A Residual Structure in Unfolded Intestinal Fatty Acid Binding Protein Consists of Amino Acids That Are Neighbors in the Native State†

Biochemistry ◽  
2006 ◽  
Vol 45 (8) ◽  
pp. 2608-2617 ◽  
Author(s):  
Ira J. Ropson ◽  
Joshua A. Boyer ◽  
Paula M. Dalessio
Keyword(s):  
Amino Acids ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Native State ◽  
Fatty Acid Binding ◽  
Residual Structure ◽  
Acid Binding Protein

scholarly journals Fatty acid binding and conformational stability of mutants of human muscle fatty acid-binding protein

1996 ◽  
Vol 314 (1) ◽  
pp. 253-260 ◽  
Author(s):  
Clemens F. M. PRINSEN ◽  
Jacques H. VEERKAMP
Keyword(s):  
Amino Acids ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Binding Activity ◽  
Human Muscle ◽  
Wild Type ◽  
Fatty Acid Binding ◽  
Mutant Proteins ◽  
Acid Binding Protein

Human muscle fatty acid-binding protein (M-FABP) is a 15 kDa cytosolic protein which may be involved in fatty acid transfer and modulation of non-esterified fatty acid concentration in heart, skeletal muscle, kidney and many other tissues. Crystallographic studies have suggested the importance of the amino acids Thr-40, Arg-106, Arg-126 and Tyr-128 for the hydrogen bonding network of the fatty acid carboxylate group. Two phenylalanines at 16 and 57 are positioned to interact with the acyl chain of the fatty acid. We prepared 13 mutant proteins by site-directed mutagenesis and tested them for fatty acid binding and stability. Substitution of amino acids Phe-16, Arg-106 or Arg-126 created proteins which showed a large decrease in or complete loss of oleic acid binding. Substitution of Phe-57 by Ser or Val and of Tyr-128 by Phe had no great effect. The stability of the mutant proteins was tested by denaturation studies on the basis of fatty acid binding or tryptophan fluorescence and compared with that of the wild-type M-FABP. There was no direct relationship between fatty acid-binding activity and stability. Less stable mutants (F57S and Y128F) did not show a marked change in fatty acid-binding activity. Substitution of Arg-126 by Gln or Arg-106 by Thr eliminated binding activity, but the former mutant protein showed wild-type stability, in contrast to the latter. The results are in agreement with crystallographic data.

Engineering a compact non-native state of intestinal fatty acid-binding protein

2000 ◽  
Vol 1476 (2) ◽  
pp. 203-218 ◽  
Author(s):  
Eugenia M. Clérico ◽  
Sergio G. Peisajovich ◽  
Marcelo Ceolı́n ◽  
Pablo D. Ghiringhelli ◽  
Mario R. Ermácora
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Native State ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

Calcium-dependent release of adipocyte fatty acid binding protein from human adipocytes

2014 ◽  
Vol 122 (03) ◽  
Author(s):  
I Schlottmann ◽  
M Ehrhart-Bornstein ◽  
M Wabitsch ◽  
SR Bornstein ◽  
V Lamounier-Zepter
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Human Adipocytes ◽  
Fatty Acid Binding ◽  
Calcium Dependent ◽  
Acid Binding Protein

Biochemical and Histochemical Studies of Liver Fatty Acid Binding Protein in Alcohol-Treated Rats.

1993 ◽  
Vol 14 (3) ◽  
pp. 171-181
Author(s):  
Shigeya WATANABE ◽  
Yoshio WAKATSUKI ◽  
Hideyuki YOSHIOKA ◽  
Masami INADA ◽  
Teruo ONO ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

Diagnostic value of fatty acid-binding protein determination in urologists and nephrologists clinical practice

2020 ◽  
pp. 92-99
Author(s):  
Konstantin R. Galkovich
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Physiological Role ◽  
Diagnostic Value ◽  
Obstructive Nephropathy ◽  
Malignant Neoplasms ◽  
Early Screening ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

This review summarizes the data on the diagnostic value of determining the fatty acid-binding protein (FABP) in urological and nephrological diseases. A physiological role of this protein in the pathogenesis of malignant neoplasms of the kidney, bladder, and prostate was analyzed. The dynamics of FABP in serum and urine with decreased renal function was studied: this protein is considered as a diagnostic and prognostic marker for chronic kidney disease and acute renal injury. The value of FABP for early screening of patients with obstructive nephropathy was revealed, and its role in predicting the restoration of kidney function was studied: the dynamics of FABP content can characterize the process of graft recovery, determine the need for hemodialysis. In patients with oligozooastenospermia, a reduced content of FABP in the ejaculate was registered, which was probably an adverse sign indicating a violation of male fertility.

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