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Biomedical subjects

Mariko Hara

Publications and source records attributed to Mariko Hara.

At least 19 recordsLinked to original sources

A tris(2,2'-bipyridine)ruthenium(II) derivative tethered to a cis-PtCl2(amine)2 moiety: syntheses, spectroscopic properties, and visible-light-induced scission of DNA.

A tris(2,2'-bipyridine)ruthenium(II) derivative having two N-(3-ammoniopropyl)carbamoyl pendant units has been prepared and reacted with cis-PtCl2(DMSO)2 (DMSO = dimethyl sulfoxide) to give a heteronuclear Ru(II)Pt(II) dimer having a cis-Pt(II)Cl2(aliphatic amine)2 unit, [Ru(bpy)2(mu-bridge)PtCl2](PF6)2 (bpy = 2,2'-bipyridine, bridge = 4,4'-bis(N-(3-aminopropyl)carbamoyl)-2,2'-bipyridine). The ESI-TOF mass spectrum of the Ru(II)Pt(II) dimer shows a set of signals corresponding to {[Ru(bpy)2(mu-bridge)PtCl2](PF6)}(+) (m/z 1181.1). The MLCT (metal-to-ligand charge transfer) luminescence intensity is enhanced upon the platination of two amine units, presumably due to the formation of a relatively rigid metallocycle. More interestingly, the luminescence intensity is further enhanced by the complexation of the Ru(II)Pt(II) dimer with either 5'-GMP (guanosine 5'-monophosphate disodium salt) or calf thymus DNA. Visible-light-induced scission of supercoiled pBR322 DNA is found to be efficiently enhanced in the presence of the title Ru(II)Pt(II) dimer.

Antineoplastic Agents↗

Anti-obese action of raspberry ketone.

Raspberry ketone (4-(4-hydroxyphenyl) butan-2-one; RK) is a major aromatic compound of red raspberry (Rubus idaeus). The structure of RK is similar to the structures of capsaicin and synephrine, compounds known to exert anti-obese actions and alter the lipid metabolism. The present study was performed to clarify whether RK helps prevent obesity and activate lipid metabolism in rodents. To test the effect on obesity, our group designed the following in vivo experiments: 1) mice were fed a high-fat diet including 0.5, 1, or 2% of RK for 10 weeks; 2) mice were given a high-fat diet for 6 weeks and subsequently fed the same high-fat diet containing 1% RK for the next 5 weeks. RK prevented the high-fat-diet-induced elevations in body weight and the weights of the liver and visceral adipose tissues (epididymal, retroperitoneal, and mesenteric). RK also decreased these weights and hepatic triacylglycerol content after they had been increased by a high-fat diet. RK significantly increased norepinephrine-induced lipolysis associated with the translocation of hormone-sensitive lipase from the cytosol to lipid droplets in rat epididymal fat cells. In conclusion, RK prevents and improves obesity and fatty liver. These effects appear to stem from the action of RK in altering the lipid metabolism, or more specifically, in increasing norepinephrine-induced lipolysis in white adipocytes.

Adipose Tissue↗

Albumin and urea production by hepatocytes cultured on extracellular matrix proteins-conjugated poly(vinyl alcohol) membranes.

Production of albumin and urea by mouse hepatocytes on poly(vinylalcohol-co-ethylamine) (PVA-EA) membranes containing immobilized extracellular matrix (ECM) proteins was investigated for 7 days. The amount of ECM proteins (collagen, vitronectin and laminin) immobilized on PVA-EA and PVA-ECM membranes was determined to range from 1.09 microg/cm2 to 1.60 microg/cm2. Hepatocytes cultured on PVA-ECM membranes in serum-free media showed higher albumin production than those cultured on PVA-EA membranes after a 7-day incubation under the conditions in this study. Urea production by hepatocytes on PVA-ECM membranes was also determined to be higher than that on PVA-EA membranes up until day 5 of incubation in serum-free media, whereas no difference of urea production by hepatocytes on different PVA-ECM membranes and PVA-EA membranes was observed at 7 days of incubation. The effect of ECM proteins in PVA-ECM membranes on hepatocyte function (such as albumin and urea production) was observed in hepatocytes cultured in serum-free media up to day 5 of incubation. The ECM proteins immobilized on the PVA-ECM membranes contributed not only to the long-term stable production of albumin and urea by hepatocytes, but also the improved surviVal (viability) of hepatocytes on PVA-ECM membranes.

Albumins↗

Peripheral blood cell separation through surface-modified polyurethane membranes.

