| First Author | Cassina V | Year | 2013 |
| Journal | Biochim Biophys Acta | Volume | 1828 |
| Issue | 2 | Pages | 455-60 |
| PubMed ID | 23122777 | Mgi Jnum | J:198867 |
| Mgi Id | MGI:5499680 | Doi | 10.1016/j.bbamem.2012.10.023 |
| Citation | Cassina V, et al. (2013) Biophysical characterization of a binding site for TLQP-21, a naturally occurring peptide which induces resistance to obesity. Biochim Biophys Acta 1828(2):455-60 |
| abstractText | Recently, we demonstrated that TLQP-21 triggers lipolysis and induces resistance to obesity by reducing fat accumulation [1]. TLQP-21 is a 21 amino acid peptide cleavage product of the neuroprotein VGF and was first identified in rat brain. Although TLQP-21 biological activity and its molecular signaling is under active investigation, a receptor for TLQP-21 has not yet been characterized. We now demonstrate that TLQP-21 stimulates intracellular calcium mobilization in CHO cells. Furthermore, using Atomic Force Microscopy (AFM), we also provide evidence of TLQP-21 binding-site characteristics in CHO cells. AFM was used in force mapping mode equipped with a cantilever suitably functionalized with TLQP-21. Attraction of this functionalized probe to the cell surface was specific and consistent with the biological activity of TLQP-21; by contrast, there was no attraction of a probe functionalized with biologically inactive analogues. We detected interaction of the peptide with the binding-site by scanning the cell surface with the cantilever tip. The attractive force between TLQP-21 and its binding site was measured, statistically analyzed and quantified at approximately 40 pN on average, indicating a single class of binding sites. Furthermore we observed that the distribution of these binding sites on the surface was relatively uniform. |
