Confocal microscopy should be able to clarify this point. Here, we show that the rex mutation, not located in the lipase domain of mPA-PLA1a, does not totally disrupt the lipase activity. It thus seems that the remaining activity is sufficient to produce down hair and nanified coarse hairs. Another noticeable point is that mPA-PLA1a, belonging to the pancreatic lipase family, needs a colipase to open and Deacetyl-ganoderic-acid-F activate its catalytic domain. The C-terminal region contains a motif which, when recognized by the colipase, allows it to match the lid domain. In silico protein structure prediction of both normal and mutant mPA-PLA1a rabbit protein suggests that the mutant protein is unable to match with the colipase. This could explain the decrease in the lipase activity. The 1362delA mutation could also affect the tertiary structure of the mPA-PLA1a and interfere with its cell membrane expected localization. The modeling indicates that the rex protein presents a destabilization of the C-terminal domain in comparison with the normal protein. The mutant mPA-PLA1a could thus present a default of localization, hampering normal activity. This is due to the fact that the deletion reduces but does not abolish the hair growth. Our rabbit mutant and normal phenotypes represent a most suitable model to better understand the function of LIPH in the hair growth and development process and should stimulate new investigative areas for human applications. Further investigations are needed to explore the mode of action of this gene in such a complex, but so instructive, mechanism of hair growth cycling. Tendons are fibrous tissues that provide attachment of Succinylsulfathiazole muscles to bone. The repetitive contraction and relaxation of muscles requires that tendons glide smoothly past adjacent tissues. The properties of the tendon surface that enable gliding and define the boundaries of the tissue are poorly understood. However, following tendon damage as a result of trauma, surgery, infection, and inflammatory disease, abnormal fibrous adhesions form between the tendon surface and overlying tissues.