Stress response of adherent cells on a polymer blend surface composed of a segmented polyurethane and MPC copolymers.
To better understand the effect of 2-methacryloyloxyethyl phosphorylcholine (MPC) copolymer in improving the biocompatibility of segmented polyurethane (SPU), the expression of heat shock protein (HSP) mRNA in HeLa S3 cells adhered on SPU blended with MPC copolymers was measured. Conventionally, MPC copolymers (PMEH) were synthesized by changing the feed ratios of MPC and 2-ethylhexyl methacrylate. X-ray photoelectron spectroscopic analysis of the SPU/PMEH film indicated that the surface concentration of MPC units on the SPU/PMEH film increased with an increase in PMEH composition. HeLa S3 cells were cultured on SPU/PMEH films. The number of adherent cells on the SPU/PMEH films decreased with an increase in the concentration of PMEH. When the PMEH composition was greater than 0.5 wt %, cell adhesion and proliferation decreased markedly. Expressions of HSP27 and HSP47 mRNA were detected using the reverse transcription-polymerase chain reaction (RT-PCR). After incubation for 24 h, both the HSP mRNA expressions in the HeLa S3 cells showed no significant differences among all samples. In HeLa S3 cells that adhered to the SPU film for 48 h, the expressions of HSP27 and HSP47 mRNA increased significantly when compared with those incubated for 24 h. In contrast, the two kinds of mRNA expressions decreased in the HeLa S3 cells that adhered to the SPU/PMEH films for 48 h. From these results, we concluded that PMEH was quite important in suppressing the stress response of adherent HeLa S3 cells. Therefore, SPU/PMEH blend polymers are useful as implantable biomedical materials.
Sawada
Shin-Ichi
S
Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University, 2-3-10 Kanda-surugadai, Chiyoda-ku, Tokyo 101-0062, Japan.
Iwasaki
Yasuhiko
Y
Nakabayashi
Nobuo
N
Ishihara
Kazuhiko
K
D000327:Adsorption; D002448:Cell Adhesion / Q000187:drug effects; D002460:Cell Line; D005353:Fibronectins / Q000737:chemistry; D055551:HSP27 Heat-Shock Proteins; D050958:HSP47 Heat-Shock Proteins / Q000235:genetics; D006360:Heat-Shock Proteins / Q000235:genetics; D006801:Humans; D008855:Microscopy, Electron, Scanning; D018832:Molecular Chaperones; D015394:Molecular Structure; D009363:Neoplasm Proteins / Q000235:genetics; D010767:Phosphorylcholine / Q000737:chemistry* / Q000494:pharmacology*; D011140:Polyurethanes / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology*; D012333:RNA, Messenger / Q000235:genetics; D014158:Transcription, Genetic / Q000235:genetics
D005353:Fibronectins; D055551:HSP27 Heat-Shock Proteins; D050958:HSP47 Heat-Shock Proteins; C057725:HSPB1 protein, human; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D009363:Neoplasm Proteins; D011140:Polyurethanes; D012333:RNA, Messenger; C494660:SERPINH1 protein, human; D010767:Phosphorylcholine