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[1.] Analyse:Jse/Fragment 007 03 - Diskussion
Bearbeitet: 12. August 2017, 22:28 Hindemith
Erstellt: 13. January 2015, 09:13 (Klgn)
Fragment, Jse, KomplettPlagiat, SMWFragment, Schutzlevel, Weissmuller et al. 2005, ZuSichten

Typus
KomplettPlagiat
Bearbeiter
Klgn
Gesichtet
No
Untersuchte Arbeit:
Seite: 7, Zeilen: 3 ff.
Quelle: Weissmuller et al. 2005
Seite(n): 230, Zeilen: -
3. INTRODUCTION

3.1. Vascular barrier

3.1.1. Structural and functional elements of the vascular barrier

The predominant barrier (~90%) to movement of macromolecules across a blood vessel wall is presented by the endothelium (2, 3). Passage of macromolecules across a cellular monolayer can occur via either a paracellular route (i.e., between cells) or a transcellular route (i.e., through cells). In non-pathologic endothelium, macromolecules such as albumin (molecular weight ~66 kD) appear to cross the cell monolayer by passing between adjacent endothelial cells (i.e., paracellular) although some degree of transcellular passage may also occur (4, 5). Endothelial permeability is determined by cytoskeletal mechanisms that regulate lateral membrane intercellular junctions (6, 7). Tight junctions, also known as zona occludens, comprise one type of intercellular junction. Transmembrane proteins found within this region which function to regulate paracellular passage of macromolecules include the proteins occludin, and members of the junctional adhesion molecule (JAM) and claudin families of proteins (8). Tight junctions form narrow, cell-to-cell contacts with adjacent cells and comprise the predominant barrier to transit of macromolecules between adjacent endothelial cells (9). Endothelial macromolecular permeability is inversely related to macromolecule size. Permeability is also dependent on the tissue of origin. For example, endothelial cells in the cerebral circulation (i.e., blood-brain barrier) demonstrate an exceptionally low permeability (10, 11). Endothelial permeability may increase markedly upon exposure to a variety of inflammatory compounds (e.g., [histamine, thrombin, reactive oxygen species, leukotrienes, bacterial endotoxins) or adverse conditions (e.g., hypoxia, ischemia) (2, 12).]


2. Stevens, T., J.G.N. Garcia, D.M. Shasby, J. Bhattacharya, and A.B. Malik. 2000. Mechanisms regulating endothelial cell barrier function. Am. J. Physiol. (Lung Cell Mol Physiol) 279:L419-L422.

3. Stevens, T., J. Creighton, and W.J. Thompson. 1999. Control of cAMP in lung endothelial cell phenotypes. Implications for control of barrier function. Am J Physiol 277:L119-126.

4. Stan, R.V. 2002. Structure and function of endothelial caveolae. Microsc Res Tech 57:350-364.

5. Michel, C.C. 1998. Capillaries, caveolae, calcium and cyclic nucleotides: a new look at micorvascular permeability. J Mol Cell Cardiol 30:2541- 2546.

6. Worthylake, R.A., and K. Burridge. 2001. Leukocyte transendothelial mirgration: orchestrating the underlying molecular machinery. Curr Opin Cell Biol 13:569-577.

7. Schoenwaelder, S.M., and K. Burridge. 1999. Bidirectional signaling between the cytoskeleton and integrins. Curr Opin Cell Biol 11:274-286.

8. Comerford, K.M., D.W. Lawrence, K. Synnestvedt, B.P. Levi, and S.P. Colgan. 2002. Role of vasodilator-stimulated phosphoprotein in protein kinase A-induced changes in endothelial junctional permeability. Faseb J

9. Tsukita, S., M. Furuse, and M. Itoh. 2001. Multifunctional strands in tight junctions. Nat Rev Mol Cell Biol 2:285-293.

10. Rubin, L.L. 1992. Endothelial cells: adhesion and tight junctions. Curr Opin Cell Biol 4:830-833.

11. Janzer, R.C., and M.C. Raff. 1987. Astrocytes induce blood-brain barrier properties in endothelial cells. Nature 325:253-257.

12. Dejana, E., R. Spagnuolo, and C. Bazzoni. 2001. Interendothelial junctions and their role in the control of angiogenesis, vascular permeability and leukocyte transmigration. Thromb Haemost 86:308- 315.

