Publications
228 results found
TOWNSEND PJ, FARZA H, MACGEOCH C, et al., 1994, HUMAN CARDIAC TROPONIN-T - IDENTIFICATION OF FETAL ISOFORMS AND ASSIGNMENT OF THE TNNT2 LOCUS TO CHROMOSOME 1Q, GENOMICS, Vol: 21, Pages: 311-316, ISSN: 0888-7543
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- Citations: 66
BARTON PJR, THOMPSON RP, ROBERT B, et al., 1994, EXPRESSION OF HOMEOBOX GENES MSX-1 AND MSX-2 DURING CARDIAC DEVELOPMENT, FASEB JOURNAL, Vol: 8, Pages: A264-A264, ISSN: 0892-6638
CHANTHOMAS PS, THOMPSON RP, ROBERT B, et al., 1993, EXPRESSION OF HOMEOBOX GENES MSX-1 (HOX-7) AND MSX-2 (HOX-8) DURING CARDIAC DEVELOPMENT IN THE CHICK, DEVELOPMENTAL DYNAMICS, Vol: 197, Pages: 203-216, ISSN: 1058-8388
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- Citations: 145
SASSE S, BRAND NJ, KYPRIANOU P, et al., 1993, TROPONIN-I GENE-EXPRESSION DURING HUMAN CARDIAC DEVELOPMENT AND IN END-STAGE HEART-FAILURE, CIRCULATION RESEARCH, Vol: 72, Pages: 932-938, ISSN: 0009-7330
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- Citations: 197
Grimaldi K, Horn DA, Hudson LD, et al., 1993, Expression of the SmN splicing protein is developmentally regulated in the rodent brain but not in the rodent heart., Dev Biol, Vol: 156, Pages: 319-323, ISSN: 0012-1606
The SmN protein is a tissue-specific splicing factor which is closely related to the ubiquitous SmB splicing protein but which is expressed only in the adult brain and heart. SmN is also detectable albeit at a low level in both the embryonic brain and heart. During heart development, SmN levels remain constant while during rodent brain development the levels of SmN rise such that SmN replaces SmB as the predominant protein in adult brain. This increase in SmN levels is dependent upon a corresponding increase in the SmN mRNA which is detectable by in situ hybridization within neurons in virtually all areas of the adult brain.
CHANTHOMAS PS, THOMPSON RP, ROBERT B, et al., 1993, EXPRESSION OF HOMEOBOX GENES MSX-1 (HOX-7) AND MSX-2 (HOX-8) DURING CARDIAC DEVELOPMENT IN THE CHICK, JOURNAL OF CELLULAR BIOCHEMISTRY, Pages: 209-209, ISSN: 0730-2312
BARTON PJR, BHAVSAR P, BRAND NJ, et al., 1993, TROPONIN GENE-EXPRESSION IN THE DEVELOPING HUMAN HEART, JOURNAL OF CELLULAR BIOCHEMISTRY, Pages: 227-227, ISSN: 0730-2312
Arai M, Alpert NR, MacLennan DH, et al., 1993, Alterations in sarcoplasmic reticulum gene expression in human heart failure. A possible mechanism for alterations in systolic and diastolic properties of the failing myocardium., Circ Res, Vol: 72, Pages: 463-469, ISSN: 0009-7330
Recent studies have shown that intracellular Ca2+ handling is abnormal in the myocardium of patients with end-stage heart failure. Muscles from the failing hearts showed a prolonged Ca2+ transient and a diminished capacity to restore a low resting Ca2+ level during diastole. Accordingly, we examined whether this defect in Ca2+ transport function is due to alterations in sarcoplasmic reticulum gene expression. We determined the messenger RNA (mRNA) levels of sarcoplasmic reticulum Ca2+ transport proteins in failing human hearts from 17 cardiac transplant recipients with a diagnosis of dilated cardiomyopathy, primary pulmonary hypertension, or ischemic heart disease. The expression levels of each mRNA were compared with each other and then correlated with that of atrial natriuretic factor (ANF) mRNA in the failing ventricle. The mRNA levels for the calcium release channel (ryanodine receptor, RYR2), Ca2+ uptake pump (Ca(2+)-ATPase, SERCA2 isoform), and phospholamban differed significantly between heart samples but showed an inverse relation with that of ventricular ANF mRNA. In contrast, calsequestrin mRNA levels remained unchanged in these failing hearts. In addition, beta-myosin and alpha-cardiac actin mRNA levels also showed an inverse relation with ANF mRNA levels. These changes were observed in both right and left ventricles of hearts with congestive heart failure due to dilated cardiomyopathy, primary pulmonary hypertension, or ischemic heart disease. The results are consistent with the hypothesis that abnormal calcium handling in the sarcoplasmic reticulum of failing hearts is due to the altered expression of the genes encoding sarcoplasmic reticulum proteins.
