Field- and Laboratory-derived Power-Cadence Profiles in World-Class and Elite Track Sprint Cyclists.

Previous investigations comparing Torque-Cadence (T-C) and Power-Cadence (P-C) profiles derived from seated and standing positions and field and laboratory conditions are not congruent with current methodological recommendations. Consequently, the aim of this investigation was to compare seated and standing T-C and P-C profiles generated from field and laboratory testing. Thirteen world-class and elite track sprint cyclists (n = 7 males, maximal power output (Pmax) = 2112 ± 395 W; n = 6 females, Pmax = 1223 ± 102 W) completed two testing sessions in which field- and laboratory-derived T-C and P-C profiles were identified. Standing P-C profiles had significantly (p < 0.05) greater Pmax than seated profiles, however there were no significant differences in optimal cadence (Fopt) between seated and standing positions. Pmax and Fopt were significantly lower in field-derived profiles in both positions compared to laboratory-derived profiles. However, there was no significant difference in the goodness-of-fit (R2) of the P-C profiles between laboratory (0.985 ± 0.02) and field-testing (0.982 ± 0.02) in each position. Valid T-C and P-C profiles can be constructed from field and laboratory protocols; however, the mechanical variables derived from the seated and standing and field and laboratory profiles cannot be used interchangeably. Both field and laboratory-derived profiles provide meaningful information and provide complementary insights into cyclists' capacity to produce power output.

The influence of cadence on fatigue during maximal sprint cycling in world-class and elite sprint cyclists.

Optimising cadence through appropriate gear selection is a key consideration for track sprint cycling performance, yet the influence of cadence on fatigue (i.e., decrement in power output) within a maximal sprint is not well understood. The aim of this study was to identify the influence of cadence on fatigue during maximal sprint cycling. Eleven world-class and elite track sprint cyclists (n = 6 men, maximal power output (Pmax) = 1894 ± 351 W, optimal cadence (Fopt) = 134 ± 8 rev∙min-1: n = 5 women, Pmax = 1114 ± 80 W, Fopt = 124 ± 8 rev∙min-1) completed two testing sessions where power-cadence profiles were constructed to determine the Fopt associated with Pmax. Cyclists also performed three maximal 15-s sprints (Fopt, ±15%Fopt) to identify fatigue per pedal stroke across these cadence ranges. There was no significant difference (p = 0.2) in the absolute fatigue per pedal stroke when cadence was fixed 15% above (16.7 ± 6.1 W∙stroke-1) and below (15.3 ± 5.1 W∙stroke-1) Fopt. Similarly, there was no significant difference in the relative fatigue per pedal stroke (% peak power∙stroke-1) across Fopt and ± 15%Fopt trials (p = 0.12). The relative decrement in power output is equivalent across the ± 15%Fopt cadence range. As such, a higher-geared, lower-cadence approach to maximal sprint cycling could be a viable method to minimise maximal pedal strokes and reduce the decrement in power output.

Cortactin: Coordinating adhesion and the actin cytoskeleton at cellular protrusions.

It has long been recognized that adhesion receptors cooperate with the cytoskeleton during morphogenesis, tissue remodeling and homeostasis. But how this occurs is less well-understood. A host of cytoskeletal regulators have been reported to have functional and biochemical linkage with adhesion receptors. The challenge remains to find functionally-coherent patterns within this increasingly large corpus of molecular information. In this review we discuss one approach, to identify distinctive functional modules that contribute to different adhesive processes. We illustrate this by considering Arp2/3-driven surface protrusion, which is utilized at both integrin-based cell-matrix adhesions and cadherin-based cell-cell adhesions. We further argue that regulatory proteins, such as cortactin, serve to coordinate the molecular components of this protrusive apparatus into a cohesive module.

Making and breaking contacts: the cellular biology of cadherin regulation.

Cadherin-mediated cell-cell interactions are dynamic processes, and cadherin function is tightly regulated in response to cellular context and signaling. Ultimately, cadherin regulation is likely to reflect the interplay between a range of fundamental cellular processes, including surface organization of receptors, cytoskeletal organization and cell trafficking, that are coordinated by signaling events. In this review we focus on recent advances in understanding how interplay with membrane trafficking and other cell-cell junctions can control cadherin function. The endocytosis of cadherins, and their post-internalization fate, influences surface expression and metabolic stability of these adhesion receptors. Similarly, at the surface, components of tight junctions provide a mode of cross-talk that regulates assembly of adherens junctions.

Myosin VI and vinculin cooperate during the morphogenesis of cadherin cell cell contacts in mammalian epithelial cells.

Cooperation between cadherins and the actin cytoskeleton controls many aspects of epithelial biogenesis. We report here that myosin VI critically regulates the morphogenesis of epithelial cell-cell contacts. As epithelial monolayers mature in culture, discontinuous cell-cell contacts are initially replaced by continuous (cohesive) contacts. Myosin VI is recruited to cell contacts as they become linear and cohesive, where it forms a biochemical complex with epithelial cadherin (E-cadherin). Myosin VI is necessary for strong cadherin adhesion, for cells to form cohesive linear contacts, and for the integrity of the apical junctional complex. We find that vinculin mediates this effect of myosin VI. Myosin VI is necessary for vinculin and E-cadherin to interact. A combination of gain and loss of function approaches identifies vinculin as a downstream effector of myosin VI that is necessary for the integrity of intercellular contacts. We propose that myosin VI and vinculin form a molecular apparatus that generates cohesive cell-cell contacts in cultured mammalian epithelia.

Dynamic microtubules regulate the local concentration of E-cadherin at cell-cell contacts.

In contrast to the well-established relationship between cadherins and the actin cytoskeleton, the potential link between cadherins and microtubules (MTs) has been less extensively investigated. We now identify a pool of MTs that extend radially into cell-cell contacts and are inhibited by manoeuvres that block the dynamic activity of MT plus-ends (e.g. in the presence of low concentrations of nocodazole and following expression of a CLIP-170 mutant). Blocking dynamic MTs perturbed the ability of cells to concentrate and accumulate E-cadherin at cell-cell contacts, as assessed both by quantitative immunofluorescence microscopy and fluorescence recovery after photobleaching (FRAP) analysis, but did not affect either transport of E-cadherin to the plasma membrane or the amount of E-cadherin expressed at the cell surface. This indicated that dynamic MTs allow cells to concentrate E-cadherin at cell-cell contacts by regulating the regional distribution of E-cadherin once it reaches the cell surface. Importantly, dynamic MTs were necessary for myosin II to accumulate and be activated at cadherin adhesive contacts, a mechanism that supports the focal accumulation of E-cadherin. We propose that this population of MTs represents a novel form of cadherin-MT cooperation, where cadherin adhesions recruit dynamic MTs that, in turn, support the local concentration of cadherin molecules by regulating myosin II activity at cell-cell contacts.