Adipocytokines: leptin - the classical, resistin - the controversical, adiponectin - the promising, and more to come

被引:348
作者
Koerner, A
Kratzsch, J
Kiess, W
机构
[1] Univ Leipzig, Univ Hosp Children & Adolescents, D-04317 Leipzig, Germany
[2] Univ Leipzig, Inst Lab Med Clin Chem & Mol Diagnost, Leipzig, Germany
关键词
adipocytokines; adiponectin; leptin; resistin; visfatin; adipose tissue; obesity;
D O I
10.1016/j.beem.2005.07.008
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
With the growing prevalence of obesity, scientific interest in the biology of adipose tissue has been extended to the secretory products of adipocytes, since they are increasingly shown to affect several aspects in the pathogenesis of obesity-related diseases. The cloning of the ob gene is consistent with this concept and suggests that body fat content in adult rodents is regulated by a negative feedback loop centred in the hypothalamus. In recent years, a number of additional signalling molecules secreted by adipose tissue have been discovered, commonly referred to as 'adipocytokines'. Among these, adiponectin is perhaps the most interesting and promising compound for the clinician since it has profound protective actions in the pathogenesis of diabetes and cardiovascular disease. Adiponectin is low in obese subjects and, in particular, insulin-resistant patients. In contrast, resistin seems to be of greater relevance in relation to the immune stress response than in the regulation of glucose homeostasis. However, inflammatory processes have recently been connected with the development of atherosclerosis. Finally, little is known regarding the clinical relevance of visfatin. Recent research has revealed many functions of adipocytokines extending far beyond metabolism, such as immunity, cancer and bone formation. This report aims to review some of the recent topics of adipocytokine research that may be of particular importance.
引用
收藏
页码:525 / 546
页数:22
相关论文
共 176 条
[31]   A mutation in the human leptin receptor gene causes obesity and pituitary dysfunction [J].
Clément, K ;
Vaisse, C ;
Lahlou, N ;
Cabrol, S ;
Pelloux, V ;
Cassuto, D ;
Gourmelen, M ;
Dina, C ;
Chambaz, J ;
Lacorte, JM ;
Basdevant, A ;
Bougneres, P ;
Lebouc, Y ;
Froguel, P ;
Guy-Grand, B .
NATURE, 1998, 392 (6674) :398-401
[32]   Variation in the resistin gene is associated with obesity and insulin-related phenotypes in Finnish subjects [J].
Conneely, KN ;
Silander, K ;
Scott, LJ ;
Mohlke, KL ;
Lazaridis, KN ;
Valle, TT ;
Tuomilehto, J ;
Bergman, RN ;
Watanabe, RM ;
Buchanan, TA ;
Collins, FS ;
Boehnke, M .
DIABETOLOGIA, 2004, 47 (10) :1782-1788
[33]   Leptin and the regulation of body weight [J].
Considine, RV ;
Caro, JF .
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 1997, 29 (11) :1255-1272
[34]   Serum immunoreactive leptin concentrations in normal-weight and obese humans [J].
Considine, RV ;
Sinha, MK ;
Heiman, ML ;
Kriauciunas, A ;
Stephens, TW ;
Nyce, MR ;
Ohannesian, JP ;
Marco, CC ;
McKee, LJ ;
Bauer, TL ;
Caro, JF .
NEW ENGLAND JOURNAL OF MEDICINE, 1996, 334 (05) :292-295
[35]   Binding of a pure 125I-monoiodoleptin analog to mouse tissues:: a developmental study [J].
Dal Farra, C ;
Zsürger, N ;
Vincent, JP ;
Cupo, A .
PEPTIDES, 2000, 21 (04) :577-587
[36]   Adipose tissue expression of the lipid droplet-associating proteins S3-12 and perilipin is controlled by peroxisome proliferator-activated receptor-γ [J].
Dalen, KT ;
Schoonjans, K ;
Ulven, SM ;
Weedon-Fekjaer, MS ;
Bentzen, TG ;
Koutnikova, H ;
Auwerx, J ;
Nebbl, HI .
DIABETES, 2004, 53 (05) :1243-1252
[37]   Apelin, a potent diuretic neuropeptide counteracting vasopressin actions through inhibition of vasopressin neuron activity and vasopressin release [J].
De Mota, N ;
Goazigo, ARL ;
El Messari, S ;
Chartrel, N ;
Roesch, D ;
Dujardin, C ;
Kordon, C ;
Vaudry, H ;
Moos, FO ;
Llorens-Cortes, C .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (28) :10464-10469
[38]   Regulation of adiponectin expression in human adipocytes:: Effects of adiposity, glucocorticoids, and tumor necrosis factor α [J].
Degawa-Yamauchi, M ;
Moss, KA ;
Bovenkerk, JE ;
Shankar, SS ;
Morrison, CL ;
Lelliott, CJ ;
Vidal-Puig, A ;
Jones, R ;
Considine, RV .
OBESITY RESEARCH, 2005, 13 (04) :662-669
[39]   Ligand-independent dimerization of the extracellular domain of the leptin receptor and determination of the stoichiometry of leptin binding [J].
Devos, R ;
Guisez, Y ;
VanderHeyden, J ;
White, DW ;
Kalai, M ;
Fountoulakis, M ;
Plaetinck, G .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (29) :18304-18310
[40]   Leptin inhibits bone formation through a hypothalamic relay: A central control of bone mass [J].
Ducy, P ;
Amling, M ;
Takeda, S ;
Priemel, M ;
Schilling, AF ;
Beil, FT ;
Shen, JH ;
Vinson, C ;
Rueger, JM ;
Karsenty, G .
CELL, 2000, 100 (02) :197-207