Comparing functional outcomes in minimally invasive versus open inguinal hernia repair using the army physical fitness test.

PURPOSE: The advantages of minimally invasive inguinal hernia repair (MIHR) over open hernia repair (OHR) continue to be debated. We compared MIHR to OHR by utilizing the Army Physical Fitness Test (APFT) as an outcome measure. METHODS: The APFT is a three-component test scored on a normalized 300 point scale taken semiannually by active-duty military. We identified 1119 patients who met inclusion criteria: 588 in the OHR group and 531 in the MIHR group. Changes in APFT scores, time on post-operative duty restrictions (military profile), and time interval to first post-operative APFT were compared using regression analysis. RESULTS: Postoperatively, no APFT score change difference was observed between the OHR or MIHR groups (- 7.3 ± 30 versus - 5.5 ± 27.7, p = 0.2989). Service members undergoing OHR and MIHR underwent their first post-operative APFT at equal mean timeframes (6.6 ± 5 months versus 6.7 ± 5.1, p = 0.74). No difference was observed for time in months spent on an official temporary duty restriction (military profile) for either OHR or MIHR (0.16 ± 0.16 versus 0.15 ± 0.17, p = 0.311). On adjusted regression analysis, higher pre-operative APFT scores and BMI ≥ 30 were independently associated with reduction in post-operative APFT scores. Higher-baseline APFT scores were independently associated with less time on a post-operative profile, whereas higher BMI (≥ 30) and lower rank were independently associated with longer post-operative profile duration. Higher-baseline APFT scores and lower rank were independently associated with shorter time intervals to the first post-operative APFT. CONCLUSION: Overall, no differences in post-operative APFT scores, military profile time, or time to first post-operative APFT were observed between minimally invasive or open hernioplasty in this military population.

A chlamydial type III translocated protein is tyrosine-phosphorylated at the site of entry and associated with recruitment of actin.

The obligate intracellular bacterium Chlamydia trachomatis rapidly induces its own entry into host cells. Initial attachment is mediated by electrostatic interactions to heparan sulfate moieties on the host cell, followed by irreversible binding to an unknown secondary receptor. This secondary binding leads to the recruitment of actin to the site of attachment, formation of an actin-rich, pedestal-like structure, and finally internalization of the bacteria. How chlamydiae induce this process is unknown. We have identified a high-molecular-mass tyrosine-phosphorylated protein that is rapidly phosphorylated on attachment to the host cell. Immunoelectron microscopy studies revealed that this tyrosine-phosphorylated protein is localized to the cytoplasmic face of the plasma membrane at the site of attachment of surface-associated chlamydiae. The phosphoprotein was isolated by immunoprecipitation with the antiphosphotyrosine antibody 4G10 and identified as the chlamydial protein CT456, a hypothetical protein with unknown function. The chlamydial protein (Tarp) appears to be translocated into the host cell by type III secretion because it is exported in a Yersinia heterologous expression assay. Phosphotyrosine signaling across the plasma membrane preceded the recruitment of actin to the site of chlamydial attachment and may represent the initial signal transduced from pathogen to the host cell. These results suggest that C. trachomatis internalization is mediated by a chlamydial type III-secreted effector protein.

NF-kappa B-dependent inhibition of apoptosis is essential for host cellsurvival during Rickettsia rickettsii infection.

The possibility that bacteria may have evolved strategies to overcome host cell apoptosis was explored by using Rickettsia rickettsii, an obligate intracellular Gram-negative bacteria that is the etiologic agent of Rocky Mountain spotted fever. The vascular endothelial cell, the primary target cell during in vivo infection, exhibits no evidence of apoptosis during natural infection and is maintained for a sufficient time to allow replication and cell-to-cell spread prior to eventual death due to necrotic damage. Prior work in our laboratory demonstrated that R. rickettsii infection activates the transcription factor NF-kappa B and alters expression of several genes under its control. However, when R. rickettsii-induced activation of NF-kappa B was inhibited, apoptosis of infected but not uninfected endothelial cells rapidly ensued. In addition, human embryonic fibroblasts stably transfected with a superrepressor mutant inhibitory subunit Ikappa B that rendered NF-kappa B inactivatable also underwent apoptosis when infected, whereas infected wild-type human embryonic fibroblasts survived. R. rickettsii, therefore, appeared to inhibit host cell apoptosis via a mechanism dependent on NF-kappa B activation. Apoptotic nuclear changes correlated with presence of intracellular organisms and thus this previously unrecognized proapoptotic signal, masked by concomitant NF-kappa B activation, likely required intracellular infection. Our studies demonstrate that a bacterial organism can exert an antiapoptotic effect, thus modulating the host cell's apoptotic response to its own advantage by potentially allowing the host cell to remain as a site of infection.