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Autor     Jo Rae Wright
Titel    Immunoregulatoroy Functions of Surfactant Proteins
Zeitschrift    Nature Reviews
Jahr    2005
Jahrgang    5
Seiten    58-68
ISSN    1474-1733
URL    http://www.nature.com/nri/journal/v5/n1/full/nri1528.html

Literaturverz.   

yes
Fußnoten    yes
Fragmente    11


Fragmente der Quelle:
[1.] Mag/Fragment 013 01 - Diskussion
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Figure 2: Schematic structure of airway and alveolus and their host-defence mechanisms. The lung is constantly challenged by inhaled pathogens, pollutans [sic] and particles. Several different defence mechanisms contribute to lung defence. These include filtration in the naso-oropharynx and conducting airways, sneezing, coughing and mucociliary clearance. Small particles might reach the alveolar gas-exchange regions of the lung. Host-defence functions in the peripheral air-spaces include surfactant, other opsonins (such as immunoglobulins) and innate immune cells (including alveolar macrophages and neutrophiles [sic]). Surfactant protein A (SP-A); surfactant protein D (SP-D) (adapted from Wright, 2005).


Wright JR. Immunoregulatory functions of surfactant proteins. Nat Rev Immunol. 2005 Jan; 5 (1): 58-68. Review.

12a source Mag.png

Figure 1 Lung host-defence mechanisms. The lung is constantly challenged by inhaled pathogens, pollutants and particles. Several different defence mechanisms contribute to lung defence. These include filtration in the naso-oropharynx and conducting airways, sneezing, coughing and mucociliary clearance. Small particles might reach the alveolar gas-exchange regions of the lung. Host-defence functions in the peripheral air-spaces include surfactant, other opsonins (such as immunoglobulins) and innate immune cells (including alveolar macrophages and neutrophils). SP-A, surfactant protein A; SP-D, surfactant protein D.

Anmerkungen

The source is given, but it does not make clear that the extensive figure caption is copied literally from the source.

Neither does the word "adapted" suggest that the figure is an exact copy of the figure in the source.

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SP-B is essential for the ability of surfactant to reduce surface tension (Nogee, 2004), and SP-C has recently been shown to bind lipopolysaccharide (LPS) (Augosto et al., 2002; Augosto et al., 2003). In the absence of surfactant, surface tension is extremely high at end expiration and tends to collapse the lung. This makes breathing difficult to the extent that respiration is frequently impossible without ventilatory support and surfactant replacement. A deficiency of surfactant – which can result in “Respiratory-Distress Syndrome (RDS)” – occurs when infants are born prematurely, before their surfactant biosynthetic machinery has matured. Treatment of these premature infants with exogenous surfactant replacement reduces mortality and morbidity, because of this disease (Wright, 2005).

Augusto LA, Li J, Synguelakis M, Johansson J, Chaby R. Structural basis for interactions between lung surfactant protein C and bacterial lipopolysaccharide. J Biol Chem. 2002 Jun 28; 277 (26): 23484-92. Epub 2002 Apr 29.

Augusto LA, Synguelakis M, Johansson J, Pedron T, Girard R, Chaby R. Interaction of pulmonary surfactant protein C with CD14 and lipopolysaccharide. Infect Immun. 2003 Jan; 71 (1): 61-7.

Nogee LM. Alterations in SP-B and SP-C expression in neonatal lung disease. Annu Rev Physiol. 2004; 66: 601-23. Review.

Wright JR. Immunoregulatory functions of surfactant proteins. Nat Rev Immunol. 2005 Jan; 5 (1): 58-68. Review.

SP-B is essential for the ability of surfactant to reduce surface tension3, and SP-C has recently been shown to bind lipopolysaccharide (LPS)4,5. In the absence of surfactant, surface tension is extremely high at end expiration and tends to collapse the lung. This makes breathing difficult to the extent that respiration is frequently impossible without ventilatory support and surfactant replacement. A deficiency of surfactant — which can result in RESPIRATORY-DISTRESS SYNDROME — occurs when infants are born prematurely, before their surfactant biosynthetic machinery has matured. Treatment of these babies with exogenous surfactant replacement (BOX 1) reduces mortality and morbidity due to this disease.