Cell separation from peripheral blood was investigated using surface-modified polyurethane (PU) membranes with different functional groups. Both red blood cells and platelets could pass through unmodified PU and PU-SO(3)H membranes, whereas the red blood cells preferentially passed through PU-N(C(2)H(5))(2) and PU-NHC(2)H(4)OH membranes. The permeation ratio of T and B cells was <25% for the surface-modified and unmodified PU membranes. CD34(+) cells have been recognized as various kinds of stem cells including hematopoietic and mesenchymal stem cells. The adhesiveness of CD34(+) cells on the PU membranes was found to be higher than that of red blood cells, platelets, T cells, or B cells. Overall, the adhesiveness of blood cells on the PU membranes increased in the following order: red blood cells </= platelets < T cells </= B cells < CD34(+) cells. Treatment of PU-COOH membranes with a human albumin solution to detach adhered blood cells, allowed recovery of mainly CD34(+) cells in the permeate, whereas both red blood cells and platelets could be isolated in the permeate using unmodified PU membranes. The PU membranes showed different permeation and recovery ratios of specific cells depending on the functional groups attached to the membranes.

Antigens, CD↗

Serum protein adsorption and platelet adhesion on aspartic-acid-immobilized polysulfone membranes.

Polysulfone (PSf) membranes that covalently conjugated with aspartic acid (ASP-PSf) were prepared and analyzed for hemocompatability. Compared to PSf or other types of surface-modified PSf membranes, the ASP-PSf membranes had a reduced ability to adsorb protein from either a plasma solution or a mixed solution of albumin, globulin and fibrinogen. This appears to be due to the creation of a hydrophilic surface by the aspartic acid zwitterion immobilized on the ASP-PSf membranes. Furthermore, the analyses of membrane protein adsorption showed that a mixed protein solution recapitulates the cooperative adsorption of proteins that occurs in plasma. We also found that the number of adhering platelets was the lowest on the ASP-PSf membranes and, in general, that platelet adhesion decreased in parallel with fibrinogen adsorption. In summary, aspartic acid immobilized on the ASP-PSf membranes, which have zwitterions with a net zero charge, effectively contributes to the hydrophilic and hemocompatible sites on the surface of the hydrophobic PSf membranes.

Adsorption↗

Production of interferon-beta by fibroblast cells on membranes prepared with RGD-containing peptides.

The production of interferon-beta by NB1-RGB fibroblast cells cultured on protein and peptide membranes prepared from silk fibroin, motif peptides of silk fibroin [(AG)(n)] containing arginine-glycine-aspartic acid (RGD) peptide, and Pronectin was investigated. The cell density on various protein and peptide membranes was approximately the same, although the production of interferon-beta depended significantly on the membranes where the cells were cultured. The highest production of interferon-beta was observed when the cells were cultured on (AG)(6)RGD(AG)(7) membranes prepared with hexafluoroacetone (HFA) as the casting solvent. On RGD-containing peptide membranes more centrally located in the peptides, the cells produced more interferon-beta when the peptide membranes were prepared with HFA as the casting solvent. However, there was no enhanced production of interferon-beta by cells on (AG)(6)RGD(AG)(7) membranes prepared with 9 mol/L LiBr or 4.5 mol/L LiClO(4) solution as the casting solvent. Therefore, both the chemical composition and the secondary and higher order structure of the peptide membranes are important for enhanced production of interferon-beta. The blocking of integrin beta(1) on the cells by anti-integrin beta(1) antibody prevented the enhanced production of interferon-beta on (AG)(6)RGD(AG)(7) membranes prepared with HFA. We suggest that the cells must bind to the RGD sequence having the appropriate conformation through their integrin beta(1) for enhanced production of interferon-beta.

Amino Acid Sequence↗

Glycerol replacement corrects defective skin hydration, elasticity, and barrier function in aquaporin-3-deficient mice.

