TY - JOUR
T1 - Isolation and characterization of two fatty acid binding proteins from mouse brain
AU - Myers-Payne, Sean C.
AU - Hubbell, Timothy
AU - Pu, Lixia
AU - Schnütgen, Frank
AU - Börchers, Torsten
AU - Wood, W. Gibson
AU - Spener, Friedrich
AU - Schroeder, Friedhelm
PY - 1996/4
Y1 - 1996/4
N2 - Two fatty acid binding proteins (FABPs) were isolated from Swiss Webster mouse brains. Neither protein cross-reacted with antisera to recombinant liver L-FABP. One protein, designated brain H-FABP, migrated on tricine sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) as a single band at 14.5 kDa with pl 4.9. Brain H-FABP bound NBD-stearic acid and cis-parinaric acid with K(D) values near 0.02 and 0.5 μM, respectively. Brain H-FABP cross-reacted with affinity-purified antisera to recombinant heart H-FABP. The second protein, mouse brain B-FABP, migrated on tricine SDS-PAGE gels as a doublet at 16.0 and 15.5 kDa with pI values of 4.5 and 4.7, respectively. Brain B-FABP bound NBD-stearic acid and cis-parinaric acid with K(D) values near 0.01 and 0.7 μM, respectively. The brain B-FABP doublet was immunoreactive with affinity-purified antibodies against recombinant mouse brain B-FABP, but not with affinity-purified antibodies against heart H-FABP. [3H]Oleate competition binding indicated that the two brain FABPs had distinct ligand binding specificities. Both bound fatty acids, fatty acyl CoA, and lysophosphatidic acid. Although both preferentially bound unsaturated fatty acids, twofold differences in specific saturated fatty acid binding were observed. Brain B-FABP and brain H-FABP represented 0.1 and 0.01% of brain total cytosolic protein, respectively. In summary, mouse brain contains two native fatty acid binding proteins, brain H-FABP and brain B-FABP.
AB - Two fatty acid binding proteins (FABPs) were isolated from Swiss Webster mouse brains. Neither protein cross-reacted with antisera to recombinant liver L-FABP. One protein, designated brain H-FABP, migrated on tricine sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) as a single band at 14.5 kDa with pl 4.9. Brain H-FABP bound NBD-stearic acid and cis-parinaric acid with K(D) values near 0.02 and 0.5 μM, respectively. Brain H-FABP cross-reacted with affinity-purified antisera to recombinant heart H-FABP. The second protein, mouse brain B-FABP, migrated on tricine SDS-PAGE gels as a doublet at 16.0 and 15.5 kDa with pI values of 4.5 and 4.7, respectively. Brain B-FABP bound NBD-stearic acid and cis-parinaric acid with K(D) values near 0.01 and 0.7 μM, respectively. The brain B-FABP doublet was immunoreactive with affinity-purified antibodies against recombinant mouse brain B-FABP, but not with affinity-purified antibodies against heart H-FABP. [3H]Oleate competition binding indicated that the two brain FABPs had distinct ligand binding specificities. Both bound fatty acids, fatty acyl CoA, and lysophosphatidic acid. Although both preferentially bound unsaturated fatty acids, twofold differences in specific saturated fatty acid binding were observed. Brain B-FABP and brain H-FABP represented 0.1 and 0.01% of brain total cytosolic protein, respectively. In summary, mouse brain contains two native fatty acid binding proteins, brain H-FABP and brain B-FABP.
KW - Brain
KW - Fatty acid
KW - Fatty acid binding protein
KW - Mouse
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U2 - 10.1046/j.1471-4159.1996.66041648.x
DO - 10.1046/j.1471-4159.1996.66041648.x
M3 - Article
C2 - 8627322
AN - SCOPUS:0029873906
SN - 0022-3042
VL - 66
SP - 1648
EP - 1656
JO - Journal of Neurochemistry
JF - Journal of Neurochemistry
IS - 4
ER -