3. Nogee, L. M. Alterations in SP-B and SP-C expression in neonatal lung disease. Annu. Rev. Physiol. 66, 601–623 (2004).

4. Augusto, L. A. et al. Interaction of pulmonary surfactant protein C with CD14 and lipopolysaccharide. Infect. Immun. 71, 61–67 (2003).

5. Augusto, L. A., Li, J., Synguelakis, M., Johansson, J. & Chaby, R. Structural basis for interactions between lung surfactant protein C and bacterial lipopolysaccharide. J. Biol. Chem. 277, 23484–23492 (2002).

Anmerkungen

The source is given, but the extent of the copied text is not clear to the reader. Neither is it clear that the copy is almost literal. Also three references to the literature are taken from the source.

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(Hindemith) Schumann

[3.] Mag/Fragment 018 09 - Diskussion
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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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(SleepyHollow02)

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The collectins are assembled as trimeric subunits, which multimerize to varying degrees. SP-A is mainly an octadecamer and forms a bouquet-like structure that is similar to MBL, whereas SP-D forms a dodecamer (Wright, 2005).

19a diss Mag.png

Figure 3: Collectin and C1q structure. Surfactant protein A (SP-A) and SP-D are members of a family of proteins known as collectins. a Collectins have collagen-like amino (N)-terminal regions and C-type (calcium dependent) carbohydrate-recognition domains (CRDs). Collectins consist of structural subunits that are composed of trimeric polypeptide chains, which are identical except for human SP-A. The trimers are assembled into oligomers. b SP-A and mannose-binding lectin (MBL) are octadecamers (18-mers), consisting of six trimeric subunits. SP-D is a dodecamer (12-mer), consisting of four trimeric subunits. Although C1q is structurally homologous to SP-A and MBL, it is not a collectin as it does not have a lectin domain (CRD) (adapted from Wright, 2005).


Wright JR. Immunoregulatory functions of surfactant proteins. Nat Rev Immunol. 2005 Jan; 5 (1): 58-68. Review.

[Page 59]

The collectins are assembled as trimeric subunits, which multimerize to varying degrees. SP-A is mainly an octadecamer and forms a bouquet-like structure that is similar to MBL, whereas SP-D forms a dodecamer (FIG. 2).

[Page 60]

19a source Mag.png

Figure 2 Collectin and C1q structure. Surfactant protein A (SP-A) and SP-D are members of a family of proteins known as collectins. a Collectins have collagen-like amino (N)-terminal regions and C-type (calcium dependent) carbohydrate-recognition domains (CRDs). Collectins consist of structural subunits that are composed of trimeric polypeptide chains, which are identical except for human SP-A. The trimers are assembled into oligomers. b SP-A and mannose-binding lectin (MBL) are octadecamers (18-mers), consisting of six trimeric subunits. SP-D is a dodecamer (12-mer), consisting of four trimeric subunits. Although C1q is structurally homologous to SP-A and MBL, it is not a collectin as it does not have a lectin domain (CRD). Note that these models are not drawn to scale.

Anmerkungen

The source is mentioned. Nevertheless there is no hint that the texts are identical.

The figure has not been "adapted" but rather "copied".

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(Graf Isolan)

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For example, both surfactant proteins, SP-A and SP-D, bind to mannose and glucose but bind only poorly to galactose (Haagsman et al., 1987; Lim et al.; 1994; Persson et al., 1990). The high affinity of the collectins for clustered oligosaccharides is thought to be important for their ability to distinguish non-self from self, as most carbohydrates in animals are terminated by sugars, such as galactose or sialic acid, that are poorly recognized by the collectins.

Haagsman HP, Hawgood S, Sargeant T, Buckley D, White RT, Drickamer K, Benson BJ. The major lung surfactant protein, SP 28-36, is a calcium-dependent, carbohydrate-binding protein. J Biol Chem. 1987 Oct 15; 262 (29):13877-80.

