The content of arthrodial membrane glands in arthropods has seldom been studied. Here, we have analyzed the proteins of the arthrodial membrane gland of the trochanter-coxa articulation of the fourth pair of legs in the harvestman Mischonyx cuspidatus via reverse-phase high-performance liquid chromatography (RP-HPLC), polyacrylamide gel electrophoresis (PAGE), and nanoscale liquid chromatography coupled to mass spectrometry (nLC-MS/MS) analysis. Most of the fractions studied are hydrophobic, being proteins with molecular weights of ∼28, 62, and ∼198 kDa. These proteins seem to be homologous to proteins involved in product secretion, cytoskeleton, protein binding, cellular metabolism, and antimicrobial action among others. Lubricant function is also possible based on the literature. We were able to identify 147 proteins in the inner region, 91 proteins from the outer dorsal region, and 36 proteins from the outer ventral region. Some proteins are present only in one of these regions and some are shared by one or more regions. Our work provides, to the best of our knowledge, the first proteome characterization of the content of an arthrodial membrane gland in arachnids. Dataset Identifier: ftp://massive.ucsd.edu/MSV000087195/.
© 2021 The Authors. Published by American Chemical Society.