Dramatic enhancement of the specific expression of the heart-type fatty acid binding protein in rat brown adipose tissue by cold exposure

FEBS Letters ◽  
1997 ◽  
Vol 410 (2-3) ◽  
pp. 383-386 ◽  
Author(s):  
Takiko Daikoku ◽  
Yasuo Shinohara ◽  
Atsushi Shima ◽  
Naoshi Yamazaki ◽  
Hiroshi Terada
2004 ◽  
Vol 287 (5) ◽  
pp. R1132-R1140 ◽  
Author(s):  
Yourka D. Tchoukalova ◽  
Michael G. Sarr ◽  
Michael D. Jensen

To understand the significance of the reported depot differences in preadipocyte dynamics, we developed a procedure to identify committed preadipocytes in the stromovascular fraction of fresh human adipose tissue. We documented that adipocyte fatty acid binding protein (aP2) is expressed in human preadipocyte clones capable of replication, indicating that can be used as a marker of committed preadipocytes. Because aP2 expression can be induced in macrophages, stromovascular cells were also stained for the macrophage marker CD68. We found aP2+CD68− cells (designated as committed preadipocytes) that did not have lipid droplets (true preadipocytes) and that did have lipid droplets <6.5 μm in diameter (very immature adipocytes). Adipose tissue from subcutaneous, omental, and mesenteric depots was obtained from nine patients undergoing bariatric surgery for measurement of stromovascular cell number, the number of committed preadipocytes (aP2+CD68−), aP2+ macrophages (aP2+CD68+), and aP2− macrophages (aP2−CD68+). The number of committed preadipocytes did not differ significantly between depots but varied >20-fold among individuals. Total cell number, stromovascular cell number, and the number of aP2− macrophages was less ( P < 0.05) in subcutaneous than in omental fat (means ± SE, in millions: subcutaneous, 2.3 ± 0.3, 1.4 ± 0.3, and 0.17 ± 0.08; and omental, 4.8 ± 0.7, 3.8 ± 0.5, and 0.34 ± 0.06); mesenteric depot was intermediate. These data indicate that the cellular composition of adipose tissue varies between depots and between individuals. The ability to quantify committed preadipocytes in fresh adipose tissue should facilitate study of adipose tissue biology.


1990 ◽  
Vol 267 (2) ◽  
pp. 373-378 ◽  
Author(s):  
M K Armstrong ◽  
D A Bernlohr ◽  
J Storch ◽  
S D Clarke

Western-blot analysis using antiserum to 3T3-L1-cell fatty acid binding protein (FABP) revealed that pig adipose tissue contains a 15 kDa protein immunologically similar to the murine protein. This 15 kDa protein was purified from pig adipose tissue by sequential application of Sephadex G-50 gel filtration, cation exchange and covalent chromatography on Thiol-Sepharose-4B. The purity of the pig protein was established by two-dimensional polyacrylamide-gel electrophoresis. Isoelectric focusing indicated that the pig adipose FABP (a-FABP) exists with two charge isoforms (pI 5.1 and 5.2), both of which persist after delipidation. The N-terminus of the purified pig a-FABP was blocked; however, cleavage with CNBr allowed recovery of a 12-amino-acid peptide which was identical with the murine a-FABP sequence (residues 36-48) at 10 of 12 positions. The pig a-FABP bound 12-(9-anthroyloxy)oleic acid saturably and stoichiometrically, with an apparent dissociation constant of 1.0 microM. Northern-blot analysis using the cDNA for the murine 3T3-L1 FABP revealed that the pig a-FABP was expressed exclusively in adipose tissue.


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