Lim BL, Wang JY, Holmskov U, Hoppe HJ, Reid KB. Expression of the carbohydrate recognition domain of lung surfactant protein D and demonstration of its binding to lipopolysaccharides of gram-negative bacteria. Biochem Biophys Res Commun. 1994 Aug 15; 202 (3):1674-80.

Persson A, Chang D, Crouch E. Surfactant protein D is a divalent cation-dependent carbohydrate-binding protein. J Biol Chem. 1990 Apr 5; 265 (10): 5755-60.

For example, both SP-A and SP-D bind to mannose and glucose but bind poorly to galactose23–25. [...] However, the high affinity of the collectins for clustered oligosaccharides is thought to be important for their ability to distinguish non-self from self, as most carbohydrates in animals are terminated by sugars, such as galatose [sic] or sialic acid, that are poorly recognized by the collectins.

23. Haagsman, H. P. et al. The major lung surfactant protein, SP 28–36, is a calcium-dependent, carbohydrate-binding protein. J. Biol. Chem. 262, 13877–13880 (1987). This paper was the first to report that SP-A is a member of the collectin family of collagenous C-type lectins.

24. Persson, A., Chang, D. & Crouch, E. Surfactant protein D is a divalent cation-dependent carbohydrate-binding protein. J. Biol. Chem. 265, 5755–5760 (1990).

25. Lim, B. L., Wang, J. Y., Holmskov, U., Hoppe, H. J. & Reid, K. B. Expression of the carbohydrate recognition domain of lung surfactant protein D and demonstration of its binding to lipopolysaccharides of Gram-negative bacteria. Biochem. Biophys. Res. Commun. 202, 1674–1680 (1994).

Anmerkungen

The remainder of the text on this page is copied from Wright with minor adaptations. Wright is indicated as source in the preceding sentence.

In this fragment, Mag adopts Wright’s summary of the findings of three other papers, using Wright’s words, without acknowledging Wright as source.

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Surfactant proteins A and D bind to a variety of bacteria, viruses, allergens and apoptotic cells and thereby function as opsonins to enhance the uptake of these cells and particles. Binding of the collectins to pathogens occurs by various mechanisms. Some pathogens are aggregated by SP-A and/or SP-D and were phagocytized by immune cells like macrophages. SP-A and SP-D also have direct effects on immune cells and modulate the production of cytokines and inflammatory mediators.

Numerous studies have reported that SP-A mediates cellular functions through C1q receptors (Ferguson et al., 1999; Malholtra et al., 1994), including C1qR (also known as CD93) (Nepomuceno et al., 1997; Steinberger et al., 2002) and calreticulin (Malhotra et al., 1990; Malholtra et al., 1993). SP-A and SP-D are able to bind Calreticulin, which in turn binds to CD91. CD91 is a component of the binding complex (Gardai et al., 2003).

The binding of SP-A and/or SP-D to the signal-inhibitory regulatory protein-α (SIRP-α) modulates cellular functions in a similar way like the binding complex of surfactant proteins with the CD91–calreticulin complex. In the absence of a pathogen, SP-A binds through its lectin domain to SIRP-α, whereas in the presence of a foreign organism or cell debris, to which the lectin domain of SP-A binds, the free collagen-like region activates immune cells through CD91–calreticulin. Importantly, engagement of the different receptors elicits different responses. Upon binding of SP-A to SIRP-α, the inflammatory-mediator production is inhibited. By contrast, SP-A enhances inflammatory mediator like tumour-necrosis factor (TNF), CXCL12 and CCL2 production through its binding to the CD91-calreticulin complex. Therefore, SP-A and SP-D both are able to enhance and inhibit inflammatory-mediator production to modulate the regulation of immune cells.

Another receptor that binds surfactant protein A was identified by Chroneos and colleagues and termed SP-R210 (Chroneos et al., 1996). Blocking of this receptor with specific antibodies leads to a loss of SP-A mediated functions, including inhibition of lymphocyte proliferation (Borron et al., 1998), enhanced uptake of bacteria by macrophages (Weikert et al., 1997) and mycobacterial killing by a nitric-oxide-dependent pathway (Weikert et al., 2000). Nevertheless, the molecular identity of SP-R210 is still unclear.


