A previous study revealed that DNA-chitosan complex prepared from the reaction between native DNA and chitosan in aqueous solution has suitable porosity for cell seeding, is nontoxic, and causes only a mild soft-tissue response. This simple and easy fabrication method for porous DNA-chitosan complex provides for a wide variety of applications as a scaffold material. The present study evaluated whether rinsing with PBS solution can fabricate DNA-chitosan complex in a mold and the histopathological responses of rat soft tissues to fabricated DNA-chitosan complexes. DNA-chitosan complex paste was prepared by mixing distilled water and freeze-dried water-rinsed DNA-chitosan complex powder. A DNA-chitosan complex disk could be fabricated by rinsing with PBS buffer and subsequently freeze-drying the DNA-chitosan complex paste in the mold. Thus, a wide range of applications of DNA-chitosan complex for tissue engineering can be anticipated using the present easy fabrication method. The porosity of the disk was 85%, and many pores were visible in the DNA-chitosan complex (before fabrication) and in the fabricated DNA-chitosan disk. The values of the complex disks gradually reduced in the tissues although 60% of disks remained in the tissues. In conclusion, an easy fabrication method for making porous DNA-chitosan complex disks was developed. It was found that the fabrication method can delay the biodegradation of the DNA-chitosan complex disk without serious tissue responses in vivo. DNA-chitosan complex is promising as a scaffold material, and a wide range of applications of DNA-chitosan complex for tissue engineering are anticipated.

We have reported previously that the expression of CGR1 increased at an early stage of the yeast-mycelial transition (morphogenesis) in Candida albicans. We now show that Cgr1p interacts in a yeast two-hybrid system with the C. albicans Msi3p (CaMsi3p), a putative novel member of the heat shock protein 70 (HSP70) family. The DNA sequence of CaMSI3 encodes a predicted protein of 702 amino acids with a molecular mass of 78.6 kDa. The amino acid sequence of CaMsi3p is 63% identical to Msi3p/Sse1p of the HSP70 family of Saccharomyces cerevisiae. Further, CaMSI3 complemented the temperature-sensitive phenotype of the msi3 − mutant of S. cerevisiae. Other heat shock proteins of C. albicans are required for morphogenesis and are highly antigenic. These observations suggest that CaMSI3 may well provide functions for this organism unrelated to a heat shock function. The DDBJ Accession No. for the sequence reported in this paper is AB061274.

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By using real-time RT-PCR, we profiled the expression of CGR1, CaMSI3, EFG1, NRG1, and TUP1 in Candida albicans strains JCM9061 and CAI4 under several conditions, including induction of morphological transition, heat shock, and treatment with calcium inhibitors. Expression of CaMSI3 changed under these growth conditions except during heat shock. CGR1 expression increased during the early stages of hyphal growth in JCM9061, while expression was strain-dependent during heat shock. Both EFG1 and NRG1 were similarly expressed under hypha-inducing conditions and heat shock. Expression of TUP1 was slightly different from the expression of EFG1 or NRG1.

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