Immunological studies of the uncoupling protein of brown adipose tissue

1985 ◽  
Vol 63 (2) ◽  
pp. 96-101 ◽  
Author(s):  
Michael Afong ◽  
Kimberley A. Olynyk ◽  
Hasmukh V. Patel ◽  
John Arnold ◽  
Shuen-Kuei Liao ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Uncoupling Protein ◽  
Mammalian Species ◽  
Cross Reactivity ◽  
Rabbit Antibody ◽  
Antibody Preparation ◽  
Brown Adipose ◽  
Immunological Relationship ◽  
Relationship Of

The immunological relationship of the uncoupling protein from brown adipose tissue of several mammalian species was examined by using a rabbit antibody preparation against the rat protein. Complete cross-reactivity of the antibody to the protein from hamster, mouse, and rat was found, whereas the protein from rabbit cross-reacted only 25%. Cross-reactivity was also found with the human uncoupling protein, although the human protein was found to be about 1 kdalton smaller than the rat protein. No protein of the size of the uncoupling protein was detected in several tumor cell lines examined.

Size analysis of uncoupling protein and its precursor from brown adipose tissue of different species

1985 ◽  
Vol 63 (9) ◽  
pp. 988-991 ◽  
Author(s):  
Karl B. Freeman ◽  
Karen Meyrick ◽  
Hasmukh V. Patel ◽  
Robert G. Ridley
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Uncoupling Protein ◽  
Mammalian Species ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Apparent Size ◽  
Size Analysis ◽  
Brown Adipose ◽  
Different Sources

The apparent size of the monomeric form of uncoupling protein from brown adipose tissue of several mammalian species was compared by sodium dodecyl sulfate – polyacrylamide gel electrophoresis. Including earlier results the apparent molecular mass of the protein from rat was about 32 000 daltons and varied about 1500–2000 daltons from the different sources with the size increasing in the order human < rat ≤ mouse ≤ hamster ≤ rabbit. The size of newly synthesized uncoupling protein was also found to vary among species. However in the two cases examined, rat and rabbit, the precursor and its respective mature monomeric protein had the same apparent size as shown by coelectrophoresis.

scholarly journals An immunological study of the uncoupling protein of brown adipose tissue mitochondria

1983 ◽  
Vol 210 (3) ◽  
pp. 859-866 ◽  
Author(s):  
D Ricquier ◽  
J P Barlet ◽  
J M Garel ◽  
M Combes-George ◽  
M P Dubois
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Uncoupling Protein ◽  
Cross Reactivity ◽  
Binding Activity ◽  
Immunological Study ◽  
Mitochondrial Membranes ◽  
Double Immunodiffusion ◽  
Brown Adipose ◽  
Antigen Antibody

1. Ewes were injected with purified 32,000-Mr uncoupling protein from mitochondria of brown adipose tissue of cold-adapted rats in order to raise antibodies. 2. The existence of antibodies in the plasma of ewes and the cross-reactivity of plasmas were demonstrated and studied by 125I-labelled antigen-antibody reaction, double immunodiffusion, the inhibition of GDP binding to the 32,000 Mr protein and by immunohistochemistry. 3. The antibodies raised against the homogeneous protein yielded a single immunoprecipitation band with detergent-solubilized mitochondrial membranes of brown adipose tissue from rat, hamster, guinea-pig, rabbit and with the purified uncoupling protein of these animals. No immunoprecipitation was obtained with the protein purified from brown adipose tissue of term lamb foetus. 4. The GDP-binding activity of the uncoupling protein (isolated or in solubilized membranes) was largely inhibited by the antiserum. 5. The anti-(rat uncoupling protein) could not cross-react with solubilized membranes from liver or muscle, nor with the purified beef heart or rat liver ADP/ATP translocator.