Borron P, McCormack FX, Elhalwagi BM, Chroneos ZC, Lewis JF, Zhu S, Wright JR, Shepherd VL, Possmayer F, Inchley K, Fraher LJ. Surfactant protein A inhibits T cell proliferation via its collagen-like tail and a 210-kDa receptor. Am J Physiol. 1998 Oct; 275 (4 Pt 1): L679-86.

Borron PJ, Crouch EC, Lewis JF, Wright JR, Possmayer F, Fraher LJ. Recombinant rat surfactant-associated protein D inhibits human T lymphocyte proliferation and IL-2 production. J Immunol. 1998 Nov 1; 161 (9): 4599-603.

Chroneos ZC, Abdolrasulnia R, Whitsett JA, Rice WR, Shepherd VL. Purification of a cell-surface receptor for surfactant protein A. J Biol Chem. 1996 Jul 5; 271 (27): 16375-83.

Ferguson JS, Voelker DR, McCormack FX, Schlesinger LS. Surfactant protein D binds to Mycobacterium tuberculosis bacilli and lipoarabinomannan via carbohydrate-lectin interactions resulting in reduced phagocytosis of the bacteria by macrophages. J Immunol. 1999 Jul 1; 163 (1): 312-21.

Gardai SJ, Xiao YQ, Dickinson M, Nick JA, Voelker DR, Greene KE, Henson PM. By binding SIRPalpha or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation. Cell. 2003 Oct 3; 115 (1): 13-23.

Malhotra R, Thiel S, Reid KB, Sim RB. Human leukocyte C1q receptor binds other soluble proteins with collagen domains. J Exp Med. 1990 Sep 1; 172 (3): 955-9.

Malhotra R, Willis AC, Jensenius JC, Jackson J, Sim RB. Structure and homology of human C1q receptor (collectin receptor). Immunology. 1993 Mar; 78 (3): 341-8.

Malhotra R, Haurum JS, Thiel S, Sim RB. Binding of human collectins (SP-A and MBP) to influenza virus. Biochem J. 1994 Dec 1; 304 (Pt2): 455-61.

Nepomuceno RR, Henschen-Edman AH, Burgess WH, Tenner AJ. cDNA cloning and primary structure analysis of C1qR(P), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro. Immunity. 1997 Feb; 6 (2): 119-29.

Steinberger P, Szekeres A, Wille S, Stockl J, Selenko N, Prager E, Staffler G, Madic O, Stockinger H, Knapp W. Identification of human CD93 as the phagocytic C1q receptor (C1qRp) by expression cloning. J Leukoc Biol. 2002 Jan; 71 (1): 133-40.

Weikert LF, Edwards K, Chroneos ZC, Hager C, Hoffman L, Shepherd VL. SP-A enhances uptake of bacillus Calmette-Guerin by macrophages through a specific SP-A receptor. Am J Physiol. 1997 May; 272 (5Pt1): L989-95.

Weikert LF, Lopez JP, Abdolrasulnia R, Chroneos ZC, Shepherd VL. Surfactant protein A enhances mycobacterial killing by rat macrophages through a nitric oxide-dependent pathway. Am J Physiol Lung Cell Mol Physiol. 2000 Aug; 279 (2): L216-23.

[page 60]

Numerous studies have reported that SP-A mediates cellular functions through C1q receptors37,38, including C1qR (also known as CD93)39,40 and calreticulin41,42. [...] However, recent studies have confirmed that calreticulin binds SP-A and SP-D and have shown that CD91 is a component of the binding complex43. [...] Gardai and co-workers43 recently reported that SP-A and SP-D also modulate cellular functions through signal-inhibitory regulatory protein-α (SIRP-α), as well as the CD91-calreticulin complex. [...] For example, in the absence of a pathogen, SP-A binds through its lectin domain to SIRP-α. In the presence of a foreign organism or cell debris, to which the lectin domain of SP-A binds, the free collagen-like region activates immune cells through CD91–calreticulin. Importantly, engagement of the different receptors elicits different responses. When SP-A binds SIRP-α, inflammatory-mediator production is inhibited. By contrast, SP-A enhances inflammatory mediator (for example, tumour-necrosis factor (TNF),

[page 61]

CXCL12 and CCL2) production through the CD91–calreticulin complex. This model provides at least a partial explanation for the apparently conflicting reports that SP-A and SP-D both enhance and inhibit inflammatory-mediator production and provides important information about mechanisms by which specific collectin responses might be mediated.

