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Biochemical and biophysical analysis of the intracellular lipid binding proteins of adipocytes
by
LiCata, Vince J.
, Simpson, Melanie A.
, Ribarik Coe, Natalie
, Bernlohr, David A.
in
Amino Acid Sequence
/ Animals
/ Carrier Proteins - chemistry
/ Dose-Response Relationship, Drug
/ Fatty Acid-Binding Protein 7
/ Fatty Acid-Binding Proteins
/ Fatty acids
/ Hydrogen-Ion Concentration
/ In Vitro Techniques
/ Mice
/ Mice, Knockout
/ Models, Molecular
/ Molecular Sequence Data
/ Myelin P2 Protein - chemistry
/ Neoplasm Proteins
/ Nerve Tissue Proteins
/ Physiology
/ Protein Binding
/ Proteins
/ Sequence Homology, Amino Acid
/ Static Electricity
1999
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Biochemical and biophysical analysis of the intracellular lipid binding proteins of adipocytes
by
LiCata, Vince J.
, Simpson, Melanie A.
, Ribarik Coe, Natalie
, Bernlohr, David A.
in
Amino Acid Sequence
/ Animals
/ Carrier Proteins - chemistry
/ Dose-Response Relationship, Drug
/ Fatty Acid-Binding Protein 7
/ Fatty Acid-Binding Proteins
/ Fatty acids
/ Hydrogen-Ion Concentration
/ In Vitro Techniques
/ Mice
/ Mice, Knockout
/ Models, Molecular
/ Molecular Sequence Data
/ Myelin P2 Protein - chemistry
/ Neoplasm Proteins
/ Nerve Tissue Proteins
/ Physiology
/ Protein Binding
/ Proteins
/ Sequence Homology, Amino Acid
/ Static Electricity
1999
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Biochemical and biophysical analysis of the intracellular lipid binding proteins of adipocytes
by
LiCata, Vince J.
, Simpson, Melanie A.
, Ribarik Coe, Natalie
, Bernlohr, David A.
in
Amino Acid Sequence
/ Animals
/ Carrier Proteins - chemistry
/ Dose-Response Relationship, Drug
/ Fatty Acid-Binding Protein 7
/ Fatty Acid-Binding Proteins
/ Fatty acids
/ Hydrogen-Ion Concentration
/ In Vitro Techniques
/ Mice
/ Mice, Knockout
/ Models, Molecular
/ Molecular Sequence Data
/ Myelin P2 Protein - chemistry
/ Neoplasm Proteins
/ Nerve Tissue Proteins
/ Physiology
/ Protein Binding
/ Proteins
/ Sequence Homology, Amino Acid
/ Static Electricity
1999
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Biochemical and biophysical analysis of the intracellular lipid binding proteins of adipocytes
Journal Article
Biochemical and biophysical analysis of the intracellular lipid binding proteins of adipocytes
1999
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Overview
Adipocytes express two lipid-binding proteins; the major one termed the adipocyte lipid-binding protein or aP2 (ALBP/aP2) and a minor one referred to as the keratinocyte lipid-binding protein (KLBP). In order to evaluate the potential physiological roles for these proteins, their biochemical and biophysical properties have been analyzed and compared. ALBP/aP2 and KLBP exhibit similar binding affinities for most long-chain fatty acids; however, ALBP/aP2 exhibits a two to three-fold increased affinity for myristic, palmitic, oleic and linoleic acids, the predominant fatty acids of adipocytes. As measured by guanidinium hydrochloride denaturation, the stability of ALBP/aP2 is nearly 3 kcal/mol greater than that of KLBP. While the pI of ALBP/aP2 was determined to be 9.0, that of KLBP is 6.5 suggesting differing net charges at physiological pH. Analysis of surface electrostatic properties of ALBP/aP2 and KLBP revealed similar charge polarity, although differences in the detailed charge distribution exist between the proteins. The distribution of hydrophobic patches was also different between the proteins,ALBP/aP2 has only scattered hydrophobic surfaces while KLBP has a large hydrophobic patch near the ligand portal into the binding cavity. In sum, these results point out that despite the striking similarity between ALBP/aP2 and KLBP in tertiary structure, significant differences in ligand binding and surface properties exist between the two proteins. Hence, while it is tempting to speculate that ALBP/aP2 and KLBP are metabolically interchangeable, careful analysis suggests that the two proteins are quite distinct and likely to play unique metabolic roles.
Publisher
Springer Nature B.V
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