PuSH - Publication Server of Helmholtz Zentrum München: Cleavage of the vaspin N-terminus releases cell-penetrating peptides that affect early stages of adipogenesis and inhibit lipolysis in mature adipocytes.

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Tindall, C.* ; Erkner, E.* ; Stichel, J.* ; Beck-Sickinger, A.G.* ; Hoffmann, A. ; Weiner, J.* ; Heiker, J.T.

Cleavage of the vaspin N-terminus releases cell-penetrating peptides that affect early stages of adipogenesis and inhibit lipolysis in mature adipocytes.

Adipocyte 10, 216-231 (2021)

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Vaspin expression and function is related to metabolic disorders and comorbidities of obesity. In various cellular and animal models of obesity, diabetes and atherosclerosis vaspin has shown beneficial, protective and/or compensatory action. While testing proteases for inhibition by vaspin, we noticed specific cleavage within the vaspin N-terminus and sequence analysis predicted cell-penetrating activity for the released peptides. These findings raised the question whether these proteolytic peptides exhibit biological activity.We synthesized various N-terminal vaspin peptides to investigate cell-penetrating activity and analyse uptake mechanisms. Focusing on adipocytes, we performed microarray analysis and functional assays to elucidate biological activities of the vaspin-derived peptide, which is released by KLK7 cleavage (vaspin residues 21-30; VaspinN). Our study provides first evidence that proteolytic processing of the vaspin N-terminus releases cell-penetrating and bioactive peptides with effects on adipocyte biology. The VaspinN peptide increased preadipocyte proliferation, interfered with clonal expansion during the early stage of adipogenesis and blunted adrenergic cAMP-signalling, downstream lipolysis as well as insulin signalling in mature adipocytes.Protease-mediated release of functional N-terminal peptides presents an additional facet of vaspin action. Future studies will address the mechanisms underlying the biological activities and clarify, if vaspin-derived peptides may have potential as therapeutic agents for the treatment of metabolic diseases.

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Publication type Article: Journal article

Document type Scientific Article

Corresponding Author

Keywords Adipose Tissue ; Internalization ; Kallikrein ; Obesity ; Proteolysis ; Serpin; Protein Transduction Domain; Adipose-tissue Inflammation; Mitotic Clonal Expansion; Heparan-sulfate; Kallikrein 7; Tat Protein; C Inhibitor; Beta-sheet; Hiv-1 Tat; Obesity

ISSN (print) / ISBN 2162-3945

e-ISSN 2162-397X

Journal Adipocyte

Quellenangaben Volume: 10, Issue: 1, Pages: 216-231

Publisher Landes Bioscience

Publishing Place 530 Walnut Street, Ste 850, Philadelphia, Pa 19106 Usa

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Helmholtz Institute for Metabolism, Obesity and Vascular Research (HI-MAG)

Grants Deutsche Forschungsgemeinschaft