SP-R210 was identified more than eight years ago as an SP-A receptor45. SP-R210 was purified by SP-A affinity chromatography, and a SP-R210-specific antibody was shown to block SP-A-mediated functions, including inhibition of lymphocyte proliferation46, enhanced uptake of bacteria by macrophages47 and mycobacterial killing by a nitric-oxide-dependent pathway48. However, the molecular identity of SP-R210 has not yet been established.

[...]

Figure 3 Functions of SP-A and SP-D. Surfactant protein A (SP-A) and SP-D bind to a variety of bacteria, viruses, allergens and apoptotic cells and thereby function as opsonins to enhance the uptake of these cells and particles. Binding of the collectins to pathogens occurs by various mechanisms. Some pathogens are aggregated by SP-A and/or SP-D. SP-A and SP-D also have direct effects on immune cells and modulate the production of cytokines and inflammatory mediators.


37. Tenner, A. J. Membrane receptors for soluble defense collagens. Curr. Opin. Immunol. 11, 34–41 (1999).

38. Malhotra, R., Lu, J., Holmskov, U. & Sim, R. B. Collectins, collectin receptors and the lectin pathway of complement activation. Clin. Exp. Immunol. 97, 4–9 (1994).

39. Nepomuceno, R. R., Henschen-Edman, A. H., Burgess, W. H. & Tenner, A. J. cDNA cloning and primary structure analysis of C1aRp, the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro. Immunity 6, 119–129 (1997).

40. Steinberger, P. et al. Identification of human CD93 as the phagocytic C1q receptor (C1qRp) by expression cloning. J. Leukoc. Biol. 71, 133–140 (2002).

41. Malhotra, R., Willis, A., Jensenius, J., Jackson, J. & Sim, R. Structure and homology of human C1q receptor (collectin receptor). Immunology 78, 341–348 (1993).

42. Malhotra, R., Thiel, S., Reid, K. B. & Sim, R. B. Human leukocyte C1q receptor binds other soluble proteins with collagen domains. J. Exp. Med. 172, 955–959 (1990).

43. Gardai, S. J. et al. By binding SIRPα or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation. Cell 115, 13–23 (2003).
This is a compelling study showing that SP-A and SP-D bind two distinct receptors: SIRP-α and CD91–calreticulin.

45. Chroneos, Z. C., Abdolrasulnia, R., Whitsett, J. A., Rice, W. R. & Shepherd, V. L. Purification of a cell-surface receptor for surfactant protein A. J. Biol. Chem. 271, 16375–16383 (1996).
This paper was the first to report the characterization of an SP-A receptor.

46. Borron, P. et al. Surfactant protein A inhibits T cell proliferation via its collagen-like tail and a 210-kDa receptor. Am. J. Physiol. Lung Cell. Mol. Physiol. 275, L679–L686 (1998).

47. Weikert, L. F. et al. SP-A enhances uptake of bacillus Calmette-Guerin by macrophages through a specific SP-A receptor. Am. J. Physiol. Lung Cell. Mol. Physiol. 272, L989–L995 (1997).

48. Weikert, L. F., Lopez, J. P., Abdolrasulnia, R., Chroneos, Z. C. & Shepherd, V. L. Surfactant protein A enhances mycobacterial killing by rat macrophages through a nitric oxide-dependent pathway. Am. J. Physiol. Lung Cell. Mol. Physiol. 279, L216–L223 (2000).

Anmerkungen

Mag adopts Wright's literary review without indicating Wright as the source.

Note: there are two references "Borron et al. (1998)" in the bibliography.

