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Liverpool Can End English Soccer’s Cycle Of Embarrassment

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The Premier League has grossly underperformed on the biggest stage despite its riches.

By Tim Wigmore

Filed under Soccer

Clive Brunskill / Getty Images

The English Premier League is the richest football league on the planet. It has 14 of the 30 richest clubs in the world, according to an analysis that was published in January by consulting firm Deloitte . No other league boasts more than Italy’s five teams.

This suggests that Liverpool’s place in the UEFA Champions League semifinals — where it currently leads Roma 5-2 on aggregate — should come as no surprise. And yet, an English team still playing at this advanced phase of the tournament has become an anomaly. If Liverpool can hold off Roma on Wednesday, it will be the first English team to make the final in six seasons. That drought only underscores that for the top tier of English soccer, a seemingly bottomless pit of cash to spend on players has not translated into success. In recent years, the domination of the European superclubs — Barcelona, Bayern Munich and Real Madrid — has combined with the English clubs’ own failings to leave English teams floundering in the Champions League.

A decade ago, this wasn’t the case — the Premier League dominated in the Champions League. In the five seasons from 2004-05 to 2008-09, six of the 10 finalists were English, with four separate clubs — Arsenal, Chelsea, Liverpool and Manchester United — represented. The 2007-08 season was the apogee of English supremacy: Chelsea and Manchester United met in the final, Liverpool was in the semifinals, and Arsenal made it to the quarterfinals. The following season, English clubs again made up three of the four semifinalists.

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But since Manchester United lost the final to Barcelona in 2009, the Premier League’s hold over the Champions League has loosened. From 2009-10 to 2011-12, six English teams, out of a possible 12, reached the quarterfinals; only two — fewer than in each of 2008 and 2009 — reached the semifinals. The downtick in all-around EPL performance in the event was masked by Chelsea, which won the competition in 2012.

The Premier League is widely extolled as the best league in the world. Yet recent results suggest that in terms of the pure quality of its top teams, it has been left behind. In the six seasons since 2012-13, the Premier League has produced six Champions League quarterfinalists. Over that same time period, Spain’s La Liga has had 18 — three every single season — and 11 have subsequently reached the semifinals. Germany’s Bundesliga has produced 10 quarterfinalists.

Fig. 1.

An MSP fiber grown in vitro. Platinum replicas of MSP fibers show that the fibers are composed of a dense meshwork of MSP filaments. A plasma membrane-derived vesicle (lower left) is located at one end of the fiber and is the site of MSP filament addition. Bar, 500 μm.

View this table:
Table 1.

Effect of chemical manipulation of vesicles on fiber assembly

Both the vesicles that assemble fibers in vitro and the plasma membrane at the leading edge of the lamellipod of crawling sperm label with antiphosphotyrosine antibodies ( Fig. 2A ) (see Italiano et al., 1996 ). We found that a protein tyrosine phosphatase, YOP from Yersenia enterocolitica, blocked fiber assembly when added to S100 at 800 U/ml ( Fig. 2B ). When we added YOP together with 1 mM sodium orthovanadate, a potent inhibitor of tyrosine phosphatases ( Gordon, 1991 ), fiber assembly was rescued and the rate of fiber growth was indistinguishable from that in control extracts to which neither enzyme or inhibitor had been added. Western blot analysis using antiphosphotyrosine antibody showed that S100 contained a single major labeled band at M r ∼48 kDa. Labeling of this band could not be detected in S100 treated with YOP, but reappeared in samples treated with YOP plus orthovanadate ( Fig. 2C ). Moreover, antiphosphotyrosine detected this band in the vesicles harvested from S100 but not in the soluble cytosolic fraction ( Fig. 3A ). Thus, the vesicles from which fibers grow in the reconstituted motility system appear to require a 48 kDa integral membrane protein that requires tyrosine phosphorylation for activity.

Fig. 2.

Tyrosine phosphorylation is required for MSP polymerization. (A) Confocal fluorescence micrographs of a sperm (left) and a fiber assembled in vitro (right). Antiphosphotyrosine (green) labels the plasma membrane at the tips of fiber complexes in vivo and the vesicles of MSP fibers grown in vitro; both are sites of MSP cytoskeletal polymerization. The fiber complexes in the lamellipod and the fiber are stained with anti-MSP antibody (red). The antiphosphotyrosine fluorescence in the cell body is due to labeling of a mitochondrial enzyme, fumerate reductase, which contains phosphotyrosine residues. Bar, 1 μm. (B) The effect of the tyrosine phosphatase YOP on fiber assembly. The upper panel shows a phase contrast micrograph of fibers grown for 10 minutes in untreated S100. Addition of YOP to S100 (center panel) blocks assembly so that no fibers are detectable after 60 minutes. By contrast, the addition of YOP in the presence of sodium orthovanadate (bottom panel), a potent inhibitor of tyrosine phosphatases, restores the capacity of S100 to construct fibers. Bar, 10 μm. (C) The effect of YOP on protein tyrosine phosphorylation in S100 cell-free extract. The left lane shows a Coomassie-stained gel of S100. The right lanes show corresponding western blots probed with antiphosphotyrosine antibody. A single ∼48 kDa band is labeled in S100. This band is unlabeled in YOP-treated S100 but restored in S100 treated with YOP in the presence of sodium orthovanadate.

Fig. 3.

Only fractions that contain the 48 kDa phosphoprotein induce MSP polymerization. (A) Coomassie-stained gels and corresponding western blots probed with antiphosphotyrosine of the vesicle and cytosol fractions of S100. The 48 kDa protein (arrowhead) is detectable only in the vesicle fraction. (B) SEM of filaments assembled on addition of the detergent-solubilized extract of membrane vesicles to cytosol in the presence of ATP. No filaments were observed when the detergent-solubilized extract was omitted. (C) Coomassie-stained gel of fractions 36-42 obtained by gel filtration chromatography of CHAPS-solubilized vesicle components. A western blot probed with antiphosphotyrosine (anti-pY) of the region containing p48 is shown below. Fractions that triggered MSP polymerization when added to cytosol + ATP are indicated by `+'; fractions that yielded no detectable filament formation are designated `-'. (D) SEM of filaments assembled by the addition of fraction 39 to cytosol + ATP. Bars in B and D, 1 μm.

To isolate the 48 kDa protein (p48) from the membrane, we treated the vesicles with either 1% Triton X-100 or 10 mM CHAPS followed by centrifugation at 10,000 g for 5 minutes. Because the supernatant did not contain intact vesicles, this material failed to produce fibers when added back to cytosol. However, the membrane extract did induce the assembly of extensive meshworks of filaments, readily detectable by scanning electron microscopy (SEM), when recombined with cytosol ( Fig. 3B ) (see Italiano et al., 1996 ).