| Title: | Protein-lipid Association in Lizard Chemical Signals |
| Author(s): | Mangiacotti M; Baeckens S; Fumagalli M; Martin J; Scali S; Sacchi R; |
| Address: | "Department of Earth and Environmental Sciences, University of Pavia, Via Taramelli 24, 27100 Pavia, Italy. Functional Morphology Lab, Department of Biology, University of Antwerp, Universiteitsplein 1, 2610 Wilrijk, Belgium. Evolution and Optics of Nanostructures Group, Department of Biology, Ghent University, 9000 Gent, Belgium. Department of Biology and Biotechnologies 'L. Spallanzani', University of Pavia, Via Ferrata 9, 27100 Pavia, Italy. Departamento de Ecologia Evolutiva, Museo Nacional de Ciencias Naturales, CSIC, Jose Gutierrez Abascal 2, E-28006 Madrid, Spain. Sezione Erpetologia, Museo di Storia Naturale di Milano, Corso Venezia 55, IT-20121 Milano, Italy" |
| ISSN/ISBN: | 2517-4843 (Electronic) 2517-4843 (Linking) |
| Abstract: | "Chemical communication in terrestrial vertebrates is often built on complex blends, where semiochemical and structural compounds may form an integrated functional unit. In lizards, many species have specialized epidermal glands whose secretions are waxy, homogeneous blends of lipids and proteins, both active in communication. The intimate co-occurrence of such compounds allows us to hypothesize that they should undergo a certain degree of covariation, considering both their semiochemical role and the support-to-lipid function hypothesized for the protein fraction. In order to assess the occurrence and level of protein-lipid covariation, we compared the composition and complexity of the two fractions in the femoral gland secretions of 36 lizard species, combining phylogenetically-informed analysis with tandem mass spectrometry. We found the composition and complexity of the two fractions to be strongly correlated. The composition of the protein fraction was mostly influenced by the relative proportion of cholestanol, provitamin D(3), stigmasterol, and tocopherol, while the complexity of the protein pattern increased with that of lipids. Additionally, two identified proteins (carbonic anhydrase and protein disulfide isomerase) increased their concentration as provitamin D(3) became more abundant. Although our approach does not allow us to decrypt the functional relations between the proteinaceous and lipid components, nor under the semiochemical or structural hypothesis, the finding that the proteins involved in this association were enzymes opens up to new perspectives about protein role: They may confer dynamic properties to the blend, making it able to compensate predictable variation of the environmental conditions. This may expand the view about proteins in the support-to-lipid hypothesis, from being a passive and inert component of the secretions to become an active and dynamic one, thus providing cues for future research" |
| Notes: | "PubMed-not-MEDLINEMangiacotti, M Baeckens, S Fumagalli, M Martin, J Scali, S Sacchi, R eng England 2023/05/25 Integr Org Biol. 2023 May 8; 5(1):obad016. doi: 10.1093/iob/obad016. eCollection 2023" |