Structural and functional elements of the vascular barrier

The predominant barrier (~90%) to movement of macromolecules across a blood vessel wall is presented by the endothelium [19, 20]. Passage of macromolecules across a cellular monolayer can occur via either a paracellular route (i.e., between cells) or a transcellular route (i.e., through cells). In non-pathologic endothelium, macromolecules such as albumin (molecular weight ~65 kD) appear to cross the cell monolayer by passing between adjacent endothelial cells (i.e., paracellular) although some degree of transcellular passage may also occur [21, 22]. Endothelial permeability is determined by cytoskeletal mechanisms that regulate lateral membrane intercellular junctions [23, 24]. Tight junctions, also known as zona occludens, comprise one type of intercellular junction. Transmembrane proteins found within this region which function to regulate paracellular passage of macromolecules include the proteins occludin, and members of the junctional adhesion molecule (JAM) and claudin families of proteins [18]. Tight junctions form narrow, cell-to-cell contacts with adjacent cells and comprise the predominant barrier to transit of macromolecules between adjacent endothelial cells [25]. Endothelial macromolecular permeability is inversely related to macromolecule size. Permeability is also dependent on the tissue of origin. For example, endothelial cells in the cerebral circulation (i.e., blood-brain barrier) demonstrate an exceptionally low permeability [26, 27]. Endothelial permeability may increase markedly upon exposure to a variety of inflammatory compounds (e.g., histamine, thrombin, reactive oxygen species, leukotrienes, bacterial endotoxins) or adverse conditions (e.g., hypoxia, ischemia) [6, 19].


6. Dejana E, Spagnuolo R, Bazzoni G. Interendothelial junctions and their role in the control of angiogenesis, vascular permeability and leukocyte transmigration. Thromb Haemost 2001; 86: 308-15.

18. Comerford KM, Lawrence DW, Synnestvedt K et al. Role of vasodilator-stimulated phosphoprotein in PKA-induced changes in endothelial junctional permeability. FASEB J 2002; 16: 583-5.

19. Stevens T, Garcia JGN, Shasby DM et al. Mechanisms regulating endothelial cell barrier function. Am J Physiol Lung Cell Mol Physiol 2000; 279: L419-22.

20. Stevens T, Creighton J, Thompson WJ. Control of cAMP in lung endothelial cell phenotypes. Implications for control of barrier function. Am J Physiol 1999; 277: L119-26.

21. Stan RV. Structure and function of endothelial caveolae. Microsc Res Tech 2002; 57: 350-64.

22. Michel CC. Capillaries, caveolae, calcium and cyclic nucleotides: A new look at microvascular permeability. J Mol Cell Cardiol 1998; 30: 2541-6.

23. Worthylake RA, Burridge K. Leukocyte transendothelial migration: Orchestrating the underlying molecular machinery. Curr Opin Cell Biol 2001; 13: 569-77.

24. Schoenwaelder SM, Burridge K. Bidirectional signaling between the cytoskeleton and integrins. Curr Opin Cell Biol 1999; 11: 274-86.

25. Tsukita S, Furuse M, Itoh M. Multifunctional strands in tight junctions. Nat Rev Mol Cell Biol 2001; 2: 285-93.

26. Rubin LL. Endothelial cells: Adhesion and tight junctions. Curr Opin Cell Biol 1992; 4: 830-3.

27. Janzer RC, Raff MC. Astrocytes induce blood-brain barrier properties in endothelial cells. Nature 1987; 325: 253-7.

Anmerkungen

The source is not mentioned here.

Sichter
(Hindemith)

[2.] Analyse:Jse/Fragment 019 04 - Diskussion
Bearbeitet: 12. August 2017, 21:44 Hindemith
Erstellt: 12. August 2017, 21:36 (Hindemith)
Barbe et al 2005, BauernOpfer, Fragment, Jse, SMWFragment, Schutzlevel, ZuSichten

Typus
BauernOpfer
Bearbeiter
Hindemith
Gesichtet
No
Untersuchte Arbeit:
Seite: 19, Zeilen: 4-8, 11-25
Quelle: Barbe et al 2005
Seite(n): 104, 105, 108, Zeilen: 104: r.col: 45ff; 105: l.col: 19ff; 108: l.col: 8ff
In total, 25 Caenorhabditis elegans (Ce- Inx and 8 Drosophila melanogaster (Dm-Inx) innexins have been identified. Mutant analysis and molecular characterization have shown that innexins are not functionally equivalent and are engaged in similar roles to connexins, e.g. in synaptic transmission, embryonic and postembryonic developement (94).

