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@ARTICLE{Griffiths:93894,
      author       = {Griffiths, P. J. and Isackson, H. and Pelc, R. and Redwood,
                      C. S. and Funari, S. S. and Watkins, H. and Ashley, C. C.
                      and DESY},
      title        = {{S}ynchronous {I}n {S}itu {ATP}ase {A}ctivity, {M}echanics,
                      and ${C}a2^+$ {S}ensitivity of {H}uman and {P}orcine
                      {M}yocardium},
      journal      = {Biophysical journal},
      volume       = {97},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PHPPUBDB-11771},
      pages        = {2503-2512},
      year         = {2009},
      abstract     = {Flash-frozen myocardium samples provide a valuable means of
                      correlating clinical cardiomyopathies with abnormalities in
                      sarcomeric contractile and biochemical parameters. We
                      examined flash-frozen left-ventricle human cardiomyocyte
                      bundles from healthy donors to determine control parameters
                      for isometric tension (P(o)) development and Ca(2+)
                      sensitivity, while simultaneously measuring actomyosin
                      ATPase activity in situ by a fluorimetric technique. P(o)
                      was 17 kN m(-2) and $pCa(50\%)$ was 5.99 (28 degrees C, I =
                      130 mM). ATPase activity increased linearly with tension to
                      132 muM s(-1). To determine the influence of flash-freezing,
                      we compared the same parameters in both glycerinated and
                      flash-frozen porcine left-ventricle trabeculae. P(o) in
                      glycerinated porcine myocardium was 25 kN m(-2), and maximum
                      ATPase activity was 183 microM s(-1). In flash-frozen
                      porcine myocardium, P(o) was 16 kN m(-2) and maximum ATPase
                      activity was 207 microM s(-1). $pCa(50\%)$ was 5.77 in the
                      glycerinated and 5.83 in the flash-frozen sample. Both
                      passive and active stiffness of flash-frozen porcine
                      myocardium were lower than for glycerinated tissue and
                      similar to the human samples. Although lower stiffness and
                      isometric tension development may indicate flash-freezing
                      impairment of axial force transmission, we cannot exclude
                      variability between samples as the cause. ATPase activity
                      and $pCa(50\%)$ were unaffected by flash-freezing. The lower
                      ATPase activity measured in human tissue suggests a slower
                      actomyosin turnover by the contractile proteins.},
      keywords     = {Actomyosin: chemistry / Adenosine Triphosphatases:
                      chemistry / Adenosine Triphosphate: chemistry / Animals /
                      Biophysics: methods / Calcium: chemistry / Calcium:
                      metabolism / Fluorometry: methods / Glycerol: chemistry /
                      Humans / Hydrogen-Ion Concentration / Microscopy, Atomic
                      Force: methods / Myocardial Contraction / Myocardium:
                      metabolism / Myocardium: pathology / Myosins: chemistry /
                      Swine / Adenosine Triphosphate (NLM Chemicals) / Glycerol
                      (NLM Chemicals) / Calcium (NLM Chemicals) / Actomyosin (NLM
                      Chemicals) / Adenosine Triphosphatases (NLM Chemicals) /
                      Myosins (NLM Chemicals)},
      cin          = {HASYLAB},
      ddc          = {570},
      cid          = {$I:(DE-H253)HASYLAB_-2012_-20130307$},
      pnm          = {DORIS Beamline A2 (POF1-550)},
      pid          = {G:(DE-H253)POF1-A2-20130405},
      experiment   = {EXP:(DE-H253)D-A2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19883593},
      pmc          = {pmc:PMC2770627},
      UT           = {WOS:000271454000016},
      doi          = {10.1016/j.bpj.2009.07.058},
      url          = {https://bib-pubdb1.desy.de/record/93894},
}