scholarly journals Two distinct types of fatty acid-binding protein are expressed in heart ventricle of Antarctic teleost fishes

1998 ◽  
Vol 330 (1) ◽  
pp. 375-382 ◽  
Author(s):  
E. Michael VAYDA ◽  
L. Richard LONDRAVILLE ◽  
E. Robert CASHON ◽  
Lori COSTELLO ◽  
D. Bruce SIDELL
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Cardiac Tissue ◽  
Binding Protein ◽  
Pectoral Muscle ◽  
Amino Acid Sequences ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Gobionotothen Gibberifrons ◽  
Antarctic Teleosts

This report provides the first evidence for the existence of two distinct types of fatty acid-binding protein (FABP) in cardiac tissue of vertebrates. Four species of Antarctic teleost fish (Chaenocephalus aceratus, Cryodraco antarcticus, Gobionotothen gibberifrons and Notothenia coriiceps) exhibited two FABP mRNAs of 1.0 kb and 0.8 kb, which we have termed Hh-FABP and Had-FABP (isolated from eart tissue, with similarity to mammalian eart-type FABP or mammalian ipose-type FABP respectively). These FABP types appear to be products of distinct genes. Both FABP transcripts were abundant in cardiac and aerobic pectoral muscle. However, relative abundance of the two types varied distinctly among other tissues such as kidney, brain, spleen and white muscle. Neither FABP type was expressed in liver or intestine. The coding regions of Hh-FABP and Had-FABP cDNAs from the same species are only ~ 60% identical with one another. However, homologues of each FABP species, which exhibit > 98% identity to their respective types, were isolated from three other Antarctic teleosts. Phylogenetic analysis of aligned amino-acid sequences places Hh-FABP with other vertebrate heart-type FABPs, and Had with adipose/cutaneous FABPs. Expression of two distinct FABPs in cardiac tissue of Antarctic teleosts may be related to their ability to both utilize fatty acid as the primary metabolic fuel and to store lipid intracellularly.

scholarly journals Characterization and amino acid sequence of a fatty acid-binding protein from human heart

1988 ◽  
Vol 252 (1) ◽  
pp. 191-198 ◽  
Author(s):  
G D Offner ◽  
P Brecher ◽  
W B Sawlivich ◽  
C E Costello ◽  
R F Troxler
Keyword(s):  
Fatty Acid ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Heart ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Amino Acid Sequences ◽  
British Library ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

The complete amino acid sequence of a fatty acid-binding protein from human heart was determined by automated Edman degradation of CNBr, BNPS-skatole [3′-bromo-3-methyl-2-(2-nitrobenzenesulphenyl)indolenine], hydroxylamine, Staphylococcus aureus V8 proteinase, tryptic and chymotryptic peptides, and by digestion of the protein with carboxypeptidase A. The sequence of the blocked N-terminal tryptic peptide from citraconylated protein was determined by collisionally induced decomposition mass spectrometry. The protein contains 132 amino acid residues, is enriched with respect to threonine and lysine, lacks cysteine, has an acetylated valine residue at the N-terminus, and has an Mr of 14768 and an isoelectric point of 5.25. This protein contains two short internal repeated sequences from residues 48-54 and from residues 114-119 located within regions of predicted beta-structure and decreasing hydrophobicity. These short repeats are contained within two longer repeated regions from residues 48-60 and residues 114-125, which display 62% sequence similarity. These regions could accommodate the charged and uncharged moieties of long-chain fatty acids and may represent fatty acid-binding domains consistent with the finding that human heart fatty acid-binding protein binds 2 mol of oleate or palmitate/mol of protein. Detailed evidence for the amino acid sequences of the peptides has been deposited as Supplementary Publication SUP 50143 (23 pages) at the British Library Lending Division, Boston Spa, Yorkshire LS23 7BQ, U.K., from whom copies may be obtained as indicated in Biochem. J. (1988) 249, 5.

Presence of two new fatty acid binding proteins in catfish liver

1996 ◽  
Vol 74 (5) ◽  
pp. 675-680 ◽  
Author(s):  
Santiago M. Di Pietro ◽  
José A. Santomé
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Bovine Heart

A basic fatty acid binding protein (FABP), closely related to that of chicken liver, was isolated and characterized from catfish (Rhamdia sapo) liver in a previous work. Results herein show the presence of another two FABPs in which partial amino acid sequences reveal great similarity with the corresponding sequences of other already known FABPs belonging to the heart type. The purification procedures for both proteins involve gel filtration, anion-exchange chromatography, and sodium dodecyl sulfate – polyacrylamide gel electrophoresis (as a last step). Because both FABP N-termini were blocked, they were submitted to in-gel tryptic digestion and the resulting peptides were separated by high performance liquid chromatography, and sequenced by Edman degradation. One of these proteins presented the highest identity percentage when compared with those of the human and bovine heart and bovine brain (81%), and the other when compared with those of chicken retina (75%) and mouse and bovine heart FABP (70%). The presence of several FABPs plus the fact that they belong to different types, as found in the Rhamdia sapo liver, is unusual in mammals, which express a characteristic liver-type member of this protein family.Key words: fatty acid binding protein, liver, catfish, Rhamdia sapo.

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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