2006
DOI: 10.1210/en.2005-1373
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Agouti-Related Protein Is Posttranslationally Cleaved by Proprotein Convertase 1 to Generate Agouti-Related Protein (AGRP)83–132: Interaction between AGRP83–132 and Melanocortin Receptors Cannot Be Influenced by Syndecan-3

Abstract: Agouti-related protein (AGRP) plays a key role in energy homeostasis. The carboxyl-terminal domain of AGRP acts as an endogenous antagonist of the melanocortin-4 receptor (MC4-R). It has been suggested that the amino-terminal domain of AGRP binds to syndecan-3, thereby modulating the effects of carboxyl-terminal AGRP at the MC4-R. This model assumes that AGRP is secreted as a full-length peptide. In this study we found that AGRP is processed intracellularly after Arg(79)-Glu(80)-Pro(81)-Arg(82). The processing… Show more

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Cited by 105 publications
(93 citation statements)
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“…Short hairpin RNA (ShRNA) constructs for furin and Ac45 were designed and tested by cotransfection with the corresponding cDNA. Efficient silencing of exogenous furin in ␤TC3 cells has been described previously (32) and silencing of Ac45 is shown in Fig. 5A.…”
Section: Ex Vivo Knockdown Of Furin and Ac45 Mimics The In Vivo Phenomentioning
confidence: 74%
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“…Short hairpin RNA (ShRNA) constructs for furin and Ac45 were designed and tested by cotransfection with the corresponding cDNA. Efficient silencing of exogenous furin in ␤TC3 cells has been described previously (32) and silencing of Ac45 is shown in Fig. 5A.…”
Section: Ex Vivo Knockdown Of Furin and Ac45 Mimics The In Vivo Phenomentioning
confidence: 74%
“…Regulated secretion experiments were performed essentially as described (8), except that cells were incubated overnight in nonsupplemented serum-free DMEM. Sample preparation and separation by SDS/PAGE have been described previously (32). For Western blotting (49), anti-FLAG antibody M2 (Sigma) was used.…”
Section: Cell Lines and Transfections See Si Materials And Methods Fmentioning
confidence: 99%
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“…However, the N-terminal sequences of Aisp and Agrp have undergone considerable sequence divergence since duplication. Indeed, a series of studies from our group, 73,76,77 and from White and colleagues, 78,79 reveal that the N-terminal domains of Asip and Agrp have evolved to serve very different functions. The N-terminal domain of Asip contains a glycosylation site and a high density of positively charged residues referred to as the 'basic region.'…”
Section: 75mentioning
confidence: 99%
“…First, the affinity of full-length Agrp for Mc4r is approximately 10-fold less than that of a C-terminal Agrp fragment; 73,78 second, full-length Agrp is post-translationally cleaved by a proprotein convertase such that the C-terminal domain is the active form in vivo. 78 By contrast, the active form of Asip in tissues is the full-length protein. 82 A summary of the similarities and differences in mechanisms of Asip and Agrp action are summarized in Figure 2a.…”
Section: 75mentioning
confidence: 99%