BRAND NJ, DABHADE N, BHAVSAR PK, et al., 1993, IDENTIFICATION OF ZINC FINGER AND SRY-LIKE TRANSCRIPTION FACTORS EXPRESSED IN HUMAN HEART, JOURNAL OF CELLULAR BIOCHEMISTRY, Pages: 190-190, ISSN: 0730-2312
BHAVSAR PK, BRAND NJ, YACOUB MH, et al., 1993, THE HUMAN CARDIAC TROPONIN-I GENE - A MODEL FOR CARDIAC-SPECIFIC REGULATION, JOURNAL OF CELLULAR BIOCHEMISTRY, Pages: 189-189, ISSN: 0730-2312
Hailstones D, Barton P, Chan-Thomas P, et al., 1992, Differential regulation of the atrial isoforms of the myosin light chains during striated muscle development., J Biol Chem, Vol: 267, Pages: 23295-23300, ISSN: 0021-9258
We have isolated a cDNA that encodes the human regulatory myosin light chain isoform predominant in adult atrial muscle. The cDNA contains an open reading frame of 175 amino acids and encodes a hydrophilic protein of a largely helical structure with two potential phosphorylation sites. The protein is different from any other regulatory myosin light chain so far described and is the product of a previously uncharacterized single copy gene. An isoform-specific probe was used to analyze the expression of this isoform in adult muscle and in cardiac and skeletal muscle development in vivo and in vitro. Parallel analysis of the corresponding human alkali myosin light chain (predominant in adult atrium) showed that both isoforms are expressed in early heart development, in both atrium and ventricle. Although the atrial alkali light chain is expressed throughout embryonic striated muscle development, the regulatory myosin light chain was not detected in skeletal myogenesis in vivo or in vitro. Thus the atrial isoforms are not universally or exclusively "paired" and can be independently regulated. We propose that the manner in which these particular isoforms fulfill the functional requirements of the muscle at different developmental times may have direct impact on their regulation.
CHANTHOMAS PS, THOMPSON RP, YACOUB MH, et al., 1992, HOMEOBOX GENE-EXPRESSION IN ENDOCARDIAL CUSHION TISSUE AND CONDUCTION SYSTEM OF THE DEVELOPING CHICK HEART, CIRCULATION, Vol: 86, Pages: 842-842, ISSN: 0009-7322
Denny P, Swift S, Brand N, et al., 1992, A conserved family of genes related to the testis determining gene, SRY., Nucleic Acids Res, Vol: 20, ISSN: 0305-1048
BARTON PJR, BHAVSAR PK, BRAND NJ, et al., 1992, GENE-EXPRESSION DURING CARDIAC DEVELOPMENT, SYMP ON MOLECULAR BIOLOGY OF MUSCLE, Publisher: COMPANY BIOLOGISTS LTD, Pages: 251-264, ISSN: 0081-1386
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- Citations: 6
Barton PJ, Bhavsar PK, Brand NJ, et al., 1992, Gene expression during cardiac development., Pages: 251-264
The vertebrate heart forms as two concentric epithelial cylinders of myocardium and endocardium separated by an extended basement membrane matrix commonly referred to as cardiac jelly. Subsequent maturation involves a complex series of events including asymmetric changes in cell shape and division which contribute to bending and the formation of the bulboventricular loop, the formation of specialised tissues including endocardial cushion tissue of the atrioventricular (AV) and outflow tract regions, the development of conductive tissue and myocyte maturation leading to the overall pattern of expression characteristic of mature heart muscle. These processes depend on a precise spatial and temporal control of gene expression both of genes encoding regulatory molecules and those encoding structural components of the heart. In this chapter we address three aspects of cardiac development, namely, the determination of cell fate during formation of endocardial cushion tissue in the embryonic heart, transitions in troponin gene expression during fetal myocyte maturation, and the use of cloning techniques based on the polymerase chain reaction for identifying transcription factors present in the heart.
