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  1. Article ; Online: Small Peptide, Large Implications: Endotrophin in Heart Failure with Preserved Ejection Fraction.

    Maya-Ramos, Lisandro / Scherer, Philipp E / de Lemos, James A

    Clinical chemistry

    2023  Volume 69, Issue 8, Page(s) 793–795

    MeSH term(s) Humans ; Stroke Volume ; Heart Failure ; Peptide Fragments ; Peptides ; Ventricular Function, Left
    Chemical Substances endotrophin ; Peptide Fragments ; Peptides
    Language English
    Publishing date 2023-02-04
    Publishing country England
    Document type Journal Article
    ZDB-ID 80102-1
    ISSN 1530-8561 ; 0009-9147
    ISSN (online) 1530-8561
    ISSN 0009-9147
    DOI 10.1093/clinchem/hvac211
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Programmed cell death along the midline axis patterns ipsilaterality in gastrulation.

    Maya-Ramos, Lisandro / Mikawa, Takashi

    Science (New York, N.Y.)

    2020  Volume 367, Issue 6474, Page(s) 197–200

    Abstract: Bilateral symmetry is the predominant body plan in the animal kingdom. Cells on the left and right sides remain compartmentalized on their ipsilateral side throughout life, but with occasional variation, as evidenced by gynandromorphs and human disorders. ...

    Abstract Bilateral symmetry is the predominant body plan in the animal kingdom. Cells on the left and right sides remain compartmentalized on their ipsilateral side throughout life, but with occasional variation, as evidenced by gynandromorphs and human disorders. How this evolutionarily conserved body plan is programmed remains a fundamental yet unanswered question. Here, we show that germ-layer patterning in avian gastrulation is ipsilateral despite cells undergoing highly invasive mesenchymal transformation and cell migration. Contralateral invasion is suppressed by extracellular matrix (ECM) and programmed cell death (PCD) along the embryonic midline. Ipsilateral gastrulation was lost by midline ECM and PCD inhibition but restored with exogenously induced PCD. Our data support ipsilaterality as an integral component of bilaterality and highlight a positive functional role of PCD in development.
    MeSH term(s) Animals ; Animals, Genetically Modified ; Apoptosis ; Cell Movement ; Chick Embryo ; Epithelial-Mesenchymal Transition ; Extracellular Matrix ; Gastrulation ; Green Fluorescent Proteins
    Chemical Substances Green Fluorescent Proteins (147336-22-9)
    Language English
    Publishing date 2020-01-08
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.aaw2731
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Induction of the Proepicardium.

    Maya-Ramos, Lisandro / Cleland, James / Bressan, Michael / Mikawa, Takashi

    Journal of developmental biology

    2013  Volume 1, Issue 2, Page(s) 82–91

    Abstract: The proepicardium is a transient extracardiac embryonic tissue that gives rise to the epicardium and a number of coronary vascular cell lineages. This important extracardiac tissue develops through multiple steps of inductive events, from specification ... ...

    Abstract The proepicardium is a transient extracardiac embryonic tissue that gives rise to the epicardium and a number of coronary vascular cell lineages. This important extracardiac tissue develops through multiple steps of inductive events, from specification of multiple cell lineages to morphogenesis. This article will review our current understanding of inductive events involved in patterning of the proepicardium precursor field, specification of cell types within the proepicardium, and their extension and attachment to the heart.
    Language English
    Publishing date 2013-07-08
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2720870-9
    ISSN 2221-3759
    ISSN 2221-3759
    DOI 10.3390/jdb1020082
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Role for high-glucose-induced protein O-GlcNAcylation in stimulating cardiac fibroblast collagen synthesis.

    Aguilar, Hugo / Fricovsky, Eduardo / Ihm, Sang / Schimke, Magdalena / Maya-Ramos, Lisandro / Aroonsakool, Nakon / Ceballos, Guillermo / Dillmann, Wolfgang / Villarreal, Francisco / Ramirez-Sanchez, Israel

    American journal of physiology. Cell physiology

    2014  Volume 306, Issue 9, Page(s) C794–804

    Abstract: Excess enzyme-mediated protein O-GlcNAcylation is known to occur with diabetes mellitus. A characteristic of diabetic cardiomyopathy is the development of myocardial fibrosis. The role that enhanced protein O-GlcNAcylation plays in modulating the ... ...

