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Background: There is a need for biomarkers in accessible matrices, such as blood, for the diagnosis of neurodegenerative diseases. The aim of this study was to measure the serum levels of brain-type fatty acid-binding protein (FABP) and heart-type FABP in patients with dementia-involving diseases., Methods: Brain- and heart-type FABP were measured in serum samples from patients with either Alzheimer's disease (AD) (n = 31), Parkinson's disease (PD, n = 43), or other cognitive disorders (OCD, n = 42) and in 52 healthy controls. The localization of brain- and heart-type FABP was determined in brain sections by immunohistochemistry., Results: Brain-type FABP levels were elevated in serum of 29%, 35%, and 24% of the patients with AD, PD, and OCD, respectively, and in 2% of the healthy donors. Heart-type FABP serum levels were not different amongst the patient groups. Brain-type and heart-type FABP expression was observed in reactive astrocytes in brain sections of patients with AD., Conclusions: In contrast to heart-type FABP, serum levels of brain-type FABP are elevated in a significant proportion of patients with various neurodegenerative diseases and can therefore have importance for defining subgroups of these patients., (© 2010 The Author(s). European Journal of Neurology © 2010 EFNS.)

The long-distance migratory flights of birds are predominantly fueled by the oxidation of fatty acids, which are sourced primarily from extracellular adipose stores. These fatty acids have to be transported, via the circulatory system, to the mitochondria of the active muscles. An important facilitator of fatty acid transport within the cytoplasm of muscle cells is fatty acid binding protein (FABP), which serves as an intracellular carrier of long-chain fatty acids. In mammals, the muscular FABP content is related to the fatty acid oxidation capacity of the tissue. The aim of this study was to measure FABP in samples taken from the cardiac, pectoralis, and semimembranosus muscles of a long-distance avian migrant, the barnacle goose (Branta leucopsis), at various stages of development. Western blot analysis identified a single goose muscle protein of 15 kDa that was able to bind fatty acids and showed a 66% cross-reactivity with antibodies against human heart-type FABP. Captive goslings showed no significant changes in FABP content of either the heart (62.6 +/- 10.6 microgram/g wet wt) or the semimembranosus muscle (8.4 +/- 1.9 microgram/g wet wt) during development. However, in both peripheral and deep sites within the pectoralis muscle, FABP content of samples taken from captive goslings were approximately 10-fold higher throughout development and reached values of 30-40 microgram/g wet wt in fledging goslings at 7 wk of age. A further twofold higher value was seen in wild but not in captive goslings immediately before migration (12 wk of age). Similarly, FABP content was significantly higher in pectoralis samples taken from wild adults (94.3 +/- 3.6 microgram/g wet wt) compared with those from captive adults (60.5 +/- 3.6 micro/g wet wt). These results suggest that the experience of flight activity may be of critical importance in achieving maximal expression of FABP in the pectoralis muscles of postfledging and mature geese immediately before migration.

Objective: To test whether fatty acid binding protein (FABP) is a useful plasma marker for the early detection of exercise induced skeletal muscle injury in healthy subjects., Methods: Plasma concentrations of FABP and myoglobin (Mb) were measured in six healthy physical education teacher trainees after 20 minutes of downhill running (16% incline; mean lactate 4 mmol/l; 70% (VO2MAX). Creatine kinase (CK) was measured for comparison., Results: Significant increases were found in plasma FABP (mean peak level 50 micrograms/l), Mb (823 micrograms/l), and CK (491 U/l). Mb and FABP concentrations were already significantly elevated (p < 0.05) at 30 minutes, but CK not until two hours after exercise. Whereas Mb and FABP decreased to normal levels within 24 hours, CK activity remained elevated until 48 hours. The Mb to FABP ratio in plasma after exercise induced muscle injury was 15.0 (1.3) (mean (SEM)) (range 7.4-31.1), which is within the range of ratios calculated for skeletal muscle tissue contents of Mb and FABP, but different from the reported plasma ratio after myocardial injury (4-6)., Conclusions: After eccentric exercise induced muscle injury, plasma FABP and Mb increase and decrease more rapidly than CK, indicating that both FABP and Mb are more useful than CK for the early detection of such injuries and the monitoring of injury during repeated exercise bouts. In addition, the Mb to FABP ratio in the plasma identifies the type of muscle injured.

Cytoplasmic heart-type fatty acid-binding protein has recently gained much attention in clinical diagnosis as a very early marker of acute myocardial infarction. Immunoassays have been developed for determination of this protein in plasma and urine samples. In the present study it is shown that those types of fatty acid-binding proteins which are abundant in tissues other than heart and muscle do not interfere with immunochemical determination of heart-type fatty acid-binding protein. To provide sufficient protein of consistent quality as standard in these immunoassays, human heart-type fatty acid-binding protein was cloned, expressed in Escherichia coli and purified to homogeneity. For quantitation of the recombinant protein its extinction coefficient was determined. Comparison of the recombinant and tissue-derived proteins by a variety of methods revealed both proteins to show similar kinetic as well as equilibrium constants with respect to two monoclonal antibodies currently applied in immunochemical detection of heart-type fatty acid-binding protein. Both preparations were indistiguishable in sandwich-ELISA and immunosensor measurements. A high stability of the recombinant protein was proven by ELISA measurements during storage and several freeze and thaw cycles. Thus, recombinant and tissue-derived heart-type fatty acid-binding proteins are immunochemically equivalent. The recombinant human heart-type fatty acid-binding protein is now available as standard for immunoassays.

To allow a more rapid determination of heart-type fatty acid-binding protein (FABP) concentration in plasma a direct non-competitive (sandwich-type) ELISA was developed which uses high-affinity monoclonal antibodies to FABP. Total performance time of the one-step immunoassay is 45 min. The standard curve was linear between 0.2-6 micrograms/L, and the within-run and between-run coefficients of variations were below 6 and 11%, respectively. The serum FABP concentration measured in 79 healthy individuals was 1.6 (0.8) [mean (SD), range 0.3-5.0] micrograms/L. The assay can be used for rapid plasma or serum FABP measurement in the early diagnosis of acute myocardial infarction.

Heart-type fatty acid-binding protein (H-FABP), a 15 kDa non-enzymatic protein, which is abundantly present in heart and some skeletal muscles, was recently found to be a useful plasma marker for acute myocardial infarction. The BIAcore biosensor technology was used to raise and characterize a panel of 13 monoclonal antibodies against human H-FABP which did not crossreact with other FABP types of human origin. The kinetics of association and dissociation between FABP and the monoclonal antibodies was studied. By pairwise mapping several distinct epitopes could be identified.