Adiponectin, chemerin, cytokines, and dipeptidyl peptidase 4 are released from human adipose tissue in a depot-dependent manner: an in vitro system including human serum albumin

Dipeptidyl peptidase 4 (DPP4), a transmembrane protein, has been identified in human adipose tissue and is considered to be associated with obesity-related type 2 diabetes. Since adipose tissue is relatively hypoxic in obese participants, we investigated the expression of DPP4 in human preadipocytes (hPA) and adipocytes in hypoxia, during differentiation and upon insulin stimulation. The results show that DPP4 is abundantly expressed in hPA but very sparsely in adipocytes. During differentiationin vitro, the expression of DPP4 in hPA is reduced on the addition of differentiation medium, indicating that this protein can be hPA marker. Long term hypoxia altered the expression of DPP4 in hPA. Inin vitrohypoxic conditions the protease activity of shed DPP4 is reduced; however, in the presence of insulin, the increase in DPP4 expression is potentiated by hypoxia.

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The Measurement of the Extracellular Space in an In Vitro System of Human Leucocytes

Clinical Science ◽

10.1042/cs0420647 ◽

1972 ◽

Vol 42 (5) ◽

pp. 647-649

Author(s):

J. Patrick ◽

P. J. Hilton

Keyword(s):

Molecular Weight ◽

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

High Molecular Weight ◽

Extracellular Space ◽

Extracellular Fluid ◽

In Vitro System ◽

Significant Difference

1. The extracellular space of an in vitro system of human leucocytes in an artificial extracellular fluid has been measured with Na235SO4, 131I-labelled human serum albumin and 125I-labelled polyvinylpyrrolidone of high molecular weight. 2. There was no significant difference between the space measured with Na235SO4 and 125I-labelled polyvinylpyrrolidone. The space measured with 131I-labelled human serum albumin was significantly larger than that measured with 125I-labelled polyvinylpyrrolidone. 3. High-molecular-weight 125I-labelled polyvinylpyrrolidone appears to be a useful extracellular marker for this in vitro system.

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Haemolytic activity of polyamidoamine dendrimers and the protective role of human serum albumin

Proceedings of The Royal Society A Mathematical Physical and Engineering Sciences ◽

10.1098/rspa.2009.0050 ◽

2009 ◽

Vol 466 (2117) ◽

pp. 1527-1534 ◽

Cited By ~ 31

Author(s):

Barbara Klajnert ◽

Sylwia Pikala ◽

Maria Bryszewska

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Protective Role ◽

Haemolytic Activity ◽

Dependent Manner ◽

Concentration Dependent Manner ◽

Polyamidoamine Dendrimers

We have examined the haemolytic activity of polyamidoamine dendrimers. Haemolysis increased in a generation- and concentration-dependent manner. Moreover, the longer the incubation time, the greater the amount of haemoglobin released. When human serum albumin (HSA) was present in the incubation buffer, the extent of haemolysis decreased. This protective effect may be due to the high affinity of dendrimers for proteins: dendrimers that interact with HSA are unable to disrupt the membrane to the same extent as free dendrimers. The presence of HSA makes the buffer more relevant to physiological conditions. The results of this study suggest that the actual haemotoxicity of dendrimers in vivo is lower than is observed in vitro .

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Study on the interaction of ertugliflozin with human serum albumin in vitro by multispectroscopic methods, molecular docking, and molecular dynamics simulation

Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy ◽

10.1016/j.saa.2019.04.047 ◽

2019 ◽

Vol 219 ◽

pp. 83-90 ◽

Cited By ~ 14

Author(s):

Wenjing Wang ◽

Na Gan ◽

Qiaomei Sun ◽

Di Wu ◽

Ruixue Gan ◽

...

