The quantitative studies of secretory granules andand lysosomes in gallbladder epithelium and gallbladder bile glycoprotein were performed in 20 gallstone patients and 15 gallstone-free subjects. The results showed that the number, the volume density and the total secrectory granules were significantly increased in gallstone patients compared with gallstone-free controls. The gallstone patients had a markedly reduced number,volume destiny and total lysosome area compared with gallstone-free subjects. The glycoprotein concenrtation in gallblader bile was increased up to 21.04±4.92g/L in gallstone paients,as compare with 13.02±5.72g/L(Plt;0.05)in the stone-free controls. The qualitity of secretory granules and lysosomes was directly proprtational to that of bile glycproteins. Evidence and secrectory granules and lysosomes was directly proporional to taht of bile glycoproteins. Evidence and argument are presentded suggesting that gallblader epithelium secrectory granules affect the concentration of bile glycoprotein and lysosomemay be related to the intracellular degradation of secretory granules.
Objective To prepare a new glycoproteinopticin specific antibody and to explore the distribution of opticin in human eye. Methods Firstly, take the opticin specific antibody to compound a synthetic peptide chain（CLPRLPIGRFT）, and then get the opticin antibody. To verify the availability of antibody through the western blot for human vitreous extract, to test the distribution of opticin in human eye by immunohistochemistry. Results Through the western blot for human vitreous extract, we can see a band with wild range at molecular weight 45times;103~50 times;103. We find that opticin exact in retina, vitreous and non-pigmented epithelium of ciliary body which distributes along the collagen fibrils in vitreous. Conclusion The availability of the antibody was confirmed by western blot. Opticin are mainly in retina, vitreous and nonpigmented epithelium of ciliary body. Opticin distributes along the collagen fibrils which may be related to the stability of vitreous. （Chin J Ocul Fundus Dis，2008，24：286-288）
In resting platelets, the 17th domain of filamin a (FLNa17) constitutively binds to the platelet membrane glycoprotein Ibα (GPIbα) at its cytoplasmic tail (GPIbα-CT) and inhibits the downstream signal activation, while the binding of ligand and blood shear force can activate platelets. To imitate the pull force transmitted from the extracellular ligand of GPIbα and the lateral tension from platelet cytoskeleton deformation, two pulling modes were applied on the GPIbα-CT/FLNa17 complex, and the molecular dynamics simulation method was used to explore the mechanical regulation on the affinity and mechanical stability of the complex. In this study, at first, nine pairs of key hydrogen bonds on the interface between GPIbα-CT and FLNa17 were identified, which was the basis for maintaining the complex structural stability. Secondly, it was found that these hydrogen bonding networks would be broken down and lead to the dissociation of FLNa17 from GPIbα-CT only under the axial pull force; but, under the lateral tension, the secondary structures at both terminals of FLNa17 would unfold to protect the interface of the GPIbα-CT/FLNa17 complex from mechanical damage. In the range of 0~40 pN, the increase of pull force promoted outward-rotation of the nitrogen atom of the 563rd phenylalanine (PHE563-N) at GPIbα-CT and the dissociation of the complex. This study for the first time revealed that the extracellular ligand-transmitted axial force could more effectively relieve the inhibition of FLNa17 on the downstream signal of GPIbα than pure mechanical tension at the atomic level, and would be useful for further understanding the platelet intracellular force-regulated signal pathway.