[...] Despite the lack of significant sequence homology, strong similarities exist at the structural and functional level with canonical gap-junction proteins. Thus pannexins share the same membrane topology with innexins and connexins as well as the hallmark of regularly spaced cysteine residues in the two extracellular loops connecting the transmembrane domains. Whereas the connexins contain three such residues, pannexins contain only two, thus resembling in this respect innexins, although the spacing of the cysteine residues in the second extracellular loop of pannexins diverges from that of innexins (94). Northern blot analysis indicates that Panx1 and Panx2 transcripts are detected in many rodent tissues, including brain and spinal cord (where Panx2 is particularly abundant), eye, thyroid, prostate, and kidney. The widespread distribution of Panx1 has been confirmed by probing human tissues with the highest levels being found in heart, gonads, and skeletal muscle. These results are at variance with those found in rodents, in that no signal was detected in skeletal musle and heart by Northern blot. Panx3 presents the most [restricted pattern of distribution and has been detected only in skin, which is devoid of Panx1 and Panx2 mRNA (94).]


94. Barbe, M.T., Hannah Monyer, and Roberto Bruzzone. 2006. Cell-cell communication beyond connexins: the pannexin channel. Physiology 21:103-114.

In total, 25 Caenorhabditis elegans (Ce-INX) and 8 Drosophila melanogaster (Dm-Inx) innexins have been identified, thereby paving the way for the application of genetic tools in the study of their function. Mutant analysis and molecular characterization have shown that innexins are not functionally equivalent and are engaged in similar roles to connexins, for example in synaptic transmission, embryonic and postembryonic development, and morphogenesis (4, 28, 35, 58, 90, 91).

[page 105]

Despite the lack of significant sequence homology (see below), strong similarities exist at the structural and functional level with canonical gap-junction proteins. Thus pannexins share the same membrane topology with innexins and connexins as well as the hallmark of regularly spaced cysteine residues in the two extracellular loops connecting the transmembrane domains (FIGURE 1). Whereas the connexins contain three such residues, pannexins contain only two, thus resembling in this respect innexins, although the spacing of the cysteine residues in the second extracellular loop of pannexins diverges from that of innexins (52).

[page 108]

Northern blot analysis indicates that Panx1 and Panx2 transcripts are detected in many rodent tissues, including brain and spinal cord (where Panx2 is particularly abundant), eye, thyroid, prostate, and kidney (14, 77, 102, 104). The widespread distribution of Panx1 has been confirmed by probing human tissues, with the highest levels being found in heart, gonads, and skeletal muscle (3). These results are at variance with those reported in rodents, in that no signal was detected in skeletal muscle and heart by Northern blot (14), whereas only a weak band was amplified by RTPCR from cardiac mRNA (77). [...]

Panx3 presents the most restricted pattern of distribution and has been detected only in skin, which is devoid of Panx1 and Panx2 mRNA (14).

Anmerkungen

The source is mentioned, but nothing has been marked as a citation.

Sichter
(Hindemith)

[3.] Analyse:Jse/Fragment 073 12 - Diskussion
Bearbeitet: 12. August 2017, 00:04 Hindemith
Erstellt: 12. August 2017, 00:02 (Hindemith)
Eltzschig et al 2006, Fragment, Jse, KomplettPlagiat, SMWFragment, Schutzlevel, ZuSichten

