An exploration of physiological, medicinal and safety aspects of Guduchi (Tinospora cordifolia): A complete Ayurvedic and modern review

Introduction: Tinospora cordifolia commonly known as “Amrita” or “Guduchi” is an important drug of Indian systems of medicine (ISM) and used in medicines since times immemorial. Guduchi is a Sanskrit word which means that ‘which protects body from diseases’. Another name for this herb is ‘Amrita’, which refers to the heavenly elixir according to Hindu mythology. The drug is well known Indian bitter and prescribed in fevers, diabetes, dyspepsia, jaundice, urinary problems, skin diseases and chronic diarrhoea and dysentery. It has been also indicated useful in the treatment of heart diseases, leprosy, helminthiasis and rheumatoid arthritis. It is an important drug and is used in form of different preparations like Satva, Ghrita, Tail, Swarasa etc. Material & Methods: For this review article Charaka Samhita, Sushruta Samhita, Ashtanga Hridaya, Ashtanga Sangraha, Bhavprakash Nighantu, Raj Nighantu, Dhanvantari Nighantu, Shaligrama Nighantu, Priya Nighantu, Kaiydev Nighantu, Madanpal Nighantu, Shodhal Nighantu, internet and modern medical literature have been reviewed. Result: The Tinospora cordifolia plant had been appreciated to having high levels for medicinal, therapeutical, curative, healing and relieving nature. Discussion: Guduchi has high therapeutic potential by its anti-toxic, anti-inflammatory, anti-pyretic and anti-oxidant properties. There is also no evidence that Guduchi has any toxic content or side effects, which proves its safety aspect as well. Conclusion: The therapeutic and safety aspects studies reported in the present review confirm the medicinal properties of herb Tinospora cordifolia (Giloy) in preventing various diseases or abnormalities by increasing immunity naturally in human bodies

Patterns of Periodontal Destruction among Smokeless Tobacco Users in a Central Indian Population

Background: Findings of studies testing the association between smokeless tobacco (SLT) use and periodontal health have shown varying results in different populations. Considering the high prevalence of SLT use in India, the present study was conducted to understand the pattern of periodontal destruction within different areas of the dentition among SLT users. Methods: Age, gender, oral hygiene habits, the frequency and duration of SLT consumption, the type of SLT product used, and the site of retention of the SLT product in the oral cavity were recorded among 90 SLT users. Probing depth (PD), recession (REC), and clinical attachment loss (CAL) at SLT-associated and non SLT-associated teeth of the mandibular arch were compared based on the site of retention of the SLT product, the type of product used, and the duration of the habit. Results: REC and CAL were significantly higher at the SLT-associated zones compared to non SLT-associated zones and at both interproximal and mid-buccal sites of SLT-associated teeth. Among individuals who had the habit for more than 5 years and also among those who had the habit for 5–10 years, PD, REC, and CAL were significantly higher at SLT-associated teeth than at non SLT-associated teeth. Significantly greater periodontal destruction was observed at SLT-associated teeth among khaini users and gutkha users. Conclusions: Smokeless tobacco consumption resulted in greater destruction of periodontal tissues. The severity of periodontal destruction at SLT-associated sites differed depending on the type of smokeless tobacco used, the site of retention of the SLT, and the duration of the habit

Enzymatic activities of the human AGPAT isoform 3 and isoform 5: localization of AGPAT5 to mitochondria[S]

The enzyme 1-acylglycerol-3-phosphate-O-acyltransferase (AGPAT) converts lysophosphatidic acid (LPA) to phosphatidic acid (PA). In this study, we show enzymatic properties, tissue distribution, and subcellular localization of human AGPAT3 and AGPAT5. In cells overexpressing these isoforms, the proteins were detected in the nuclear envelope and the endoplasmic reticulum. AGPAT5-GFP fusion protein was localized in the mitochondria of both Chinese hamster ovary and human epithelial cervical cancer cells. Using lysates of AD293 cells infected with AGPAT3 and AGPAT5 recombinant adenovirus, we show that AGPAT3 and AGPAT5 proteins have AGPAT activity. Both the isoforms have similar apparent Vmax of 6.35 and 2.42 nmol/min/mg protein, respectively, for similar LPA. The difference between the two isoforms is in their use of additional lysophospholipids. AGPAT3 shows significant esterification of lysophosphatidylinositol (LPI) in the presence of C20:4 fatty acid, whereas AGPAT5 demonstrates significant acyltransferase activity toward lysophosphatidylethanolamine (LPE) in the presence of C18:1 fatty acid. The AGPAT3 mRNA is ubiquitously expressed in human tissues with several-fold differences in the expression pattern compared with the closely related AGPAT4. In summary, we show that in the presence of different fatty acids, AGPAT3 and AGPAT5 prefer different lysophospholipids as acyl acceptors. More importantly, localization of overexpressed AGPAT5 (this study) as well as GPAT1 and 2 (previous studies) in mitochondria supports the idea that the mitochondria might be capable of synthesizing some of their own glycerophospholipids