PMID- 9521644
OWN - NLM
STAT- MEDLINE
DCOM- 19980421
LR  - 20161124
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 37
IP  - 10
DP  - 1998 Mar 10
TI  - Bovine epidermal fatty acid-binding protein: determination of ligand specificity 
      and cellular localization in retina and testis.
PG  - 3250-7
AB  - The fatty acid-binding protein (FABP) family consists of small, cytosolic 
      proteins believed to be involved in the uptake, transport, and solubilization of 
      their hydrophobic ligands. Members of this family have highly conserved sequences 
      and tertiary structures. Using an antibody against testis lipid-binding protein, 
      a member of the FABP family, a protein was identified from bovine retina and 
      testis that coeluted with exogenously added docosahexaenoic acid during 
      purification. Amino acid sequencing and subsequent isolation of its cDNA revealed 
      it to be nearly identical to a bovine protein expressed in the differentiating 
      lens and to be the likely bovine homologue of the human epidermal fatty 
      acid-binding protein (E-FABP). From quantitative Western blot analysis, it was 
      estimated that bovine E-FABP comprised 0.9%, 0.1%, and 2.4% of retina, testis, 
      and lens cytosolic proteins, respectively. Binding studies using the fluorescent 
      probe ADIFAB indicated that this protein bound fatty acids of differing levels of 
      saturation with relatively high affinities. Kd values ranged from 27 to 97 nM. In 
      addition, the protein was immunolocalized to the Muller cells in the retina as 
      well as to Sertoli cells in the testis. The location of bovine E-FABP in cells 
      known to be supportive to other cell types in their tissues and the ability of 
      E-FABP to bind a variety of fatty acids with similar affinities indicate that it 
      may be involved in the uptake and transport of fatty acids essential for the 
      nourishment of the surrounding cell types.
FAU - Kingma, P B
AU  - Kingma PB
AD  - Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, 
      Tennessee 37232-0146, USA.
FAU - Bok, D
AU  - Bok D
FAU - Ong, D E
AU  - Ong DE
LA  - eng
SI  - GENBANK/AF059507
GR  - EY00331/EY/NEI NIH HHS/United States
GR  - EY00444/EY/NEI NIH HHS/United States
GR  - HD 25206/HD/NICHD NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (FABP5 protein, human)
RN  - 0 (FABP7 protein, human)
RN  - 0 (Fatty Acid-Binding Protein 7)
RN  - 0 (Fatty Acid-Binding Proteins)
RN  - 0 (Fatty Acids)
RN  - 0 (Ligands)
RN  - 0 (Myelin P2 Protein)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Tumor Suppressor Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Binding Sites
MH  - Biological Transport, Active
MH  - Carrier Proteins/chemistry/genetics/*metabolism
MH  - Cattle
MH  - DNA, Complementary/genetics
MH  - Fatty Acid-Binding Protein 7
MH  - Fatty Acid-Binding Proteins
MH  - Fatty Acids/metabolism
MH  - Humans
MH  - Immunohistochemistry
MH  - In Vitro Techniques
MH  - Kinetics
MH  - Lens, Crystalline/metabolism
MH  - Ligands
MH  - Male
MH  - Microscopy, Immunoelectron
MH  - Molecular Sequence Data
MH  - Myelin P2 Protein/chemistry/genetics/*metabolism
MH  - *Neoplasm Proteins
MH  - Retina/*metabolism/ultrastructure
MH  - Sertoli Cells/metabolism
MH  - Skin/metabolism
MH  - Testis/*metabolism
MH  - *Tumor Suppressor Proteins
EDAT- 1998/04/02 00:00
MHDA- 1998/04/02 00:01
CRDT- 1998/04/02 00:00
PHST- 1998/04/02 00:00 [pubmed]
PHST- 1998/04/02 00:01 [medline]
PHST- 1998/04/02 00:00 [entrez]
AID - bi972520l [pii]
AID - 10.1021/bi972520l [doi]
PST - ppublish
SO  - Biochemistry. 1998 Mar 10;37(10):3250-7. doi: 10.1021/bi972520l.