BHAVSAR PK, DHOOT GK, CUMMING DVE, et al., 1991, DEVELOPMENTAL EXPRESSION OF TROPONIN-I ISOFORMS IN FETAL HUMAN HEART, FEBS LETTERS, Vol: 292, Pages: 5-8, ISSN: 0014-5793
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- Citations: 91
MACGEOCH C, BARTON PJR, VALLINS WJ, et al., 1991, THE HUMAN CARDIAC TROPONIN-I LOCUS - ASSIGNMENT TO CHROMOSOME 19P13.2-19Q13.2, HUMAN GENETICS, Vol: 88, Pages: 101-104, ISSN: 0340-6717
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- Citations: 33
BRAND NJ, DABHADE N, YACOUB M, et al., 1991, DETERMINATION OF THE 5' EXON STRUCTURE OF THE HUMAN CARDIAC ALPHA-MYOSIN HEAVY-CHAIN GENE, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Vol: 179, Pages: 1255-1258, ISSN: 0006-291X
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- Citations: 5
BARTON PJR, MOSCOSO G, THOMPSON RP, 1991, DETECTION OF MYOSIN GENE-EXPRESSION IN THE DEVELOPING HEART USING PROBES DERIVED BY POLYMERASE CHAIN-REACTION, INTERNATIONAL JOURNAL OF CARDIOLOGY, Vol: 30, Pages: 116-118, ISSN: 0167-5273
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- Citations: 6
Lyons GE, Schiaffino S, Sassoon D, et al., 1990, Developmental regulation of myosin gene expression in mouse cardiac muscle., J Cell Biol, Vol: 111, Pages: 2427-2436, ISSN: 0021-9525
Expression of the two isoforms of cardiac myosin heavy chain (MHC), MHC alpha and MHC beta, in mammals is regulated postnatally by a variety of stimuli, including serum hormone levels. Less is known about the factors that regulate myosin gene expression in rapidly growing cardiac muscle in embryos. Using isoform-specific 35S-labeled cRNA probes corresponding to the two MHC genes and the two myosin alkali light chain (MLC) genes expressed in cardiac muscle, we have investigated the temporal and spatial pattern of expression of these different genes in the developing mouse heart by in situ hybridization. Between 7.5 and 8 d post coitum (p.c.), the newly formed cardiac tube begins to express MHC alpha, MHC beta, MLC1 atrial (MLC1A), and MLC1 ventricular (MLC1V) gene transcripts at high levels throughout the myocardium. As a distinct ventricular chamber forms between 8 and 9 d p.c., MHC beta mRNAs begin to be restricted to ventricular myocytes. This process is complete by 10.5 d p.c. During this time, MHC alpha mRNA levels decrease in ventricular muscle cells but continue to be expressed at high levels in atrial muscle cells. MHC alpha transcripts continue to decrease in ventricular myocytes until 16 d p.c., when they are detectable at low levels, but then increase, and finally replace MHC beta mRNAs in ventricular muscle by 7 d after birth. Like MHC beta, MLC1V transcripts become restricted to ventricular myocytes, but at a slower rate. MLC1V mRNAs continue to be detected at low levels in atrial cells until 15.5 d p.c. MLC1A mRNA levels gradually decrease but are still detectable in ventricular cells until a few days after birth. This dynamic pattern of changes in the myosin phenotype in the prenatal mouse heart suggests that there are different regulatory mechanisms for cell-specific expression of myosin isoforms during cardiac development.
VALLINS WJ, BRAND NJ, DABHADE N, et al., 1990, MOLECULAR-CLONING OF HUMAN CARDIAC TROPONIN-I USING POLYMERASE CHAIN-REACTION, FEBS LETTERS, Vol: 270, Pages: 57-61, ISSN: 0014-5793
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- Citations: 119
Soussi-Yanicostas N, Barbet JP, Laurent-Winter C, et al., 1990, Transition of myosin isozymes during development of human masseter muscle. Persistence of developmental isoforms during postnatal stage., Development, Vol: 108, Pages: 239-249, ISSN: 0950-1991
Previous results have shown that the adult human masseter muscle contains myosin isoforms that are specific to early stages of development in trunk and limb muscles, i.e. embryonic and fetal (neonatal) myosin heavy chains (MHC) and embryonic myosin light chain (MLC1emb). We wanted to know if this specific pattern is the result of a late maturation or of a distinct evolution during development. We show here that the embryonic and the fetal MHC and the MLC1emb are expressed throughout perinatal and postnatal masseter development. Our results also demonstrate that MLC1emb accumulation increases considerably during the postnatal period. In addition, both the slow MLCs and the slow isoform of tropomyosin are expressed later in the masseter than quadriceps and the fast skeletal muscle isoform MLC3 is not detected during fetal and early postnatal development in the masseter whereas it is expressed throughout fetal development in the quadriceps. Our results thus confirm previous histochemical data and demonstrate that the masseter muscle displays a pattern of myosin and tropomyosin isoform transitions different to that previously described in trunk and limb muscles. This suggests that control of masseter muscle development involves mechanisms distinct from other body muscles, possibly as a result of either its craniofacial innervation or of a possibly different embryonic origin.