Keyword(s):

Molecular Dynamics ◽

Molecular Docking ◽

Molecular Dynamics Simulation ◽

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Dynamics Simulation

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Nof2206Probing the interaction of memantine, an important Alzheimer's drug, with human serum albumin: In silico and In vitro approach

Journal of Molecular Liquids ◽

10.1016/j.molliq.2021.116888 ◽

2021 ◽

pp. 116888

Author(s):

Fahad A. Alhumaydhi ◽

Mohammad Abdullah Aljasir ◽

Abdullah S.M. Aljohani ◽

Suliman A. Alsagaby ◽

Ameen S.S. Alwashmi ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

In Silico

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Synthesis and In Vitro Assessment of pH-Sensitive Human Serum Albumin Conjugates of Pirarubicin

Pharmaceuticals ◽

10.3390/ph14010022 ◽

2020 ◽

Vol 14 (1) ◽

pp. 22

Author(s):

Kenji Tsukigawa ◽

Shuhei Imoto ◽

Keishi Yamasaki ◽

Koji Nishi ◽

Toshihiko Tsutsumi ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Coupling Reaction ◽

Synthetic Polymer ◽

Ph Sensitive ◽

Acidic Ph ◽

Polymer Conjugate ◽

Acidic Conditions

In a previous study, we reported on the development of a synthetic polymer conjugate of pirarubicin (THP) that was formed via an acid-labile hydrazone bond between the polymer and the THP. However, the synthetic polymer itself was non-biodegradable, which could lead to unexpected adverse effects. Human serum albumin (HSA), which has a high biocompatibility and good biodegradability, is also a potent carrier for delivering antitumor drugs. The objective of this study was to develop pH-sensitive HSA conjugates of THP (HSA-THP), and investigate the release of THP and the cytotoxicity under acidic conditions in vitro for further clinical development. HSA-THP was synthesized by conjugating maleimide hydrazone derivatives of THP with poly-thiolated HSA using 2-iminothiolane, via a thiol-maleimide coupling reaction. We synthesized two types of HSA-THP that contained different amounts of THP (HSA-THP2 and HSA-THP4). Free THP was released from both of the HSA conjugates more rapidly at an acidic pH, and the rates of release for HSA-THP2 and HSA-THP4 were similar. Moreover, both HSA-THPs exhibited a higher cytotoxicity at acidic pH than at neutral pH, which is consistent with the effective liberation of free THP under acidic conditions. These findings suggest that these types of HSA-THPs are promising candidates for further development.

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The in Vitro Anti-HIV Efficacy of Negatively Charged Human Serum Albumin Is Antagonized by Heparin

AIDS Research and Human Retroviruses ◽

10.1089/aid.1997.13.677 ◽

1997 ◽

Vol 13 (8) ◽

pp. 677-683 ◽

Cited By ~ 3

Author(s):

P.J. SWART ◽

C.S. SUN ◽

M.E. KUIPERS ◽

C. ASUNCION ◽

S. JOSEPHS ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Anti Hiv

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Kinetic study of the photochemical changes of (ZZ)-bilirubin IX α bound to human serum albumin. Demonstration of (EZ)-bilirubin IX α as an intermediate in photochemical changes from (ZZ)-bilirubin IX α to (EZ)-cyclobilirubin IX α

Biochemical Journal ◽

10.1042/bj2260251 ◽

1985 ◽

Vol 226 (1) ◽

pp. 251-258 ◽

Cited By ~ 25

Author(s):

S Itoh ◽

S Onishi

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Kinetic Study ◽

Human Serum ◽

Photochemical Reaction ◽

Relative Rate ◽

Significant Preference ◽

Geometrical Isomers ◽

Relative Rate Constants

The present study was performed to elucidate why the photochemical reaction of (ZZ)-bilirubin bound to human serum albumin is singularly selective, and only one of the two (EZ)- and (ZE)-bilirubins, the (ZE)-isomer, is produced. In a kinetic study of the photochemical reaction in vitro, the sum of the relative rate constants of photochemical transformation of (EZ)-bilirubin into both (EZ)-cyclobilirubin and (ZZ)-bilirubin, with a significant preference for the former, was proved to be considerably larger than that of the transformation of (ZZ)-bilirubin into (EZ)-bilirubin. Therefore only one of the geometrical isomers, namely (ZE)-bilirubin, is apparently formed. It was concluded that (EZ)-bilirubin photochemically undergoes (EZ)-cyclization, i.e. structural photoisomerization, while bound to its high-affinity site on human serum albumin, and is an intermediate in the transformation of (ZZ)-bilirubin into (EZ)-cyclobilirubin.

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