acid-phosphatase and pimagedine

Diabetes causes impairment of various enzyme activities in the physiological system, including lysosomal enzymes. The effect of feeding curcumin, quercetin and aminoguanidine on lysosomal enzyme activities viz., N-acetyl-β-d-glucosaminidase, β-d-glucuronidase, β-d-galactosidase and acid phosphatase were studied in different tissues of streptozotocin-induced diabetic rats.. Rats were divided into four control groups and four diabetic groups. Experimental groups were fed with diet supplemented with curcumin (0.5%) or quercetin (0.1%) or aminoguanidine (0.05%). Lysosomal enzyme activities were determined in various tissues.. The specific activity of N-acetyl-β-d-glucosaminidase in liver of diabetic rats was decreased when compared to control rats and was ameliorated with curcumin and quercetin treatment by 67% and 78%, respectively. On the other hand, β-d-glucuronidase activity was higher in the brain of diabetic rats (0.90 ± 0.04 nmol/mg protein/min), when compared to control rats (0.45 ± 0.02 nmol/mg protein/min) and was decreased in curcumin (0.75 ± 0.05 nmol/mg protein/min) and quercetin (0.74 ± 0.11 nmol/mg protein/min) treated rats. β-d-galactosidase activity in spleen of curcumin and quercetin fed diabetic group rats was ameliorated by 68% and 58%, respectively, in comparison to diabetic rats. Acid phosphatase activity in diabetic rats decreased in testis when compared to control.. Curcumin and quercetin feeding modulated lysosomal enzyme activities in different tissues during diabetes and the effect was comparable to well-known anti-glycative agent - aminoguanidine.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; beta-Galactosidase; Blood Glucose; Curcumin; Diabetes Mellitus, Experimental; Enzyme Inhibitors; Fasting; Glucuronidase; Guanidines; Liver; Male; Quercetin; Rats; Rats, Wistar; Spleen

High nitric oxide (NO) levels inhibit osteoclast (OC)-mediated bone resorption in vivo and in vitro, and nitrate donors protect against estrogen-deficient bone loss in postmenopausal women. Conversely, decreased NO production potentiates OC bone resorption in vitro and is associated with in vivo bone loss in rats and humans. Previously, we reported that bone sections from rats administered aminoguanidine (AG), a selective inhibitor of NO production via inducible NO synthase, exhibited both increased OC resorptive activity as well as greater numbers of OC. Here, we investigated further whether AG promoted osteoclastogenesis, in addition to stimulating mature OC function, using a modified in vivo chick chorioallantoic membrane (CAM) system and an in vitro chick bone marrow OC-like cell developmental model. AG, focally administered in small agarose plugs placed directly adjacent to a bone chip implanted on the CAM, dose-dependently elicited neoangiogenesis while stimulating the number, size, and bone pit resorptive activity of individual OC ectopically formed in vivo. In addition to enhancing OC precursor recruitment via neoangiogenesis, AG also exerted other vascular-independent effects on osteoclastogenesis. Thus, AG promoted the in vitro fusion and formation from bone marrow precursor cells of larger OC-like cells that contained more nuclei per cell and exhibited multiple OC differentiation markers. AG stimulated development was inversely correlated with declining medium nitrite levels. In contrast, three different NO donors each dose-dependently inhibited in vitro OC-like cell development while raising medium nitrite levels. Therefore, NO sensitively regulates OC-mediated bone resorption through affecting OC recruitment (angiogenesis), formation (fusion and differentiation), and bone resorptive activity in vitro and in vivo. Possibly, the stimulation of neoangiogenesis and OC-mediated bone remodeling via AG or other pro-angiogenic agents may find clinical applications in reconstructive surgery, fracture repair, or the treatment of avascular necrosis.

Topics: Acid Phosphatase; Allantois; Animals; Biomarkers; Bone and Bones; Bone Marrow Cells; Bone Resorption; Cell Differentiation; Cells, Cultured; Chick Embryo; Chorion; Coculture Techniques; Enzyme Inhibitors; Guanidines; Isoenzymes; Neovascularization, Physiologic; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Nitrites; Osteoclasts; Phenotype; Tartrate-Resistant Acid Phosphatase