Immunochemical detection and quantitation of brown adipose tissue uncoupling protein

1987 ◽  
Vol 65 (3) ◽  
pp. 245-251 ◽  
Author(s):  
Mary F. Henningfield ◽  
Robert W. Swick
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Uncoupling Protein ◽  
Mammalian Species ◽  
Sodium Dodecyl ◽  
Mitochondrial Uncoupling ◽  
Immunochemical Method ◽  
Nucleotide Binding Sites ◽  
Mitochondrial Uncoupling Protein ◽  
Brown Adipose

A polyclonal antisera against rat brown adipose tissue mitochondrial uncoupling protein was used to examine mitochondrial samples from liver and white and brown adipose tissue from several mammalian species. A sodium dodecyl sulfate – polyacrylamide gel electrophoretic separation of proteins combined with an immunochemical method allowed for visualization of antigen–antibody complexes on nitrocellulose blots. Hamster, cavy, monkey, and mouse brown adipose tissue mitochondrial samples cross-reacted with the antisera. Mitochondria prepared from white fat obtained from young swine and sheep contained two closely migrating, antigenically active proteins. Hepatic mitochondria samples did not contain antigenically active protein. Reflectance densitometry was used for quantitation of the uncoupling protein in various mitochondrial samples. In rats fed diets low in protein, there appears to be a dissociation between the concentration of uncoupling protein and the number of nucleotide binding sites as given by the [3H]GDP binding assay. These results are indicative of a physiological activation of the uncoupling protein.

scholarly journals A single mutation in uncoupling protein of rat brown adipose tissue mitochondria abolishes GDP sensitivity of H+ transport.

1994 ◽  
Vol 269 (10) ◽  
pp. 7435-7438
Author(s):  
D.L. Murdza-Inglis ◽  
M. Modriansky ◽  
H.V. Patel ◽  
G. Woldegiorgis ◽  
K.B. Freeman ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Uncoupling Protein ◽  
Single Mutation ◽  
Brown Adipose

scholarly journals TAF7L modulates brown adipose tissue formation

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Haiying Zhou ◽  
Bo Wan ◽  
Ivan Grubisic ◽  
Tommy Kaplan ◽  
Robert Tjian
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Core Promoter ◽  
Uncoupling Protein ◽  
Dna Looping ◽  
Chromatin Interactions ◽  
Brown Adipose ◽  
Important Regulator

Brown adipose tissue (BAT) plays an essential role in metabolic homeostasis by dissipating energy via thermogenesis through uncoupling protein 1 (UCP1). Previously, we reported that the TATA-binding protein associated factor 7L (TAF7L) is an important regulator of white adipose tissue (WAT) differentiation. In this study, we show that TAF7L also serves as a molecular switch between brown fat and muscle lineages in vivo and in vitro. In adipose tissue, TAF7L-containing TFIID complexes associate with PPARγ to mediate DNA looping between distal enhancers and core promoter elements. Our findings suggest that the presence of the tissue-specific TAF7L subunit in TFIID functions to promote long-range chromatin interactions during BAT lineage specification.

KCTD10 regulates brown adipose tissue thermogenesis and metabolic function via Notch Signaling

2021 ◽  
Author(s):  
Mingsheng Ye ◽  
Liping Luo ◽  
Qi Guo ◽  
Guanghua Lei ◽  
Chao Zeng ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Notch Signaling ◽  
Molecular Mechanisms ◽  
Uncoupling Protein ◽  
Notch Signaling Pathway ◽  
Whole Body ◽  
Brown Adipocyte ◽  
Metabolic Function ◽  
Brown Adipose

Brown adipose tissue (BAT) is emerging as a target to beat obesity through the dissipation of chemical energy to heat. However, the molecular mechanisms of brown adipocyte thermogenesis remain to be further elucidated. Here, we show that KCTD10, a member of the polymerase delta-interacting protein 1 (PDIP1) family, was reduced in BAT by cold stress and a β3 adrenoceptor agonist. Moreover, KCTD10 level increased in the BAT of obese mice, and KCTD10 overexpression attenuates uncoupling protein 1 (UCP1) expression in primary brown adipocytes. BAT-specific KCTD10 knockdown mice had increased thermogenesis and cold tolerance protecting from high fat diet (HFD)-induced obesity. Conversely, overexpression of KCTD10 in BAT caused reduced thermogenesis, cold intolerance, and obesity. Mechanistically, inhibiting Notch signaling restored the KCTD10 overexpression suppressed thermogenesis. Our study presents that KCTD10 serves as an upstream regulator of notch signaling pathway to regulate BAT thermogenesis and whole-body metabolic function.

Sign in / Sign up

Export Citation Format

Share Document