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Glycoprotein 340 (gp340) is also discussed as a protein that binds SP-D through its CRD (Holmskov et al., 1997). Because of its localisation at the cell surface of alveolar macrophages, gp340 was suggested to be a SP-D receptor. It is identical to salivary agglutinin, a high-molecular-weight component of saliva that binds Streptococcus mutans, a bacterium that causes dental caries (Prakobphol et al., 2000). This putative receptor gp340 has no transmembrane domain so that it is suggested that it could interact with an adaptor molecule on the surface of the cell (Wright, 2005).

Additionally, a family of conserved cellular receptors that recognize pathogen-associated molecular patterns (PAMP) are discussed as binding-partners for SP-A and SP-D. This family of Toll-like receptors (TLRs) is activated by ligands like flagellin and CpG-containing DNA from bacteria, peptidoglycan from Gram-positive bacteria, LPS from Gram-negative bacteria, RNA from viruses and zymosan from yeast (Takeda et al., 2003). All these activation mechanisms end up in a series of conserved responses that culminate in inflammation and the production of inflammatory cytokines, such as TNF and interleukin-1β. The SP-A dependent binding to TLR4 results in an activation of the nuclear factor κB (NF-κB) signalling pathway and upregulation of cytokine synthesis (Guillot et al., 2002), whereas interaction of SP-A with TLR2 attenuates stimulation of TLR2 signalling and also stimulation of TNF secretion induced by zymosan or peptidoglycan (Sato et al., 2003).

In addition to phagocytosis, SP-A and SP-D have also the ability to regulate the production of inflammatory mediators by immune cells in a context-dependent manner. One example shows that inflammatory mediators, such as TNF, are both up- and downregulated by SP-A and SP-D (Crouch and Wright, 2001). The release of TNF that is induced by LPS or intact bacteria is inhibited by SP-A (Hickling et al., 1998; McIntosh et al., 1996; Rosseau et al., 1999). In contrast, SP-A enhances TNF production either when alone (Kremlev et al., 1994, Kremlev et al., 1997) or in presence of “rough” LPS (Sano et al., 1999).

A further effect of surfactant proteins SP-A and SP-D is the enhanced uptake of apoptotic cells by alveolar macrophages in vitro (Schagat, et al., 2001), which could be even shown for lungs of naïve mice in the case of SP-D (Vandivier et al., 2002).


Crouch E, Wright JR. Surfactant proteins a and d and pulmonary host defense. Annu Rev Physiol. 2001; 63: 521-54. Review.

Guillot L, Balloy V, McCormack FX, Golenbock DT, Chignard M, Si-Tahar M. Cutting edge: the immunostimulatory activity of the lung surfactant protein-A involves Toll-like receptor 4. J Immunol. 2002 Jun 15; 168 (12): 5989-92.

Hickling TP, Sim RB, Malhotra R. Induction of TNF-alpha release from human buffy coat cells by Pseudomonas aeruginosa is reduced by lung surfactant protein A. FEBS Lett. 1998 Oct 16; 437 (1-2): 65-9.

Holmskov U, Lawson P, Teisner B, Tornoe I, Willis AC, Morgan C, Koch C, Reid KB. Isolation and characterization of a new member of the scavenger receptor superfamily, glycoprotein-340 (gp-340), as a lung surfactant protein-D binding molecule. J Biol Chem. 1997 May 23; 272 (21): 13743-9.

Kremlev SG, Phelps DS. Surfactant protein A stimulation of inflammatory cytokine and immunoglobulin production. Am J Physiol. 1994 Dec; 267 (6Pt1): L712-9.

Kremlev SG, Umstead TM, Phelps DS. Surfactant protein A regulates cytokine production in the monocytic cell line THP-1. Am J Physiol. 1997 May; 272 (5Pt1): L996-1004.

McIntosh JC, Mervin-Blake S, Conner E, Wright JR. Surfactant protein A protects growing cells and reduces TNF-alpha activity from LPS-stimulated macrophages. Am J Physiol. 1996 Aug; 271 (2Pt1): L310-9.

Prakobphol A, Xu F, Hoang VM, Larsson T, Bergstrom J, Johansson I, Frangsmyr L, Holmskov U, Leffler H, Nilsson C, Boren T, Wright JR, Stromberg N, Fisher SJ. Salivary agglutinin, which binds Streptococcus mutans and Helicobacter pylori, is the lung scavenger receptor cysteine-rich protein gp-340. J Biol Chem. 2000 Dec 22; 275 (51): 39860-6.

