Human heart tissue harvesting v1 (protocols.io.brsvm6e6)

protocols.io ◽  
2021 ◽  
Author(s):  
Marc Halushka
Keyword(s):  
Human Heart ◽  
Heart Tissue ◽  
Human Heart Tissue

Benefit of microwave-assisted acid hydrolysis of proteins for mass spectrometric profiling of the human heart tissue proteome

2007 ◽  
Vol 21 (16) ◽  
pp. 2779-2783 ◽  
Author(s):  
Mulu Gebremedhin ◽  
Hongying Zhong ◽  
Shaohua Wang ◽  
Michael Weinfeld ◽  
Liang Li
Keyword(s):  
Acid Hydrolysis ◽  
Human Heart ◽  
Heart Tissue ◽  
Mass Spectrometric ◽  
Microwave Assisted ◽  
Hydrolysis Of ◽  
Tissue Proteome ◽  
Human Heart Tissue

scholarly journals IMMUNOLOGIC RELATION OF STREPTOCOCCAL AND TISSUE ANTIGENS

1964 ◽  
Vol 119 (4) ◽  
pp. 651-666 ◽  
Author(s):  
Melvin H. Kaplan ◽  
Kathryn H. Svec
Keyword(s):  
Human Heart ◽  
Streptococcal Infection ◽  
Heart Tissue ◽  
Antigenic Determinants ◽  
Heat Inactivation ◽  
Prolonged Storage ◽  
Acute Glomerulonephritis ◽  
Streptococcal Antigen ◽  
Reactive Antibody ◽  
Human Heart Tissue

Sera from patients with recent streptococcal infection or non-suppurative sequelae exhibit with variable frequency a precipitin reaction in agar gel with a partially purified streptococcal antigen which has been shown previously to be immunologically related to human heart tissue. This precipitin could be absorbed from sera with normal human heart tissue homogenates but not with homogenates of other organs. Demonstration of this cross-reaction by heart absorption was found dependent both upon the serologic properties of individual sera and the nature or state of purification of the streptococcal product employed as test antigen. Evidence was obtained of a close association of heart-related and non-heart-related antigenic determinants in partially purified preparations of the streptococcal antigen by both gel diffusion and immunoelectrophoresis. On immunoelectrophoretic analysis, cross-reactive antigen exhibited a more rapid mobility toward the anode than M protein. It was destroyed by digestion with trypsin, pepsin, and chymotrypsin. Based on specific absorption tests with a Type 5 and Type 19 strain, the antigen was localized to cell walls and to a lesser extent to cell membranes of these strains. Precipitating activity related to cross-reactive antibody was localized to the immunoglobulin zone in immunoelectrophoresis. Reactive sera showed diminution or loss of serological activity following heat inactivation at 56°C or after prolonged storage at 4°C. Sera containing cross-reactive precipitating antibody exhibited an immunofluorescent reaction with sarcolemma of cardiac myofibers, which was inhibited by streptococcal cross-reactive antigen. By this inhibition test, the immunofluorescent reaction related to cross-reactive antibody could be distinguished from that due to other heart-reactive factors. Antibody to streptococcal cross-reactive antigen defined by precipitation-absorption tests was observed in 24 per cent of patients with recent history of uncomplicated streptococcal infection and in the majority of patients with acute rheumatic fever, rheumatic heart disease, or acute glomerulonephritis. It was observed rarely in patients with non-streptococcal related disease. These data provide evidence that induction of cross-reactive autoantibody to heart in certain individuals is associated with streptococcal infection.

scholarly journals Factors for C-Kit Expression in Cardiac Outgrowth Cells and Human Heart Tissue

2017 ◽  
Vol 58 (6) ◽  
pp. 962-968
Author(s):  
Satoshi Matsushita ◽  
Kazuo Minematsu ◽  
Taira Yamamoto ◽  
Hirotaka Inaba ◽  
Kenji Kuwaki ◽  
...  
Keyword(s):  
Human Heart ◽  
Heart Tissue ◽  
Human Heart Tissue

scholarly journals Chronotropic Responses of Human Heart Tissue Cultures

1972 ◽  
Vol 30 (6) ◽  
pp. 628-633 ◽  
Author(s):  
T. D. CHANG ◽  
G. R. CUMMING
Keyword(s):  
Human Heart ◽  
Heart Tissue ◽  
Tissue Cultures ◽  
Human Heart Tissue

Abstract 335: Titin Truncations in Human Heart Tissue

2019 ◽  
Vol 125 (Suppl_1) ◽  
Author(s):  
Quentin McAfee ◽  
Jeff Brandimarto ◽  
Joshua Rhoades ◽  
Ken Bede ◽  
Kenneth Margulies ◽  
...  
Keyword(s):  
Human Heart ◽  
Heart Tissue ◽  
Human Heart Tissue

Evidence of the Presence of Autoantibodies Specific for β1 Adrenergic Receptor in Failing Human Heart Tissue

2015 ◽  
Vol 21 (8) ◽  
pp. S30-S31
Author(s):  
Yuji Nagatomo ◽  
Christine S. Moravec ◽  
W. H. Wilson Tang
Keyword(s):  
Adrenergic Receptor ◽  
Human Heart ◽  
Heart Tissue ◽  
Human Heart Tissue

scholarly journals Bioengineering adult human heart tissue: How close are we?

2019 ◽  
Vol 3 (1) ◽  
pp. 010901 ◽  
Author(s):  
Richard J. Mills ◽  
James E. Hudson
Keyword(s):  
Human Heart ◽  
Heart Tissue ◽  
Adult Human ◽  
Human Heart Tissue

scholarly journals Localization of protective epitopes of the amino terminus of type 5 streptococcal M protein.

1986 ◽  
Vol 163 (5) ◽  
pp. 1191-1202 ◽  
Author(s):  
J B Dale ◽  
E H Beachey
Keyword(s):  
Human Heart ◽  
High Titer ◽  
Heart Tissue ◽  
M Protein ◽  
Amino Terminus ◽  
Particle Phase ◽  
Streptococcal M Protein ◽  
Elisa Inhibition ◽  
Subsequent Chemical ◽  
Human Heart Tissue

We have used a set of overlapping chemically synthesized peptides representing the amino terminus of type 5 streptococcal M protein to localize protective, as opposed to nonprotective and tissue-crossreactive epitopes that might be appropriate for vaccine formulations. Rabbit antisera raised against SM5(1-35) reacted in high titer with pep M5 by ELISA and opsonized type 5 streptococci. None of the antisera crossreacted with human heart tissue or myosin. Antisera against SM5(26-35) reacted with SM5(1-35) and pep M5 but failed to opsonize type 5 streptococci. Particle-phase ELISA indicated that SM5(26-35) antibodies were directed against nonprotective determinants of pep M5 that were not exposed on the surface of viable organisms. Opsonization and ELISA inhibition assays showed that, of the SM5(1-35) antibodies that reacted with M5, all were inhibited by SM5(14-35), whereas none was inhibited by SM5(26-35), suggesting that the protective epitopes of SM5(1-35) resided between residues 14 and 26. This was confirmed by subsequent chemical synthesis of this region; SM5(14-26) totally inhibited SM5(1-35) antibodies that reacted with pep M5 in ELISA, and completely inhibited opsonization of type 5 streptococci by SM5(1-35) antibodies. SM5(14-26) evoked high titers of type-specific, opsonic antibodies against type 5 streptococci, confirming the protective immunogenicity of this 13-residue peptide of type 5 M protein.

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