Stimulatory effect of serum albumin on the proliferation of serum-free SV40-transformed Balb/c 3T3 cells

Bedotti, Roberta; Borghetti, Angelo F.; Favilla, Roberto

doi:10.1016/0167-4889(90)90028-c

Cited by 3 publications

(3 citation statements)

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“…It has been reported that human or bovine albumin can promote SV-40-transformed Balb/c 3T3 cells and B cell proliferation in vitro , but the mechanism was unclear in these experiments [21,22] and no reports have revealed the association between albumin concentration and cell proliferation, including its biological effects. It is unclear whether albumin alone induces these changes.…”

Section: Discussionmentioning

confidence: 99%

Albumin Suppresses Human Hepatocellular Carcinoma Proliferation and the Cell Cycle

Nojiri

Joh

2014

IJMS

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Many investigations have revealed that a low recurrence rate of hepatocellular carcinoma (HCC) is associated with high serum albumin levels in patients; therefore, high levels of serum albumin are a major indicator of a favorable prognosis. However, the mechanism inhibiting the proliferation of HCC has not yet been elucidated, so we investigated the effect of serum albumin on HCC cell proliferation. Hep3B was cultured in MEM with no serum or containing 5 g/dL human albumin. As control samples, Prionex was added to generate the same osmotic pressure as albumin. After 24-h incubation, the expressions of α-fetoprotein (AFP), p53, p21, and p57 were evaluated with real-time PCR using total RNA extracted from the liver. Protein expressions and the phosphorylation of Rb (retinoblastoma) were determined by Western blot analysis using total protein extracted from the liver. For flow cytometric analysis of the cell cycle, FACS analysis was performed. The percentages of cell cycle distribution were evaluated by PI staining, and all samples were analyzed employing FACScalibur (BD) with appropriate software (ModFit LT; BD). The cell proliferation assay was performed by counting cells with using a Scepter handy automated cell counter (Millipore). The mRNA levels of AFP relative to Alb(−): Alb(−), Alb(+), and Prionex, were 1, 0.7 ± 0.2 (p < 0.001 for Alb(−)), and 1 ± 0.3, respectively. The mRNA levels of p21 were 1, 1.58 ± 0.4 (p = 0.007 for Alb(−) and p = 0.004 for Prionex), and 0.8 ± 0.2, respectively. The mRNA levels of p57 were 1, 4.4 ± 1.4 (p = 0.002 for Alb(−) and Prionex), and 1.0 ± 0.1, respectively. The protein expression levels of Rb were similar in all culture media. The phosphorylation of P807/811 and P780 of Rb protein was reduced in Alb(+). More cells in the G0/G1 phase and fewer cells in S and G2/M phases were obtained in Alb(+) than in Alb(−) (G0/G1: 60.9%, 67.7%, 61.5%; G2/M: 16.5%, 13.1%, 15.6%; S: 22.6%, 19.2%, 23.0%, Alb(−), Alb(+), Prionex, respectively). The same results were obtained in HepG2. Cell proliferation was inhibited in 5 g/dL albumin medium in both HepG2 cells and Hep3B cells in 24 h culture by counting cell numbers. The presence of albumin in serum reduces the phosphorylation of Rb proteins and enhances the expression of p21 and p57, following an increase in the G0/G1 cell population, and suppresses cell proliferation. These results suggest that albumin itself suppresses the proliferation of hepatocellular carcinoma.

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Section: Discussionmentioning

confidence: 99%

Albumin Suppresses Human Hepatocellular Carcinoma Proliferation and the Cell Cycle

Nojiri

Joh

2014

IJMS

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“…The effect is seen for both copolymers, but it is more pronounced for A 45 B 11 0C 37 - based nanoparticles. BSA-FITC loaded A 45 B 110 C 37 nanoparticles presented a viability >100%, due to the stimulatory effect of BSA on cell proliferation . Overall, the low cytotoxicity of protein nanoparticles supports their further development for therapeutic applications.…”

Section: Resultsmentioning

confidence: 84%

“…BSA-FITC loaded A 45 B 110 C 37 nanoparticles presented a viability >100%, due to the stimulatory effect of BSA on cell proliferation. 31 Overall, the low cytotoxicity of protein nanoparticles supports their further development for therapeutic applications.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Asymmetric Triblock Copolymer Nanocarriers for Controlled Localization and pH-Sensitive Release of Proteins

et al. 2016

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Designing nanocarriers to release proteins under specific conditions is required to improve therapeutic approaches, especially in treating cancer and protein deficiency diseases. We present here supramolecular assemblies based on asymmetric poly(ethylene glycol)-b-poly(methylcaprolactone)-b-poly(2-(N,Ndiethylamino)ethyl methacrylate) (PEG-b-PMCL-b-PDMAEMA) copolymers for controlled localization and pH-sensitive release of proteins. Copolymers self-assembled in soft nanoparticles with a core domain formed by PMCL, and a hydrophilic domain based on PEG mainly embedded inside, and the branched PDMAEMA exposed at the particle surface. We selected as model proteins to be attached to the nanoparticles bovine serum albumin (BSA) and acid sphingomyelinase (ASM), the latter being an ideal candidate for protein replacement therapy. The hydrophilic/hydrophobic ratio, nanoparticle size, and the nature of biomolecules are key factors for modulating protein localization and attachment efficiency. The predominant outer shell of PDMAEMA allows efficient pH-triggered release of BSA and ASM, and in acidic conditions >70% of the bound proteins were released. Uptake of protein-attached nanoparticles by HELA cells, together with low toxicity and pH-responsive release, supports such protein-bound nanoparticles as efficient stimuli-responsive candidates for protein therapy.

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Stimulatory effect of serum albumin on the proliferation of serum-free SV40-transformed Balb/c 3T3 cells

Cited by 3 publications

References 14 publications

Albumin Suppresses Human Hepatocellular Carcinoma Proliferation and the Cell Cycle

Albumin Suppresses Human Hepatocellular Carcinoma Proliferation and the Cell Cycle

Asymmetric Triblock Copolymer Nanocarriers for Controlled Localization and pH-Sensitive Release of Proteins

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