Rosseau S, Hammerl P, Maus U, Gunther A, Seeger W, Grimminger F, Lohmeyer J. Surfactant protein A down-regulates proinflammatory cytokine production evoked by Candida albicans in human alveolar macrophages and monocytes. J Immunol. 1999 Oct 15; 163 (8): 4495-502.

Sano H, Sohma H, Muta T, Nomura S, Voelker DR, Kuroki Y. Pulmonary surfactant protein A modulates the cellular response to smooth and rough lipopolysaccharides by interaction with CD14. J Immunol. 1999 Jul 1; 163 (1):387-95.

Schagat TL, Wofford JA, Wright JR. Surfactant protein A enhances alveolar macrophage phagocytosis of apoptotic neutrophils. J Immunol. 2001 Feb 15; 166 (4): 2727-33.

Sato M, Sano H, Iwaki D, Kudo K, Konishi M, Takahashi H, Takahashi T, Imaizumi H, Asai Y, Kuroki Y. Direct binding of Toll-like receptor 2 to zymosan, and zymosan-induced NF-kappa B activation and TNF-alpha secretion are down-regulated by lung collectin surfactant protein A. J Immunol. 2003 Jul 1; 171 (1): 417-25.

Takeda K, Takeuchi O, Akira S. Recognition of lipopeptides by Toll-like receptors. J Endotoxin Res. 2002; 8 (6): 459-63.

Vandivier RW, Ogden CA, Fadok VA, Hoffmann PR, Brown KK, Botto M, Walport MJ, Fisher JH, Henson PM, Greene KE. Role of surfactant proteins A, D, and C1q in the clearance of apoptotic cells in vivo and in vitro: calreticulin and CD91 as a common collectin receptor complex. J Immunol. 2002 Oct 1; 169 (7): 3978-86.

Wright JR. Immunoregulatory functions of surfactant proteins. Nat Rev Immunol. 2005 Jan; 5 (1): 58-68. Review.

Glycoprotein 340 (gp340) was initially identified as a protein that binds the CRD of SP-D49. Because of its location at the cell surface of alveolar macrophages, gp340 was suggested to be an SP-D receptor. It was subsequently shown to be identical to salivary agglutinin, a high-molecular-weight component of saliva that binds Streptococcus mutans, a bacterium that causes dental caries50. gp340 does not have a transmembrane domain, and its identity as an SP-D receptor remains unclear. The possibility that gp340 could interact with an adaptor molecule on the surface of the cell has not yet been investigated.

Other recent studies have reported that SP-A and SP-D bind to Toll-like receptors (TLRs) — a family of conserved cellular receptors that recognize pathogenassociated molecular patterns, including flagellin and CpG-containing DNA from bacteria, peptidoglycan from Gram-positive bacteria, LPS from Gram-negative bacteria, RNA from viruses and zymosan from yeast51. Activation of TLRs by these ligands initiates a conserved series of responses that culminate in inflammation and the production of inflammatory cytokines, such as TNF and interleukin-1β (IL-1β). Guillot and co-workers52 observed a TLR4-dependent SP-A activation of the nuclear factor-κB (NF-κB)-signalling pathway and upregulation of cytokine synthesis in TLR4-transfected Chinese hamster ovary cells. Such a response was lacking in the TLR4-deficient mice. In addition, Murakami and colleagues53 reported that SP-A directly binds TLR2. By contrast, the interaction of SP-A with TLR2 attenuates stimulation of TLR2 signalling and also stimulation of TNF secretion induced by zymosan or peptidoglycan. [...]

[page 62]

Collectins regulate multiple cellular responses in addition to phagocytosis. SP-A and SP-D also regulate the production of inflammatory mediators by immune cells in a context-dependent manner. Several reports show that inflammatory mediators, such as TNF, are both upregulated and downregulated27 by SP-A and SP-D. For example, SP-A inhibits62–64 the release of TNF that is induced by LPS or intact bacteria; by contrast, SP-A enhances TNF production either when alone65,66 or in the presence of ‘rough’LPS67. [...]