Typus
KomplettPlagiat
Bearbeiter
Hindemith
Gesichtet
No
Untersuchte Arbeit:
Seite: 73, Zeilen: 12-25
Quelle: Eltzschig et al 2006
Seite(n): 1106, 1107, Zeilen: 1106: r. column: last lines; 1107: l. columh: 1ff
Consistent with our findings, previous studies indicated that Cx43 phosphorylation can be modulated by inflammation and hypoxia. For instance, dephosphorylation of Cx43 and uncoupling of myocardial gap junctions occurs during myocardial ischemia. Under such circumstances, Cx43 may be reversibly dephosphorylated and rephosphorylated during hypoxia and reoxygenation dependent on fluctuations in intracellular ATP content (275). Moreover, several studies have implicated a role for Cx43 in cardioprotection by ischemic preconditioning, insomuch as protection by ischemic preconditioning is lost in cardiomyocytes and hearts of heterozygous Cx43-deficient mice (276). It is tempting to speculate that the role of Cx43 as ATP channel may also be involveld in cardioprotection by ischemic preconditioning. In fact, this may point to a clinical role of Cx43-dependent ATP release in myocardial ischemia. Thus, PMN-dependent ATP release could represent an important substrate for [nucleotidase-dependent extracellular adenosine generation during cardioprotection by ischemic preconditioning.]

275. Turner, M.S., G.A. Haywood, P. Andreka, L. You, P.E. Martin, W.H. Evans, K.A. Webster, and N.H. Bishopric. 2004. Reversible connexin 43 dephosphorylation during hypoxia and reoxygenation is linked to cellular ATP levels. Circ Res 95:726-733.

276. Schwanke, U., I. Konietzka, A. Duschin, X. Li, R. Schulz, and G. Heusch. 2002. No ischemic preconditioning in heterozygous connexin43-deficient mice. Am J Physiol Heart Circ Physiol 283:H1740-1742.

Consistent with our findings, previous studies indicated that Cx43 phosphorylation can be modulated by inflammation and hypoxia, resulting in an

[page 1107]

alteration in cellular functions. For instance, dephosphorylation of Cx43 and uncoupling of myocardial gap junctions occurs during myocardial ischemia. Under such circumstances, Cx43 may be reversibly dephosphorylated and rephosphorylated during hypoxia and reoxygenation dependent on fluctuations in intracellular ATP content.22 Moreover, several studies have implicated a role for Cx43 in cardioprotection by ischemic preconditioning, insomuch as protection by ischemic preconditioning is lost in cardiomyocytes and hearts of heterozygous Cx43-deficient mice.23 In view of the results from the present study showing a critical role of Cx43 as a phosphorylationdependent ATP release channel on PMNs in modulating endothelial adenosine responses, it is tempting to speculate that the role of Cx43 as ATP channel may also be involved in cardioprotection by ischemic preconditioning. In fact, this may point to a clinical role of Cx43-dependent ATP release in myocardial ischemia. [...] Thus, PMN-dependent ATP release could represent an important substrate for nucleotidase-dependent extracellular adenosine generation during cardioprotection by ischemic preconditioning.


22. Turner MS, Haywood GA, Andreka P, You L, Martin PE, Evans WH, Webster KA, Bishopric NH. Reversible connexin 43 dephosphorylation during hypoxia and reoxygenation is linked to cellular ATP levels. Circ Res. 2004;95:726–733.

23. Schwanke U, Konietzka I, Duschin A, Li X, Schulz R, Heusch G. No ischemic preconditioning in heterozygous connexin43-deficient mice. Am J Physiol Heart Circ Physiol. 2002;283:H1740–H1742.

Anmerkungen

The source is not given.

Sichter
(Hindemith)


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Quellen

Quelle Autor Titel Verlag Jahr Lit.-V. FN
Jse/Barbe et al 2005 Michael T. Barbe, Hannah Monyer, Roberto Bruzzone Cell-Cell Communication Beyond Connexins: The Pannexin Channels 2006 yes yes
Jse/Eltzschig et al 2006 Holger K. Eltzschig, Tobias Eckle, Alice Mager, Natalie Küper, Christian Karcher, Thomas Weissmüller, Kerstin Boengler, Rainer Schulz, Simon C. Robson, Sean P. Colgan TP Release From Activated Neutrophils Occurs via Connexin 43 and Modulates Adenosine-Dependent Endothelial Cell Function

https://doi.org/10.1161/01.RES.0000250174.31269.70 . 2006;99:1100-1108 Originally published November 9, 2006

2006 yes yes
Jse/Weissmuller et al. 2005 Thomas Weissmuller, Holger K. Eltzschig, Sean P. Colgan Dynamic purine signaling and metabolism during neutrophil–endothelial interactions Springer 2005 yes yes


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