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Anti-Hyperglycemic Property Of Medicinal Plants
Published in Amit Baran Sharangi, K. V. Peter, Medicinal Plants, 2023
Karanpreet Singh Bhatia, Arpita Roy, Navneeta Bhardavaj
Terminalia chebula, with a common name hirda belongs to Combretaceae family. It is indigenous to South Asia (India and Nepal), southwest China, Sri Lanka, Vietnam, and Malaysia. In one study Terminalia fruit was used and observed that 80% ethanolic extract was more effective against maltase activity than 50 and 100% ethanol extract. The active constituent found in these extracts was chebulagic acid and it was later observed that the chebulagic acid was responsible for downregulation of maltase activity and when orally given to maltose-loaded Sprague-Dawley rats, it resulted in lowering of postprandial blood glucose by 11.1% (Huang et al., 2012). In another study, methanolic extract of T. chebula leaves was investigated for anti-hyperglycemic effect in vitro as well as in vivo. It was found that crude extract showed 100% inhibition of alpha glucosidase and when given orally to diabetic rats, resulted in an appreciable decrease in postprandial hyperglycemia as compared to acarbose (standard drug used for diabetes treatment) (Dutta et al., 2018).
Therapeutic Potential of Anthocyanin Against Diabetes
Published in Hafiz Ansar Rasul Suleria, Megh R. Goyal, Health Benefits of Secondary Phytocompounds from Plant and Marine Sources, 2021
Tawheed Amin, H. R. Naik, Bazila Naseer, Syed Zameer Hussain
Digestion of carbohydrates inside our body occurs in a successive way with α-amylase acting initially on starch trailed by α-glucosidase to produce dietary glucose. Once the food is ingested, starch is acted upon by α-amylases (both salivary and pancreatic) and four small intestinal mucosal α-glucosidase subunits [57], and at an inner α-1,4 glucosidic linkages via an endo mechanism thereby producing linear and branched maltooligosaccharides [55]. Maltase-glucoamylase and sucrose-isomaltase (the two membrane-bound protein complexes), and mucosal α-glucosidases are exo-type starch hydrolyzing enzymes [65, 68] that produce glucose by hydrolyzingα-1,4 glucosidic linkages opposite to the reducing end of dextrins already degraded by α-amylase [6, 27, 29]. Apart from illustrious maltase activity, the C-terminal subunit (maltase-glucoamylase) is named as isomaltase because of its action on long-chain oligomers [54] whereas the N-terminal subunit (sucrose isomaltase) is named as isomaltase because of its debranching activity [28].
Muscle Disorders
Published in Philip B. Gorelick, Fernando D. Testai, Graeme J. Hankey, Joanna M. Wardlaw, Hankey's Clinical Neurology, 2020
Kourosh Rezania, Peter Pytel, Betty Soliven
The diagnosis of facial weakness in the patient or in family members is very helpful. A number of conditions may present with scapuloperoneal weakness: EMD (typically associated with contractures).Dysferlin deficiency.Reducing body myopathy.Hyaline body myopathy.Acid maltase deficiency.Mitochondrial disease.Inflammatory myopathy.Scapuloperoneal syndrome.
Subcutaneous immunoglobulin 16.5% for the treatment of pediatric patients with primary antibody immunodeficiency
Published in Expert Review of Clinical Immunology, 2023
Sudhir Gupta, Roger H. Kobayashi, Jiří Litzman, Laurel Cherwin, Sonja Hoeller, Huub Kreuwel
The excipient maltose is used as the stabilizer for SCIG 16.5% at a target concentration of 7.4% to achieve osmolality and assure IgG stability [57]. Maltose is a water-soluble disaccharide. Unlike sucrose, maltose is metabolized by kidney cells [71–73]. The SCIG and IVIG products stabilized with maltose are well tolerated [74]. This is believed to occur as because maltase, the enzyme responsible for catalyzing the hydrolysis of the disaccharide maltose to glucose, is present in the brush border of proximal convoluted renal tubules [74]. Nonclinical research has demonstrated that maltose is mostly metabolized with <5% excreted unchanged, unlike sucrose in which >60% may be excreted unchanged in the urine [75]. The conversion of maltose to glucose occurs intracellularly in the kidney; thus, maltose does not increase glucose levels in the blood, even in diabetic patients [76]. Falsely elevated blood glucose readings may occur during and after the infusion of SCIG 16.5% stabilized with maltose with some glucometer and test strip systems. When administering SCIG 16.5%, measure blood glucose with a glucose-specific method.
Effects of chronic cadmium exposure on the structure and function of intestinal mucosal flora in mice
Published in Toxin Reviews, 2022
Xiaoya Li, Yi Wu, Guozhen Xie, Zhoujin Tan
In addition, we detected the intestinal mucosal microbial activity in mice. Compared with the Zcm group, intestinal mucosal microbial activity in the Cddm and Cdzm group showed a decreased trend, as well as in the Cdgm group increased significantly. These results manifested that Cd exposure affected intestinal mucosal microbial metabolism in mice, and the ability of different doses of Cd to decompose substances was different, which might be related to the changes of intestinal flora structure and function in mice with different doses of Cd intervention. Among them, Cdgm group might have a relatively rich intestinal microbiota, which had a strong ability to decompose substances in the intestinal mucosa. In this regard, we further analyzed the possible factors causing the higher activity of intestinal mucosa microorganisms in Cdgm mice. The study confirmed that the increase of Bacteroidetes/Firmicutes in the intestine could reflect the ability of the body to absorb nutrients better, and the higher Bacteroidetes/Firmicutes value was related to the increase of invertase and maltase activities in the intestine (Cui 2013, Diao 2016). In our experiment, the Bacteroidetes/Firmicutes value of the intestinal mucosal flora of Cdgm group was the highest compared with other dose groups, which was consistent with the above-mentioned findings. From this, we speculated that the higher microbial activity of the intestinal mucosa of Cdgm group might be related to the increase of Bacteroidetes/Firmicutes in the intestinal mucosal flora.
Adult polyglucosan body disease: an acute presentation leading to unmasking of this rare disorder
Published in Hospital Practice, 2022
Jaspreet Johal, Ramiro Castro Apolo, Michael W. Johnson, Michael R. Persch, Adam Edwards, Preet Varade, Hussam Yacoub
Early diagnosis of APBD may be essential for the design and efficacy of future therapeutic trials. Repletion of the defective lysosomal acid maltase has been proposed as a treatment for GSD-II, or Pompe disease. Since GBE activity associated with APBD is characterized by a late-onset, a therapeutic time window during which treatment can be offered has been proposed [30]. Enhancement of glycogen branching activity and cessation of the accumulation of polyglucosan has been proposed as a potential treatment strategy. Inhibition of the glycogen synthase (GYS) activity, which would alter the GYS/GBE activity ratio and halt glycogen synthesis and polyglucosan buildup [31,32], is an alternative strategy. Guaiacol, an inhibitor of GYS, constitutes a promising candidate for future therapy as preliminary studies in animal models with APBD showed reduced accumulation of polyglucosans and GBE activity in cardiac, liver, and peripheral nerve tissues with no reported adverse effects [30]. Kakhlon and colleagues reported a similar outcome using rapamycin and starvation to promote decreased activity of GYS [32]. There is also limited evidence that anaplerotic dietary therapy with triheptanoin may slow disease progression. Limited functional improvement was observed in a small number of affected individuals in the early stages of the disease, whereas other studies report no benefit [33,34]. In a randomized, placebo-controlled trial, triheptanoin supplementation failed to prevent disease progression in 23 patients [4], similar to findings reported recently in two siblings diagnosed with APBD [34].