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Biomedical subjects

Q Q Zhuang

Publications and source records attributed to Q Q Zhuang.

7 recordsLinked to original sources
PubMed1995

Effect of colchicine on hepatic glycosaminoglycan metabolism in mice infected with Schistosoma japonicum.

AIM: To study the effect of colchicine on hepatic glycosaminoglycan (GAG) metabolism in mice infected with Schistosoma japonicum. METHODS: The amount of GAG was measured in the liver of mice infected with Schistosoma japonicum for 6-16 wk and treated with colchicine. RESULTS: Six weeks after infection, the GAG content of infected mice's livers and uninfected control was 14 +/- 2 micrograms/g liver and 4 +/- 1 microgram/g liver, respectively. The GAG content reached a peak about 6 times of the normal level in the 10th wk after infection, being 56 +/- 9 micrograms/g and 10 +/- 1 microgram/g for infected and uninfected mice respectively, and then declined. Treatment of infected mice with colchicine reduced the total GAG content to 22 +/- 3 micrograms/g liver, but not suppress the GAG content below the normal level in the 10th wk. Microscopic hepatic egg granuloma. CONCLUSION: Colchicine may exerts its GAG reduction effect through the suppression of granuloma formation.

Animals↗
PubMed1994

Platelet activation by platelet aggregation factor from Eisenia foelide.

A platelet activating factor from earthworm, Eisenia foelide (EPAF, 25.9 mumol.L-1), induced human platelet aggregation and 5-HT (maximal release of 89% at EPAF 74.1 mumol.L-1) was detected during this process. Neither creatine phosphate/creatine phosphate kinase (CP/CPK) nor aspirin completely inhibited the EPAF-induced platelet aggregation. In the presence of fibrinogen, EPAF (55.6 mumol.L-1) induced the aggregation of human platelet which had been thrombin-treated and degranulated. Results indicated that EPAF was a potent platelet agonist and the EPAF-induced platelet aggregation was ADP- and TXA2-independent.

Animals↗
PubMed1984

Role of actin binding protein phosphorylation in platelet cytoskeleton assembly.

Actin binding protein from human blood platelets is shown to exist in the resting platelet as a phosphorylated protein and contains two residues of phosphate per 260,000 kd. Removal of one-half of these residues with E. coli alkaline phosphatase results in the loss of its ability to crosslink F-actin into a low speed sedimentable complex (its cytoskeleton) and to bind to an F-actin affinity column. Thus, phosphorylation-dephosphorylation of ABP may be an important regulatory mechanism by which the platelet regulates its shape via its cytoskeletal structure.

Actins↗