Mice deficient in the epidermal water/glycerol transporter aquaporin-3 (AQP3) have reduced stratum corneum (SC) hydration and skin elasticity, and impaired barrier recovery after SC removal. SC glycerol content is reduced 3-fold in AQP3 null mice, whereas SC structure, protein/lipid composition, and ion/osmolyte content are not changed. We show here that glycerol replacement corrects each of the defects in AQP3 null mice. SC water content, measured by skin conductance and 3H2O accumulation, was 3-fold lower in AQP3 null vs. wild-type mice, but became similar after topical or systemic administration of glycerol in quantities that normalized SC glycerol content. SC water content was not corrected by glycerol-like osmolytes such as xylitol, erythritol, and propanediol. Orally administered glycerol fully corrected the reduced skin elasticity in AQP3 null mice as measured by the kinetics of skin displacement after suction, and the delayed barrier recovery as measured by transepidermal water loss after tape-stripping. Analysis of [14C]glycerol kinetics indicated reduced blood-to-SC transport of glycerol in AQP3 null mice, resulting in slowed lipid biosynthesis. These data provide functional evidence for a physiological role of glycerol transport by an aquaglyceroporin, and indicate that glycerol is a major determinant of SC water retention, and mechanical and biosynthetic functions. Our findings establish a scientific basis for the >200-yr-old empirical practice of including glycerol in cosmetic and medicinal skin formulations.

Administration, Oral↗

Design, synthesis, and evaluation of beta-galactosylceramide mimics promoting beta-glucocerebrosidase activity in keratinocytes.

We have established an efficient synthesis of mimics of beta-galactosylceramide (beta-GalCer) increasing a beta-glucocerebrosidase (beta-GlcCer'ase) activity that associates with the skin barrier function. Among the synthetic beta-GalCer analogues (6a-6e) described herein, compound 6e exhibited a potent effect on the activation of beta-GlcCer'ase function in vitro and reduced the transepidermal water loss (TEWL) level in a UVB-induced barrier disrupted mice model. These findings indicated that compound 6e could be useful for cosmetics and medicines to improve skin barrier function.

Animals↗

Serum protein adsorption and platelet adhesion on pluronic-adsorbed polysulfone membranes.

We examined plasma protein adsorption and platelet adhesion to polysulfone (PSf) flat membranes coated with Pluronic with varying polyethylene oxide (PEO) block length. Adsorption of albumin, globulin and fibrinogen to Pluronic-coated PSf membranes was independent of plasma dilution when concentrations of human blood plasma above 20% were applied. Increasing coating concentrations of aqueous Pluronic solution resulted in decreased protein adsorption by the PSf membranes. Pluronic F68, which was more hydrophilic than Pluronic L62 or L64 and had 80% of PEO content, was the most effective at suppressing the adsorption of plasma proteins and platelet adhesion to PSf membranes. We developed a mixed protein solution containing human albumin, gamma-globulin and fibrinogen to attempt to mimic the competitive and cooperative binding effects found in plasma. Fibrinogen adsorption from plasma could be recapitulated by the mixed protein solution. The number of platelets adhering to the PSf membranes decreased as the coating concentration of Pluronic solution was increased, and platelet adhesion decreased in parallel with fibrinogen adsorption. These results suggest that the bioinert property of PEO segments in the Pluronic, which is ascribed to their high flexibility in aqueous media, suppresses the adsorption of plasma proteins and platelets to the Pluronic-coated PSf membranes.

Adsorption↗

Enhanced production of carcinoembryonic antigen by CW-2 cells cultured on polymeric membranes immobilized with extracellular matrix proteins.

Cell growth and the production of carcinoembryonic antigen (CEA) were investigated in human colorectal adenocarcinoma tumor (CW-2) cells cultured on extracellular matrix (ECM) protein membranes, heat-treated poly(vinyl alcohol-co-ethylamine) (PVA-EA) membranes, and PVA-EA membranes containing immobilized ECM proteins. The highest concentration of CEA was found in the cell culture media of CW-2 cells on collagen (COL)-immobilized PVA-EA membranes. This is explained by the flexible mobility of COL on the COL-immobilized PVA-EA membranes causing a specific cell response for the production of CEA. An inverse relationship was observed between either the cell density or the CEA concentration in the cell culture media and the amount of fibronectin (FN) adsorbed on the COL-immobilized membranes. The CEA concentration in the cell culture media was directly related to the cell density, which, in turn, is inversely related to the amount of FN secreted by CW-2 cells. These findings indicate that cells tend to attach to the surface by secreting ECM proteins such as FN when they are grown on substrates that provide weak cell attachment.

Adenocarcinoma↗

Visible light is able to regulate neurite outgrowth.

