The technologies that we call cell micropatterning allow the control of the shape and size of cell adhesion. Combination of micro/nano technology, surface chemistry, electrochemistry and photochemistry enables us to control the adhesion, migration, differentiation of cells and the interactions between different types of cells. These methodologies bring about a new platform for the studies of cell biology. A number of techniques for cell patterning and compares their advantages and disadvantages were reviewed in this article. The applications of cell micropatterning, including those for fundamental studies in cell biology, tissue engineering and cell-based biosensors were also discussed.

Purpose To investigate the influence of paraquat on substantial nigra and doparine levels ofstriatum in C57BL mice. Methods 39 neonatal C57BL mice were randomly divided into 5 groups andwere given paraquat or 1-methyl-4-phenyl-1,2,3,6-tetra-hydropyridine(MPTP) orally in 10 th and 11 thdays odl; ( 1 ) MPTP 0.3 mg/kg, n = 8; (2) MPTP 20 mg/kg, n = 8; (3) paraquat 0.07 mg/kg, n = 8; ( 4 )paraquat 0.36 mg/kg, n = 8; (5) normal saline, n = 7. Adult spontaneous motor activity was observed atages of 120 days, then the mice were decapitated and the contents of dopamine(DA), serotonin(5-HT), andtheir metabolites in striatum were analyzed. Meanwhile, the dopamine neuons at the mesencephalon vereobserved by the method of ABC immunohistochemistry. Results Mice given Paraquat 0.36 mg/kg andMPTP 20 rng/kg showed a marked bypoactive behavior and reduced the striatal contents of DA andmetabolites without affecting 5-HT. Immunohistochemical staining showed that the amount of dopamineneurons at the midbrain decreased. Conclusions C57BL mice exposed to great amount of paraquat duringthe neonatal period could yield the alterations of behavior and some pathological and biochemical changessimilar to parkinson disease.

The PCR product of PvpA gene was cloned into prokaryotic expression vector pET41a(+) and the recombinant expression vector was then transformed into E.coli DH5a after identified by restriction enzyme digestion and PCR.The positive recombinant plasmid was transformed into E.coli BL21 (D3) and induced to express PvpA protein.The obtained protein was analyzed by SDS-PAGE and Western blotting,purified by Ni-NTA affinity chromatography.The results showed that the purified PvpA fusion protein was obtained successfully.The expressed protein reacted to the high anti-PvpA immune serum from rabbit specially by western blotting.This study would be helpful to established a new diagnostic method for the detection of M.gallisepticum.