Presence and characterization of glucagon-like peptide-1(7-36) amide receptors in solubilized membranes of rat adipose tissue.

We isolated from normal rat adipose tissue, by a Percoll-density-gradient procedure, two populations of adipocyte precursors. These preadipocytes undergo morphological and biochemical adipose conversion in primary culture. For full adipose conversion, these precursor cells, in addition to the adipogenic factor present in fetal-calf serum, require other effectors differentially. One population completes terminal differentiation in the presence of physiological concentrations of insulin. The second population requires a pre-sensitization with isobutylmethylxanthine at a critical period of the culture in order to respond to insulin. The fact that dibutyryl cyclic AMP could not be substituted for isobutylmethylxanthine suggests that the effect of the latter agent is not through its inhibition of particulate phosphodiesterase activity. These two populations further differ in their response to exogenously added haemin. Thus the existence of at least two developmentally regulated rat adipose-precursor compartments is demonstrated.

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Characterization of rat adipose tissue lipoprotein lipase using a monospecific antibody

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism ◽

10.1016/0005-2760(86)90026-3 ◽

1986 ◽

Vol 876 (3) ◽

pp. 399-412 ◽

Cited By ~ 4

Author(s):

Nadarajen A. Vydelingum ◽

Farouk AlQuadan ◽

Ahmed H. Kissebah ◽

Jacqueline Etienne

Keyword(s):

Adipose Tissue ◽

Lipoprotein Lipase ◽

Monospecific Antibody ◽

Rat Adipose Tissue ◽

Adipose Tissue Lipoprotein Lipase

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Dipeptidyl peptidases 8 and 9: specificity and molecular characterization compared with dipeptidyl peptidase IV

Biochemical Journal ◽

10.1042/bj20060079 ◽

2006 ◽

Vol 396 (2) ◽

pp. 391-399 ◽

Cited By ~ 64

Author(s):

Jais R. Bjelke ◽

Jesper Christensen ◽

Per F. Nielsen ◽

Sven Branner ◽

Anders B. Kanstrup ◽

...

Keyword(s):

Peptide Yy ◽

Expression System ◽

Baculovirus Expression System ◽

Dipeptidyl Peptidase ◽

Dipeptidyl Peptidase Iv ◽

Dipeptidyl Peptidases ◽

Glucagon Like Peptide ◽

Glucagon Like Peptide 1 ◽

Dipeptidyl Peptidase Iv Inhibition

Dipeptidyl peptidases 8 and 9 have been identified as gene members of the S9b family of dipeptidyl peptidases. In the present paper, we report the characterization of recombinant dipeptidyl peptidases 8 and 9 using the baculovirus expression system. We have found that only the full-length variants of the two proteins can be expressed as active peptidases, which are 882 and 892 amino acids in length for dipeptidyl peptidase 8 and 9 respectively. We show further that the purified proteins are active dimers and that they show similar Michaelis–Menten kinetics and substrate specificity. Both cleave the peptide hormones glucagon-like peptide-1, glucagon-like peptide-2, neuropeptide Y and peptide YY with marked kinetic differences compared with dipeptidyl peptidase IV. Inhibition of dipeptidyl peptidases IV, 8 and 9 using the well-known dipeptidyl peptidase IV inhibitor valine pyrrolidide resulted in similar Ki values, indicating that this inhibitor is non-selective for any of the three dipeptidyl peptidases.

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