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Untersuchte Arbeit:
Seite: 18, Zeilen: 9-27
Quelle: Wright_2005
Seite(n): 58-59, Zeilen: S. 58: 2. Spalte, 26-28, S. 59: 2. Spalte, 22 ff.
2.3.1 Immunoregulatory functions of surfactant proteins

As mentioned above, the host defence functions of surfactant are primarily mediated by SP-A and SP-D, which are members of the collectin family of proteins. SP-A and SP-D have been also localized to non-pulmonary sites, including the trachea, brain, testes, salivary glands, lachrymal glands, heart, prostate, kidney, pancreas and the female urogenital tract (Leth-Larsen et al., 2004; Lin et al., 2000; Madsen et al., 2000; Rubio et al., 1995), although it is not yet clear whether all of these organs express sufficient amounts of protein for it to be physiologically effective.

Among their well-established role as opsonins, SP-A and SP-D also have functions in initiating parturition, facilitating clearance of apoptotic cells and directly killing bacteria.

2.3.2 Collectin structure

In addition to the two lung collectins SP-A and SP-D, serum collectins have been identified in humans (mannose-binding lectin, MBL) and in bovidae (conglutinin, CL-43 and CL-46) (Hansen and Holmskov, 2002).

SP-A and SP-D are synthesized as primary translation products of approximately 26-36kDa and 43kDa, respectively (figure 3). The collagen-like domain is N-terminal to a coiled-coil structure that precedes the C-terminal lectin domain. The lectin domains mediate the interaction of collectins with a wide varity of pathogens. The collagen domains vary greatly in length (Holmskov et al., 2003).

The host-defence functions of surfactant are primarily mediated by SP-A and SP-D, which are members of the collectin family of proteins.

[P. 59] [...]

SP-A and SP-D have been localized to non-pulmonary sites, including the trachea, brain, testes, salivary glands, lachrymal glands, heart, prostate, kidney, pancreas and the female urogenital tract11–14, although it is not yet clear whether all of these organs express sufficient amounts of protein for it to be physiologically effective. [...] An emphasis is placed on recent studies showing that, in addition to their well-established role as opsonins, SP-A and SP-D also have novel functions in initiating parturition, facilitating clearance of apoptotic cells and directly killing bacteria.

Collectin structure

In addition to the two lung collectins SP-A and SP-D (FIG. 2), serum collectins have been identified in humans (mannose-binding lectin,MBL) and in bovidae (conglutinin, CL-43 and CL-46)15. [...] SP-A and SP-D are synthesized as primary translation products of approximately 26–36 kDa and 43 kDa, respectively. The collagen-like domain is N-terminal to a coiled-coil structure that precedes the lectin domain. The collagen domains vary greatly in length, ranging from 19 Gly-X-Y triplets in MBL to 59 in human SP-D18. --- 11. Rubio, S. et al. Pulmonary surfactant protein A (SP-A) is expressed by epithelial cells of small and large intestine. J. Biol. Chem. 270, 12162–12169 (1995).

12. Lin, Z. et al. Both human SP-A1 and SP–A2 genes are expressed in small and large intestine. Am. J. Respir. Crit. Care Med. 161, A43 (2000).

13. Madsen, J. et al. Localization of lung surfactant protein D on mucosal surfaces in human tissue. J. Immunol. 164, 5866–5870 (2000).

14. Leth-Larsen, R., Floridon, C., Nielsen, O. & Holmskov, U. Surfactant protein D in the female genital tract. Mol. Hum. Reprod. 10, 149–154 (2004).

15. Hansen, S. & Holmskov, U. Lung surfactant protein D (SP-D) and the molecular diverted descendants: conglutinin, CL-43 and CL-46. Immunobiology 205, 498–517 (2002).

18. Holmskov, U., Thiel, S. & Jensenius, J. C. Collectins and ficolins: humoral lectins of the innate immune defense. Annu. Rev. Immunol. 21, 547–578 (2003).

Anmerkungen

The source is not indicated. The references are identical. Heading 2.3.1 is identical with the title of Wright 2005.

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