Experimental treatment of complications in alloxan diabetic rats with alpha-glucosidase inhibitor from the Chinese medicinal herb ramulus mori

Yao Xue Xue Bao. 2002 Feb;37(2):108-12.


Aim: To assess the effects of the alpha-glucosidase inhibitor Sangzhi (Ramulus mori, SZ) on the relief of diabetic symptoms of hyperglycemia and the prevention of its late complications in alloxan diabetic rats with high-calorie chow.

Methods: The aqueous extract of Sangzhi was given orally to alloxan diabetic rats for 15 days. The hyperglycemic symptoms were observed. The blood glucose, lipid levels and the nephrotic representations were measured.

Results: When alloxan diabetic rats on high-calorie chow were treated with SZ, the hyperglycemic symptoms were improved, the blood lipid levels were improved, the ratio of kidney over body weight and the blood N-acetyl-beta-D-glucosaminidase (NAG) activity were lowered. The degree of renal pathological changes was significantly reduced.

Conclusion: SZ may be useful for treating diabetes and its complications.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosaminidase / blood
  • Animals
  • Blood Glucose / metabolism
  • Diabetes Mellitus, Experimental / complications
  • Diabetes Mellitus, Experimental / drug therapy*
  • Diabetes Mellitus, Experimental / metabolism
  • Diabetic Nephropathies / etiology
  • Diabetic Nephropathies / metabolism
  • Diabetic Nephropathies / prevention & control*
  • Disease Models, Animal
  • Enzyme Inhibitors / therapeutic use
  • Glycoside Hydrolase Inhibitors*
  • Hypoglycemic Agents / isolation & purification
  • Hypoglycemic Agents / pharmacology
  • Hypoglycemic Agents / therapeutic use*
  • Kidney / pathology
  • Male
  • Morus / chemistry*
  • Plants, Medicinal / chemistry
  • Rats
  • Rats, Wistar
  • Triglycerides / blood
  • alpha-Glucosidases / isolation & purification


  • Blood Glucose
  • Enzyme Inhibitors
  • Glycoside Hydrolase Inhibitors
  • Hypoglycemic Agents
  • Triglycerides
  • alpha-Glucosidases
  • Acetylglucosaminidase