The pheochromocytoma cell line PC12 displays neuronal characteristics. PC12 cells differentiate their phenotype from a proliferating cell to a neurite-bearing neuron upon treatment with nerve growth factor (NGF). The neurite outgrowth of PC12 cells on polystyrene tissue culture flasks and extracellular matrix protein-adsorbed glass plates was reversibly controlled using visible light. The percentage of cells with neurites decreased with increasing light intensity. Furthermore, neurite outgrowth was dramatically suppressed with light intensities over 300 Lux (approximately 130 microW). Neurite outgrowth occurred in the absence of irradiation by visible light, but did not occur or was limited with irradiation, depending on the membranes on which PC12 cells were cultured. These results hold promise for the creation of patterned neuronal networks corresponding to patterned irradiation of visible light on nerve cells.

Animals↗

Alteration of the 4-sphingenine scaffolds of ceramides in keratinocyte-specific Arnt-deficient mice affects skin barrier function.

Aryl hydrocarbon receptor nuclear translocator (ARNT), a transcription factor of the Per/AHR/ARNT/Sim family, regulates gene expression in response to environmental stimuli including xenobiotics and hypoxia. To examine its role in the epidermis, the Cre-loxP system was used to disrupt the Arnt gene in a keratinocyte-specific manner. Gene-targeted, newborn mice with almost normal appearance died neonatally of severe dehydration caused by water loss. Histology showed small changes in the architecture of cornified layers, with apparently preserved intercorneocyte lamellar structures responsible for the skin barrier function. In contrast, HPLC/ion-trap mass spectrometry revealed significant alterations in the compositions of ceramides, the major components of the lamellae. The murine epidermal ceramides normally contain 4-sphingenine and 4-hydroxysphinganine. In Arnt-null epidermis, 4-sphingenine was largely replaced by sphinganine and the amounts of ceramides with 4-hydroxysphinganine were greatly decreased, suggesting deficiency of dihydroceramide desaturases that catalyze the formation of both 4-sphingenyl and 4-hydroxysphinganyl moieties. A desaturase isoenzyme, DES-1, prefers desaturation, but DES-2 catalyzes both reactions to a similar extent. Transcript levels of Des-2, but not Des-1, were considerably decreased in cultured keratinocytes from Arnt-null epidermis. These results indicate that proper ceramide compositions through 4-desaturation regulated by ARNT are crucial for maintaining the epidermal barrier function.

Animals↗

Selectively reduced glycerol in skin of aquaporin-3-deficient mice may account for impaired skin hydration, elasticity, and barrier recovery.

Deletion of the epidermal water/glycerol transporter aquaporin-3 (AQP3) in mice reduced superficial skin conductance by approximately 2-fold (Ma, T., Hara, M., Sougrat, R., Verbavatz, J. M., and Verkman, A. S. (2002) J. Biol. Chem. 277, 17147-17153), suggesting defective stratum corneum (SC) hydration. Here, we demonstrate significant impairment of skin hydration, elasticity, barrier recovery, and wound healing in AQP3 null mice in a hairless (SKH1) genetic background and investigate the cause of the functional defects by analysis of SC morphology and composition. Utilizing a novel (3)H(2)O distribution method, SC water content was reduced by approximately 50% in AQP3 null mice. Skin elasticity measured by cutometry was significantly reduced in AQP3 null mice with approximately 50% reductions in elasticity parameters Uf, Ue, and Ur. Although basal skin barrier function was not impaired, AQP3 deletion produced an approximately 2-fold delay in recovery of barrier function as measured by transepidermal water loss after tape stripping. Another biosynthetic skin function, wound healing, was also approximately 2-fold delayed by AQP3 deletion. By electron microscopy AQP3 deletion did not affect the structure of the unperturbed SC. The SC content of ions (Na(+), K(+), Ca(2+), Mg(2+)) and small solutes (urea, lactic acid, glucose) was not affected by AQP3 deletion nor was the absolute amount or profile of lipids and free amino acids. However, AQP3 deletion produced significant reductions in glycerol content in SC and epidermis (in nmol/microg protein: 5.5 +/- 0.4 versus 2.3 +/- 0.7 in SC; 0.037 +/- 0.007 versus 0.022 +/- 0.005 in epidermis) but not in dermis or blood. These results establish hydration, mechanical, and biosynthetic defects in skin of AQP3-deficient mice. The selective reduction in epidermal and SC glycerol content in AQP3 null mice may account for these defects, providing the first functional evidence for physiologically important glycerol transport by an aquaporin.

Animals↗

Impaired stratum corneum hydration in mice lacking epidermal water channel aquaporin-3.

