Institute of Medical Sciences, Banaras Hindu University

About: Institute of Medical Sciences, Banaras Hindu University is a education organization based out in Varanasi, India. It is known for research contribution in the topics: Population & Visceral leishmaniasis. The organization has 3622 authors who have published 4579 publications receiving 84718 citations.

Detail microscopic analysis of deep fascia of lower limb and its surgical implication.

Abstract: Background: The knowledge regarding the structural details of deep fascia remains inadequate. It was described to be relatively avascular having predominantly protective function. Anatomical and surgical studies revealed that it had associated vascular arcade and hence incorporated it to ascertain additional vascularity to the flaps. However, not much importance has been directed towards the detailed study of the various constituents of deep fascia in order to explain its physiological and clinical implications. Therefore, this study was undertaken to unveil these details. Materials and Methods: Fifty fresh specimens of human deep fascia overlying the gastrocnemius muscle were analyzed regarding the (i) vasculature, (ii) matrix, and (iii) other structural elements. The deep fascia was procured in three forms; (a) both the layers, (b) superficial layer, and (c) deep layer. Detail study was conducted by light, confocal, and electron microscopy. Results: Under light microscopy, blood vessels including capillaries were seen associated with both the layers. Perforators traversing the intra-fascial plane could be visualized. Confocal microscope optical sections showed well-organized bright fluorescent collagen fibers and nuclei of various cells. Electron microscopic evaluation revealed many interesting constituents which are relatively unknown to the anatomist and clinicians. There were arterioles, capillaries, venules, lymphatics, nerves, mast cells, and myofibroblasts apart from collagen and elastic fibers. Conclusion: The detail structural analysis of deep fascia provided the clue to its rich vascularity and other structural constituents. They all contribute to enhance the vascularity and maintenance of the physiological functions of fasciocutaneous, adipofascial, and fascial flaps, frequently used for reconstructions. Thus, incorporation of deep fascia in the flaps during reconstruction is highly beneficial for ensuring optimal vascularity.

Anxiolytic activity of ginkgolic acid conjugates from Indian Ginkgo biloba.

Abstract: Ginkgolic acid conjugates (GAC) (6-alkylsalicylates, namely n-tridecyl-, n-pentadecyl-, n-heptadecyl-, n-pentadecenyl- and n-heptadecenylsalicylates) isolated from the leaves of Indian Ginkgo biloba Linn., (IGb) were tested for their putative role in anxiety in rats. Elevated plus maze, open-field behaviour, novelty-induced feeding latency and social interaction were the rodent behavioural models used in this study. GAC (0.3 and 0.6 mg/kg, each, p.o.) on single acute administration, showed dose-related changes in the behaviour. GAC (0.6 mg/kg) and DZ augmented open arm entries, the open arm/closed arm entries ratio and increased time spent in the open arm on the elevated plus maze. In the open field, GAC (0.6 mg/kg) and DZ significantly increased ambulation and reduced the immobility time. EGb 761 showed a similar profile. GAC (0.6 mg/kg) and DZ significantly attenuated the increased latency to feed in novel environment. By contrast, EGb 761 and Ginkocer further augmented feeding latency. None of the drugs tested showed any significant effect in the social interaction test. GAC showed consistent and significant anxiolytic activity in all the variables investigated. By contrast, EGb 761 and Ginkocer, which are devoid of GAC, did not evoke significant activity. However, increased rearing and decreased immobility time only in open field behaviour shown by EGb 761 may be due to some antianxiety activity of a lesser degree. Our observations suggest that GAC may be the active constituents of Ginkgo biloba responsible for the anxiolytic activity.

Single-Dose Indigenous Liposomal Amphotericin B in the Treatment of Indian Visceral Leishmaniasis: A Phase 2 Study

Abstract: Liposomal amphotericin B is an effective and safe alternative for the treatment of visceral leishmaniasis in the Indian subcontinent. In this study, we used a higher-dose regimen of an indigenously manufactured liposomal amphotericin B (FUNGISOME; L-AmBL), which was intended to improve the efficacy in terms of long-lasting cure rate. Thirty men and thirty women between 12 and 60 years old with parasitologically confirmed visceral leishmaniasis were enrolled in two cohorts of 15 patients each. Subjects in cohort I were administered one dose (10 mg/kg body weight) of L-AmBL intravenously. After the safety at this dose was confirmed in cohort I, patients were recruited in cohort II. They received one infusion of an escalated dose (15 mg/kg body weight). The safety of these two doses was evaluated over a period of 30 days, and efficacy was assessed for initial cure at day 30 and definitive cure at 6 months. FUNGISOME was found to be safe, with an initial cure rate of 100% at day 30 and a definitive cure rate of 93.3% at the 6-month follow-up in both the cohorts.

Purification and biochemical characterization of a highly active cysteine protease ervatamin A from the latex of Ervatamia coronaria.

Abstract: Ervatamia coronaria, a flowering plant (family Apocynaceae) indigenous to India, has medicinally important applications. A search for biochemical constituents of the latex of the plant yielded at least three thiol proteases with distinctly different properties. One of them, a highly active protease (ervatamin A), was purified to homogeneity by ion exchange and gel filtration chromatography. The enzyme exhibited high proteolytic activity toward natural substrates and amidolytic activity toward synthetic substrates. The pH and temperature optima for proteolytic activity were 8–8.5 and 50–55°C, respectively. Proteolytic activity of the enzyme was strongly inhibited by thiol-specific inhibitors. The estimated molecular mass of the enzyme was 27.6 kDa. The extinction coefficient (e1% 280) of the enzyme was estimated as 21.9, and the protein molecule consists of 8 tryptophan, 11 tyrosine and 7 cysteine residues. Isoelectric point of the purified enzyme was 8.37. Polyclonal antibodies raised against the pure enzyme gave a single precipitin line in Ouchterlony's double immunodiffusion and a typical color in ELISA. The N-terminal sequence of the enzyme showed conserved amino acid residues to other plant cysteine proteases. Ervatamin A shows high activity in relation to the other thiol proteases isolated from the same source.