa enzima utilizando-se da pteridófita cosmopolita Dryopteris filix-mas. Após centrifugação em baixa velocidade, precipitação com sulfato de estreptomicina, fracionamento com sulfato de amônio (25-70%), cromatografia em CM Sephadex C-50 e, finalmente, filtração gélica em Ultrogel AcA 34, conseguiu-se uma purificação parcial da enzima (a partir da fração citossólica obtida de pínulas reprodutivas da planta) de cerca de 41 vezes em relação ao homogenato inicial. O peso molecular aparente da FMIF nativa foi estimado em 94 kDa. A atividade da enzima aumentou linearmente com relação ao conteúdo de proteína (cerca de 150 µg) e com relação ao tempo (até 75 min). A temperatura ótima foi de 40ºC. Entretanto, a enzima exibiu atividade razoável na faixa de temperatura entre 30 e 50ºC. O D/L-mio-inositol-1-fosfato foi o principal substrato (9...

Myo-inositol is involved in normal growth and development of all living organisms and L-myo-inositol-1-phosphate synthase (MIPS; EC: 5.5.1.4) is responsible for its de novo synthesis. This enzyme has been reported for a number of life forms including plants, animals and bacteria. In the present study free myo-inositol has been detected in the common pteridophytes found in the Darjeeling Himalayas and the enzyme, L-myo-inositol-1-phosphate synthase has been partially purified from Diplopterygium glaucum (Thunb.) Nakai. A crude homogenate from the reproductive pinnules of D. glaucum was subjected to streptomycin sulphate precipitation and 0-70% ammonium sulphate fractionation followed by successive chromatography through DEAEcellulose, Hexylagarose and BioGel A-0.5m columns. This resulted in a partial purification of the enzyme of about 81-fold with 13.5% recovery. The pteridophytic MIPS specifically utilized D-glucose-6-phosphte and NAD + as its substrate and co-factor, respectively. It shows a pH optimum between 7.0 and 7.5 while the temperature maximum was 30 °C. The enzyme activity was stimulated by NH 4 + , slightly inhibited by Na + , Ba 2+ and Cd 2+ , and strongly inhibited by Li + , Zn 2+ and Hg 2+ . EDTA, pCMB and some substrate isomers like glucose-1-phosphate, fructose-6-phosphte and galactose-6-phosphate were inhibitory to the enzyme. The apparent molecular weight of the native D. glaucum MIPS was determined to be approximately 171 kDa. Key words: D-glucose-6-phosphate, Gleicheniaceae, inositol synthase, myo-inositol. Conteúdo de myo-inositol em pteridófitas e o isolamento e caracterização da sintase de L-myo-inositol-1-fosfato de Diplopterygium glaucum:Myo-inositol está envolvido no crescimento e desenvolvimento de todos os organismos vivos e a enzima sintase do L-myo-inositol-1-fosfato (MIPS; EC: 5.5.1.4) é responsável pela sua síntese de novo. Esta enzima tem sido relatada em um número grande de plantas, animais e bactérias. No presente estudo myo-inositol não complexado foi detectado em pteridófitas comuns encontradas em Darjeeling Himalayas e a enzima sintase do L-myo-inositol-1-fosfato foi parcialmente purificada a partir de Diplopterygium glaucum (Thunb.) Nakai. Um extrato protéico não purificado de pinulas reprodutivas foi precipitada com sulfato de estreptomicina e 0-70% sulfato de amônia seguido de sucessivas cromatografias em colunas de DEAE-celulose, Hexylagarose e BioGel A. Este procedimento resultou na purificação parcial de 81 vezes, com recuperação de 13.5%. A MIPS dessa pteridófita usou especificamente D-glicose-6-fosfato and NAD + como substrato e cofator, respectivamente. Mostrou pH ótimo entre 7,0 e 7,5, enquanto a temperatura ótima foi 30°C. A atividade da enzima foi estimulada por NH 4 + , pouco inibida por Na + , Ba 2+ e Cd 2+ , e fortemente inibida por Li + , Zn 2+ e Hg 2+ . EDTA, pCMB e alguns substratos isôme-ros, como glicose-1-fosfato, frutose-6-fosfato e galactose-6-fosfato inibiram a enzima. A massa molecular aparente da MIPS de D. glaucum é aproximadamente 171 kDa. Palavr...

No abstract

Abstract. Lepcha DL, Pradhan A, Chhetri DJ. 2019. Population assessment and species distribution modeling of Paris polyphylla in Sikkim Himalaya, India. Biodiversitas 20: 1299-1305.  Paris polyphylla Smith is an important therapeutic plant that grows in the Indian Himalayan region. In Sikkim, the survival of the species is threatened by illegal extraction of its rhizome. Therefore, immediate conservation initiative is required to conserve the existing species population in the wild. Population assessment through field survey followed by ENM revealed a positive correlation between predicted suitable habitats with the actual sites of its occurrence, except in disturbed habitats. Precipitation of driest month (Bio14) and slope were the most influential factors that contributed 41.9 % and 30 % respectively to the MaxEnt model. Field survey revealed that the density of the plants varied between 0.45 (pl/m2) and 3.89 (pl/m2) and the frequency varied from 36% to 76%. The IVI for P. polyphylla ranged between 2.68 to 8.66 based on locations. On the other hand, the IVI of associated species varied from 3.57 to 18.14 based on species. P. polyphylla is a vulnerable plant in Sikkim Himalaya and it is facing an imminent threat of extinction. Under this situation, it is imperative that works on predictive modeling will help conserve the species. This study identified the potential habitats for P. polyphylla in the higher elevations of Sikkim Himalaya where it could be reintroduced.

L-myo-inositol-1-phosphate synthase (MIPS; EC: 5.5.1.4) catalyzes the conversion of D-glucose-6-phosphate to 1L-myo-inositol-1-phosphate, the rate limiting step in the biosynthesis of all inositol containing compounds. Myo-inositol and its derivatives are implicated in membrane biogenesis, cell signaling, salinity stress tolerance and a number of other metabolic reactions in different organisms. This enzyme has been reported from a number of bacteria, fungi, plants and animals. In the present study some bryophytes available in the Eastern Himalaya have been screened for free myo-inositol content. It is seen that Bryum coronatum, a bryopsid shows the highest content of free myo-inositol among the species screened. Subsequently , the enzyme MIPS has been partially purified to the tune of about 70 fold with approximately 18% recovery form the reproductive part bearing gametophytes of Lunularia cruciata. The L. cruciata synthase specifically utilized D-glucose-6-phosphate and NAD + as its substrate and co-factor respectively. The optimum pH shown was 7.0 while the temperature maximum was at 30˚C.