The water and solute transporting properties of the epidermis have been proposed to be important determinants of skin moisture content and barrier properties. The water/small solute-transporting protein aquaporin-3 (AQP3) was found by immunofluorescence and immunogold electron microscopy to be expressed at the plasma membrane of epidermal keratinocytes in mouse skin. We studied the role of AQP3 in stratum corneum (SC) hydration by comparative measurements in wild-type and AQP3 null mice generated in a hairless SKH1 genetic background. The hairless AQP3 null mice had normal perinatal survival, growth, and serum chemistries but were polyuric because of defective urinary concentrating ability. AQP3 deletion resulted in a > 4-fold reduced osmotic water permeability and > 2-fold reduced glycerol permeability in epidermis. Epidermal, dermal, and SC thickness and morphology were not grossly affected by AQP3 deletion. Surface conductance measurements showed remarkably reduced SC water content in AQP3 null mice in the hairless genetic background (165 +/- 10 versus 269 +/- 12 microsiemens (microS), p < 0.001), as well as in a CD1 genetic background (209 +/- 21 versus 469 +/- 11 microS). Reduced SC hydration was seen from 3 days after birth. SC hydration in hairless wild-type and AQP3 null mice was reduced to comparable levels (90-100 microS) after a 24-h exposure to a dry atmosphere, but the difference was increased when surface evaporation was prevented by occlusion or exposure to a humidified atmosphere (179 +/- 13 versus 441 +/- 34 microS). Conductance measurements after serial tape stripping suggested reduced water content throughout the SC in AQP3 null mice. Water sorption-desorption experiments indicated reduced water holding capacity in the SC of AQP3 null mice. The impaired skin hydration in AQP3 null mice provides the first functional evidence for the involvement of AQP3 in skin physiology. Modulation of AQP3 expression or function may thus alter epidermal moisture content and water loss in skin diseases.

Age Factors↗

Chemically modified polysulfone hollow fibers with vinylpyrrolidone having improved blood compatibility.

Hydrophilic polysulfone membranes (PVP-PSf) were prepared from polysulfone membranes covalently conjugated with polyvinylpyrrolidone (PVP) on the surface. The immobilized amount of vinylpyrrolidone on PVP-PSf membranes was controlled by the amount of vinylpyrrolidone monomer in the reaction solution and the reaction time. The PVP-PSf membranes were found to be the most hydrophilic membranes among the polysulfone and surface-modified polysulfone membranes prepared in this study. This is explained by the long hydrophilic side chain of polyvinylpyrrolidone on the PVP-PSf membranes which contributes to the hydrophilic wiper on the hydrophobic PSf membranes. It was found that PVP-PSf membranes gave lower protein adsorption from a plasma solution than polysulfone and other surface-modified membranes (p < 0.01). This is attributed to the hydrophilic surface of the PVP-PSf membranes, because the hydrophilic surface is known to reduce the protein adsorption on the membranes. The PVP-PSf membranes showed a much suppressed number of adhering platelets on the surface than polysulfone and other surface-modified membranes (p < 0.01). It is suggested that the hydrophilic surface of the PVP-PSf membranes without ionic groups causes the suppression of platelet adhesion on the PVP-PSf membranes and that the long hydrophilic side chain of polyvinylpyrrolidone on PVP-PSf membranes contributes to the hydrophilic and hemocompatible wipers on the surface of the hydrophobic PSf membranes.

Adsorption↗

Rapid compensation for glycosylphosphatidylinositol anchor deficient keratinocytes after birth: visualization of glycosylphosphatidylinositol-anchored proteins in situ.

Pig-a, an X-linked gene, is a key component of glycosylphosphatidylinositol (GPI) anchor biosynthesis based on the fact that lack of this gene causes deficiencies of hundreds of GPI-anchored proteins. We previously demonstrated an essential role for the GPI-anchor in keratinocyte differentiation using male Pig-a knockout mice (K5-Cre:Pig-a flox). Here we analyzed keratinocytes of the female K5-Cre: Pig-a flox/+ mice with heterozygous knockout of Pig-a. These cells exhibited the mosaic pattern of GPI-anchor positive and negative expression typical of random inactivation of the X chromosome. The female K5-Cre:Pig-a flox/+ mice appeared slightly wrinkled with dry skin at birth and white scales starting from 4 d after birth without any histologic abnormality. This phenotype was temporary and milder than that seen in the male knockout mice. To characterize the fate of GPI-anchor-positive cells more clearly, we introduced a transgenic mouse line that expresses enhanced green fluorescent protein in GPI-anchored form into female K5-Cre:Pig-a flox/+ mice and monitored GPI-anchor-positive keratinocytes in situ. Within 36 h after birth, the upper layer of the GPI-anchor-negative zone in epidermis was replaced by the GPI-anchor-positive counterpart. This tissue replacement was accompanied by recovery in trans-epidermal water loss over a similar time course. These observations suggest that the GPI-anchoring is associated with the barrier function as well as with organized differentiation of the epidermis after birth.

