Spectroscopic fluorescence measurements of lamb and human heart tissue in vitro

2003 ◽  
Author(s):  
George Filippidis ◽  
Giannis Zacharakis ◽  
G. E. Kochiadakis ◽  
S. I. Chrysostomakis ◽  
P. E. Vardas ◽  
...  
Keyword(s):  
Human Heart ◽  
Heart Tissue ◽  
Fluorescence Measurements ◽  
Human Heart Tissue

Abstract MP143: Harnessing Glycomics to Understand Cardiac Biology and Disease

2020 ◽  
Vol 127 (Suppl_1) ◽  
Author(s):  
Christopher Ashwood ◽  
Linda Berg Luecke ◽  
Rebekah L Gundry
Keyword(s):  
Human Heart ◽  
Heart Function ◽  
Heart Tissue ◽  
Cardiac Biomarkers ◽  
Tissue Homogenate ◽  
Glycan Structure ◽  
Cell Type ◽  
Cell Type Specific ◽  
Human Heart Tissue

Cell surface glycoproteins play critical roles in maintaining cardiac structure and function, and the glycan-moiety attached to a protein is critical for proper protein folding, stability, and signaling. Despite mounting evidence that glycan structures are key modulators of heart function and must be considered when developing cardiac biomarkers, we currently do not have a comprehensive view of the glycans present in the normal human heart. Here, we used an innovative mass spectrometry approach to generate the first glycan structure libraries for primary human heart tissue, cardiomyocytes (CM) enriched from human heart tissue, and human induced pluripotent stem cell derived CM (hiPSC-CM), containing >260 N- and O- glycans. Comparing the glycome of CM enriched from primary heart tissue to that of heart tissue homogenate, 21 structures significantly differed, and the high mannose class is increased in enriched CM. Moreover, >30% of the glycome significantly changed across 20-100 days of in vitro differentiation, and only 23% of the N -glycan structures were shared between hiPSC-CM and primary CM. Overall, these observations are an important complement to genomic, transcriptomic, and proteomic profiling and reveal new considerations for the use and interpretation of hiPSC-CM models for studies of human development, disease, and drug testing. These data are also expected to aid in the evaluation of the immunogenic potential of hiPSC-CM for transplantation. Finally, harnessing differences observed between immature, proliferative hiPSC-CM and adult primary CM may be exploited to drive in vitro differentiation towards a more mature phenotype. Building on these data, current efforts are underway to develop chamber- and cell-type specific views ( e.g. cardiomyocytes, fibroblasts) of the glycome in the healthy and failing human heart. Such analyses provide a key link to understand the role glycosylation plays in cell-type specific functions and cardiac disease. The structural differences observed here, either among cell types or stages of differentiation, require complex regulation of multiple enzymes in the biosynthetic pathway, and therefore would be challenging to measure with antibody arrays, RNAseq, or proteomics. Therefore, continued application of structure-based glycomics approaches, such as the method used here, will be essential for elucidating the roles that glycans and glycoproteins play during developmental and disease processes in the human heart.

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

scholarly journals Membranes for Modelling Cardiac Tissue Stiffness In Vitro Based on Poly(trimethylene carbonate) and Poly(ethylene glycol) Polymers

Membranes ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 274 ◽  
Author(s):  
Iris Allijn ◽  
Marcelo Ribeiro ◽  
André Poot ◽  
Robert Passier ◽  
Dimitrios Stamatialis
Keyword(s):  
Ethylene Glycol ◽  
Human Heart ◽  
Cardiac Tissue ◽  
Heart Tissue ◽  
Trimethylene Carbonate ◽  
Tissue Stiffness ◽  
Poly Ethylene Glycol ◽  
Young’S Moduli ◽  
Poly Ethylene

Despite the increased expenditure of the pharmaceutical industry on research and development, the number of drugs for cardiovascular diseases that reaches the market is decreasing. A major issue is the limited ability of the current in vitro and experimental animal models to accurately mimic human heart disease, which hampers testing of the efficacy of potential cardiac drugs. Moreover, many non-heart-related drugs have severe adverse cardiac effects, which is a major cause of drugs’ retraction after approval. A main hurdle of current in vitro models is their inability to mimic the stiffness of in vivo cardiac tissue. For instance, poly(styrene) petri dishes, which are often used in these models, have a Young’s modulus in the order of GPa, while the stiffness of healthy human heart tissue is <50 kPa. In pathological conditions, such as scarring and fibrosis, the stiffness of heart tissue is in the >100 kPa range. In this study, we focus on developing new membranes, with a set of properties for mimicry of cardiac tissue stiffness in vitro, based on methacrylate-functionalized macromers and triblock-copolymers of poly(trimethylene carbonate) and poly(ethylene glycol). The new membranes have Young’s moduli in the hydrated state ranging from 18 kPa (healthy tissue) to 2.5 MPa (pathological tissue), and are suitable for cell contraction studies using human pluripotent stem-cell-derived cardiomyocytes. The membranes with higher hydrophilicity have low drug adsorption and low Young’s moduli and could be suitable for drug screening applications.

scholarly journals Bacterial Immunoglobulin Superantigen Proteins A and L Activate Human Heart Mast Cells by Interacting with Immunoglobulin E

2000 ◽  
Vol 68 (10) ◽  
pp. 5517-5524 ◽  
Author(s):  
Arturo Genovese ◽  
Jean-Pierre Bouvet ◽  
Giovanni Florio ◽  
Bärbel Lamparter-Schummert ◽  
Lars Björck ◽  
...  
Keyword(s):  
Mast Cells ◽  
Human Heart ◽  
Immunoglobulin E ◽  
Protein A ◽  
Surface Protein ◽  
Heart Tissue ◽  
Protein L ◽  
Cysteinyl Leukotriene ◽  
Proinflammatory Mediators

ABSTRACT Human heart mast cells (HHMC) have been identified in heart tissue, perivascularly, and in the intima of coronary arteries. In vitro activation of isolated HHMC induces the release of vasoactive and proinflammatory mediators (histamine, tryptase, and cysteinyl leukotriene C4 [LTC4]). We investigated the effects of several bacterial proteins on HHMC activation in vitro. HHMC released histamine, tryptase, and LTC4 in response toStaphylococcus aureus Cowan 1 and the immunoglobulin (Ig)-binding protein A, but not to S. aureus Wood 46, which does not synthesize protein A. The effect of protein A was inhibited by preincubation with monoclonal IgM VH3+. Some strains of Peptostreptococcus magnus express an Ig light chain-binding surface protein called protein L. Such bacteria and soluble protein L stimulated the release of preformed and newly synthesized mediators from HHMC. Preincubation of HHMC with either protein A or protein L resulted in complete cross-desensitization to a subsequent challenge with the heterologous stimulus or anti-IgE. Monoclonal IgE (κ chains) blocked protein L-induced release, whereas IgE (λ chains) had no effect. Streptococcal protein G, formyl-containing tripeptide, and pepstatin A did not activate HHMC. Bacterial products protein A and protein L and intact bacteria (S. aureus and P. magnus) activate HHMC by acting as Ig superantigens.

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