    Abstract Excess enzyme-mediated protein O-GlcNAcylation is known to occur with diabetes mellitus. A characteristic of diabetic cardiomyopathy is the development of myocardial fibrosis. The role that enhanced protein O-GlcNAcylation plays in modulating the phenotype of cardiac fibroblasts (CF) is unknown. To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells. Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels. The nuclear transcription factor Sp1 and arginase II evidence excess O-GlcNAcylation in HG cells. Expression in CF of an adenovirus coding for the enzyme N-acetylglucosaminidase, which removes O-GlcNAc moieties from proteins, decreased Sp1 and arginase II O-GlcNAcylation and restored HG-induced perturbations in CF back to NG levels. These findings may have important pathophysiological implications for the development of diabetes-induced cardiac fibrosis.
    MeSH term(s) Acetylglucosaminidase/genetics ; Acetylglucosaminidase/metabolism ; Animals ; Arginase/metabolism ; Cells, Cultured ; Collagen/biosynthesis ; Diabetic Cardiomyopathies/metabolism ; Diabetic Cardiomyopathies/pathology ; Fibroblasts/metabolism ; Fibroblasts/pathology ; Glucose/metabolism ; Glycosylation ; Male ; Myocardium/metabolism ; Myocardium/pathology ; Protein Processing, Post-Translational ; Rats ; Rats, Sprague-Dawley ; Signal Transduction ; Smad Proteins/metabolism ; Sp1 Transcription Factor/metabolism ; Time Factors ; Transfection ; Transforming Growth Factor beta1/metabolism ; Up-Regulation
    Chemical Substances Smad Proteins ; Sp1 Transcription Factor ; TGFB1 protein, human ; Transforming Growth Factor beta1 ; Collagen (9007-34-5) ; Acetylglucosaminidase (EC 3.2.1.52) ; Arg2 protein, rat (EC 3.5.3.1) ; Arginase (EC 3.5.3.1) ; arginase I, rat (EC 3.5.3.1) ; Glucose (IY9XDZ35W2)
    Language English
    Publishing date 2014-02-19
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 392098-7
    ISSN 1522-1563 ; 0363-6143
    ISSN (online) 1522-1563
    ISSN 0363-6143
    DOI 10.1152/ajpcell.00251.2013
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  5. Article ; Online: Excess protein O-GlcNAcylation and the progression of diabetic cardiomyopathy.

    Fricovsky, Eduardo S / Suarez, Jorge / Ihm, Sang-Hyun / Scott, Brian T / Suarez-Ramirez, Jorge A / Banerjee, Indroneal / Torres-Gonzalez, Moises / Wang, Hong / Ellrott, Irina / Maya-Ramos, Lisandro / Villarreal, Francisco / Dillmann, Wolfgang H

    American journal of physiology. Regulatory, integrative and comparative physiology

    2012  Volume 303, Issue 7, Page(s) R689–99

    Abstract: We examined the role that enzymatic protein O-GlcNAcylation plays in the development of diabetic cardiomyopathy in a mouse model of Type 2 diabetes mellitus (DM2). Mice injected with low-dose streptozotocin and fed a high-fat diet developed mild ... ...

    Abstract We examined the role that enzymatic protein O-GlcNAcylation plays in the development of diabetic cardiomyopathy in a mouse model of Type 2 diabetes mellitus (DM2). Mice injected with low-dose streptozotocin and fed a high-fat diet developed mild hyperglycemia and obesity consistent with DM2. Studies were performed from 1 to 6 mo after initiating the DM2 protocol. After 1 mo, DM2 mice showed increased body weight, impaired fasting blood glucose, and hyperinsulinemia. Echocardiographic evaluation revealed left ventricular diastolic dysfunction by 2 mo and O-GlcNAcylation of several cardiac proteins and of nuclear transcription factor Sp1. By 4 mo, systolic dysfunction was observed and sarcoplasmic reticulum Ca(2+) ATPase expression decreased by 50%. Fibrosis was not observed at any timepoint in DM2 mice. Levels of the rate-limiting enzyme of the hexosamine biosynthetic pathway, glutamine:fructose-6-phosphate amidotransferase (GFAT) were increased as early as 2 mo. Fatty acids, which are elevated in DM2 mice, can possibly be linked to excessive protein O-GlcNAcylation levels, as cultured cardiac myocytes in normal glucose treated with oleic acid showed increased O-GlcNAcylation and GFAT levels. These data indicate that the early onset of diastolic dysfunction followed by the loss of systolic function, in the absence of cardiac hypertrophy or fibrosis, is associated with increased cardiac protein O-GlcNAcylation and increased O-GlcNAcylation levels of key calcium-handling proteins. A link between excessive protein O-GlcNAcylation and cardiac dysfunction is further supported by results showing that reducing O-GlcNAcylation by O-GlcNAcase overexpression improved cardiac function in the diabetic mouse. In addition, fatty acids play a role in stimulating excess O-GlcNAcylation. The nature and time course of changes observed in cardiac function suggest that protein O-GlcNAcylation plays a mechanistic role in the triggering of diabetic cardiomyopathy in DM2.
    MeSH term(s) Animals ; Cells, Cultured ; Diabetes Mellitus, Experimental/chemically induced ; Diabetes Mellitus, Experimental/complications ; Diabetes Mellitus, Experimental/metabolism ; Diabetic Cardiomyopathies/metabolism ; Diabetic Cardiomyopathies/pathology ; Diabetic Cardiomyopathies/physiopathology ; Disease Models, Animal ; Disease Progression ; Echocardiography ; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)/metabolism ; Glycosylation ; Mice ; Mice, Inbred C57BL ; Myocytes, Cardiac/metabolism ; N-Acetylglucosaminyltransferases/metabolism ; Proteins/metabolism ; Streptozocin/adverse effects ; Ventricular Dysfunction, Left ; beta-N-Acetylhexosaminidases/metabolism
    Chemical Substances Proteins ; Streptozocin (5W494URQ81) ; N-Acetylglucosaminyltransferases (EC 2.4.1.-) ; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) (EC 2.6.1.16) ; hexosaminidase C (EC 3.2.1.50) ; beta-N-Acetylhexosaminidases (EC 3.2.1.52)
    Language English
    Publishing date 2012-08-08
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 603839-6
    ISSN 1522-1490 ; 0363-6119
    ISSN (online) 1522-1490
    ISSN 0363-6119
    DOI 10.1152/ajpregu.00548.2011
    Database MEDical Literature Analysis and Retrieval System OnLINE

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