BARTON PJR, HARRIS AJ, BUCKINGHAM ME, 1989, MYOSIN LIGHT CHAIN GENE-EXPRESSION IN DEVELOPING AND DENERVATED FETAL MUSCLE IN THE MOUSE, DEVELOPMENT, Vol: 107, Pages: 819-824, ISSN: 0950-1991
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- Citations: 24
COHENHAGUENAUER O, BARTON PJR, NGUYEN VC, et al., 1989, CHROMOSOMAL ASSIGNMENT OF 2 MYOSIN ALKALI LIGHT-CHAIN GENES ENCODING THE VENTRICULAR SLOW SKELETAL-MUSCLE ISOFORM AND THE ATRIAL FETAL MUSCLE ISOFORM (MYL3, MYL4), HUMAN GENETICS, Vol: 81, Pages: 278-282, ISSN: 0340-6717
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- Citations: 32
KIRSCHBAUM BJ, SIMONEAU JA, BAR A, et al., 1989, CHRONIC STIMULATION-INDUCED CHANGES OF MYOSIN LIGHT-CHAINS AT THE MESSENGER-RNA AND PROTEIN-LEVELS IN RAT FAST-TWITCH MUSCLE, EUROPEAN JOURNAL OF BIOCHEMISTRY, Vol: 179, Pages: 23-29, ISSN: 0014-2956
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- Citations: 48
COHENHAGUENAUER O, BARTON PJR, BUONANNO A, et al., 1989, LOCALIZATION OF THE ACETYLCHOLINE RECEPTOR-GAMMA-SUBUNIT GENE TO HUMAN-CHROMOSOME 2Q32-QTER, CYTOGENETICS AND CELL GENETICS, Vol: 52, Pages: 124-127, ISSN: 0301-0171
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- Citations: 9
COHEN A, BARTON PJR, ROBERT B, et al., 1988, PROMOTER ANALYSIS OF MYOSIN ALKALI LIGHT CHAIN GENES EXPRESSED IN MOUSE STRIATED-MUSCLE, NUCLEIC ACIDS RESEARCH, Vol: 16, Pages: 10037-10052, ISSN: 0305-1048
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- Citations: 18
BARTON PJR, ROBERT B, COHEN A, et al., 1988, STRUCTURE AND SEQUENCE OF THE MYOSIN ALKALI LIGHT CHAIN GENE EXPRESSED IN ADULT CARDIAC ATRIA AND FETAL STRIATED-MUSCLE, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 263, Pages: 12669-12676, ISSN: 0021-9258
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- Citations: 72
Pinset C, Montarras D, Chenevert J, et al., 1988, Control of myogenesis in the mouse myogenic C2 cell line by medium composition and by insulin: characterization of permissive and inducible C2 myoblasts., Differentiation, Vol: 38, Pages: 28-34, ISSN: 0301-4681
Using subcloning and manipulations of culture conditions we have isolated from the mouse myogenic cell line C2 a variant cell line that we named inducible. Unlike the progenitor cells that are referred to as permissive, inducible myoblasts differentiate poorly in Dulbecco modified Eagle medium plus fetal calf serum (FCS) and require the presence of insulin at a high concentration (1.6 10(-6) M) or insulin-like growth factor I (IGFI) at a lower concentration (2.5 10(-8) M) to differentiate. Permissive and inducible myoblasts fail to differentiate when grown in MCDB202 medium plus 20% FCS, even after a prolonged arrest in G1 phase. This shows that an arrest in G1 is in itself insufficient to trigger terminal differentiation. Both cell types also exhibit distinct patterns of accumulation of muscle mRNAs corresponding to sarcomeric actins and myosin light chain MLC1A. The possibility that these two cell lines might represent two different stages of the progression of myoblasts toward terminal differentiation is discussed.
COHENHAGUENAUER O, BARTON PJR, CONG NV, et al., 1988, ASSIGNMENT OF THE HUMAN FAST SKELETAL-MUSCLE MYOSIN ALKALI LIGHT-CHAINS GENE (MLC1F/MLC3F) TO 2Q 32.1-2QTER, HUMAN GENETICS, Vol: 78, Pages: 65-70, ISSN: 0340-6717
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- Citations: 18
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