Lisfranc injury in a national hockey league player: a case report.

Tarsometatarsal joint dislocations and fracture-dislocations are uncommon injuries most frequently resulting from high-energy trauma as encountered in crush injuries, falls, and motor vehicle accidents. Although less common in athletes, this injury is being recognized with greater frequency and may carry a poor prognosis for return to high levels of competition. These injuries present a considerable challenge to orthopedic surgeons caring for athletes because of the prolonged period of recovery often required [ 1,2,5,6,12]. The literature contains descriptions of this injury in football players, gymnasts, tennis players, and track and field athletes [2,5,9]. To our knowledge, no report of such a Lisfranc injury to a hockey player has been described. This is a case report of a National Hockey League player that sustained a Lisfranc injury requiring surgical stabilization, but was able to return to elite hockey play.

Functional characterization of Pactolus, a beta-integrin-like protein preferentially expressed by neutrophils.

Murine Pactolus is a beta-integrin-like molecule expressed exclusively on the surface of granulocytes. Cell surface expression of Pactolus is dramatically increased following activation of bone marrow neutrophils with known agonists, and cross-linking of cell surface Pactolus, suggesting the bulk of the protein is in intracellular stores. The mature protein is found in two forms depending upon the extent of N-linked glycosylation. There is no evidence to suggest that Pactolus requires an associated alpha chain for expression. In some mouse strains, a truncated form of the protein is predicted based upon alternative splicing: this form, however, is unstable and rapidly degraded after synthesis. Differences in the quantities of these Pactolus mRNA isoforms have defined two alleles. BALB/c and C3H/HeJ mice possess allele B and preferentially express the truncated, unstable product, whereas C57BL/6 mice possess allele A and only produce the membrane-bound form. Sequence analysis has shown the difference between these two alleles is due to a single base pair difference at the splice acceptor site for the truncated product. The increased expression of the membrane form of Pactolus by granulocytes of C57BL/6 mice suggests a compensatory adhesion function that is reduced in cells from the low producing strains.