Animals↗

Human epidermal glucosylceramides are major precursors of stratum corneum ceramides.

Ceramides are the major component of the stratum corneum, accounting for 30%-40% of stratum corneum lipids by weight, and are composed of at least seven molecular groups (designated ceramides 1-7). Stratum corneum ceramides, together with cholesterol and fatty acids, form extracellular lamellae that are responsible for the epidermal permeability barrier. Previous studies indicated that beta-glucocerebrosidase- and sphingomyelinase-dependent ceramide production from glucosylceramides and sphingomyelins, respectively, is important for epidermal permeability barrier homeostasis. A recent study indicated that sphingomyelins are precursors of two stratum corneum ceramide molecular groups (ceramides 2 and 5). In this study, we have examined the role of glucosylceramides in the generation of each of the seven stratum corneum ceramide molecular groups. First, the structures of various glucosylceramide species in human epidermis were determined by gas chromatography-mass spectrometry, fast atom bombardment-mass spectrometry, and nuclear magnetic resonance. The results indicate that total epidermal glucosylceramides are composed of six distinct molecular groups, glucosylceramides 1-6. Glucosylceramide 1 contains sphingenine and nonhydroxy fatty acids, glucosylceramide 2, phytosphingosine and nonhydroxy fatty acids, glucosylceramide 3, phytosphingosine with one double bond and nonhydroxy fatty acids, glucosylceramide 4, sphingenine and alpha-hydroxy fatty acids, glucosylceramide 5, phytosphingosine and alpha-hydroxy fatty acids, and glucosylceramide 6, phytosphingosine with one double bond and alpha-hydroxy fatty acids. The nonhydroxy fatty acids typically have 16-24-carbon-length chains, whereas alpha-hydroxy fatty acids are limited to 24-, 25-, and 26-carbon chains. The sphingosine bases are C18 or C20 chains. Next, acylglucosylceramides and glucosylceramides were treated with beta-glucocerebrosidase and the ceramides released were compared with stratum corneum ceramides. Ceramide moieties of acylglucosylceramides and glucosylceramides 1, 2, 4-6 correspond to stratum corneum ceramides 1-7. These results, together with those of our previous reports characterizing epidermal sphingomyelins, indicate that all ceramide species, including omega-hydroxy fatty-acid-containing ceramides, are derived from glucosylceramides, and fractions of ceramides 2 and 5 are from sphingomyelins. Furthermore, structural analysis of glucosylceramides revealed that human epidermal glycosphingolipids display a unique lipid profile that is rich in very long chain hydroxylated (alpha- and omega-hydroxy) fatty acids and phytosphingosine.

Adolescent↗

Difference in the attachment of hepatocytes between a poly(gamma-benzyl L-glutamate) (PBLG)/poly(N-isopropylacrylamide) (PNIPAAm) diblock copolymer cast surface and a PBlg/PNIPAAm Langmuir-Blodgett one.

The effects of temperature on the monolayer behavior of the poly(gamma-benzyl L-glutamate) (PBLG)/poly(N-isopropylacrylamide) (PNIPAAm) diblock copolymer at the air-water interface were examined. Differences in the adhesion and morphology of hepatocytes between Langmuir-Blodgett (LB) films and cast surfaces of the PBLG/PNIPAAm diblock copolymer were investigated. The surface pressure (pi)-area (A) curve of the block copolymer had a tendency to expand with the temperature, due to a change in the conformation of PNIPAAm with the temperature change. Attachment of hepatocytes onto the PBLG/PNIPAAm block copolymer LB surface decreased slightly with an increase of the PNIPAAm content in the block copolymer, whereas that onto the cast surface decreased rapidly with an increase of the PNIPAAm content, due to the hydrophilic property of PNIPAAm in the microphase-separated structure. Rapid morphological changes of the hepatocytes adhered to the LB surfaces, from round shapes to spreading ones, were observed, compared with the cast films. The hepatocytes that adhered to the block copolymer LB surfaces showed less flattened and spread shapes than those that adhered to the PBLG one. Also, the spheroid formation of the hepatocytes increased with an increase of the PNIPAAm content in the block copolymer cast films.

Acrylic Resins↗