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/.