[page 63]

Recent studies have shown that both SP-A and SP-D enhance the uptake of apoptotic cells by alveolar macrophages in vitro79. Vandivier and colleagues80 showed that SP-A, SP-D and C1q all enhanced apoptotic-cell uptake by mouse and human alveolar macrophages in vitro, but only SP-D altered apoptotic-cell clearance from naive mouse lung80.


27. Crouch, E. & Wright, J. R. Surfactant proteins A and D and pulmonary host defense. Annu. Rev. Physiol. 63, 521–554 (2001).

49. Holmskov, U. et al. Isolation and characterization of a new member of the scavenger receptor superfamily, glycoprotein-340 (gp-340), as a lung surfactant protein-D binding molecule. J. Biol. Chem. 272, 13743–13749 (1997).

50. Prakobphol, A. et al. Salivary agglutinin, which binds Streptococcus mutans and Helicobacter pylori, is the lung scavenger receptor cysteine-rich protein gp-340. J. Biol. Chem. 275, 39860– 39866 (2000).

51. Takeda, K., Kaisho, T. & Akira, S. Toll-like receptors. Annu. Rev. Immunol. 21, 335–376 (2003).

52. Guillot, L. et al. The immunostimulatory activity of the lung surfactant protein-A involves Toll-like receptor 4. J. Immunol. 168, 5989–5992 (2002).

53. Sato, M. et al. Direct binding of Toll-like receptor 2 to zymosan, and zymosan-induced NF-κB activation and TNF-á secretion are down-regulated by lung collectin surfactant protein A. J. Immunol. 171, 417–425 (2003).

62. Rosseau, S. et al. Surfactant protein A down-regulates proinflammatory cytokine production evoked by Candida albicans in human alveolar macrophages and monocytes. J. Immunol. 163, 4495–4502 (1999).

63. McIntosh, J. C., Mervin-Blake, S., Conner, E. & Wright, J. R. Surfactant protein A protects growing cells and reduces TNF-α activity from LPS-stimulated macrophages. Am. J. Physiol. Lung Cell. Mol. Physiol. 271, L310–L319 (1996).

64. Hickling, T. P., Sim, R. B. & Malhotra, R. Induction of TNF-α release from human buffy coat cells by Pseudomonas aeruginosa is reduced by lung surfactant protein A. FEBS Lett. 437, 65–69 (1998).

65. Kremlev, S. G., Umstead, T. M. & Phelps, D. S. Surfactant protein A regulates cytokine production in the monocytic cell line THP-1. Am. J. Physiol. Lung Cell. Mol. Physiol. 272, L996–L1004 (1997).

66. Kremlev, S. G. & Phelps, D. S. Surfactant protein A stimulation of inflammatory cytokine and immunoglobulin production. Am. J. Physiol. Lung Cell. Mol. Physiol. 267, L712–L719 (1994).

67. Sano, H. et al. Pulmonary surfactant protein A modulates the cellular response to smooth and rough lipopolysaccharides by interaction with CD14. J. Immunol. 163, 387–395 (1999).

79. Schagat, T. L., Wofford, J. A. & Wright, J. R. Surfactant protein A enhances alveolar macrophage phagocytosis of apoptotic neutrophils. J. Immunol. 166, 2727–2733 (2001). The ability of SP-A to enhance phagocytosis of apoptotic cells was first reported in this publication.

80. Vandivier, R. W. et al. Role of surfactant proteins A, D, and C1q in the clearance of apoptotic cells in vivo and in vitro: calreticulin and CD91 as a common collectin receptor complex. J. Immunol. 169, 3978–3986 (2002).

Anmerkungen

The source is given for the statement: "This putative receptor gp340 has no transmembrane domain so that it is suggested that it could interact with an adaptor molecule on the surface of the cell", but not for the rest of the page which also follows the source very closely and gives the same references to the literature.

Sichter
(Hindemith), PlagProf:-)

[8.] Mag/Fragment 022 01 - Diskussion
Zuletzt bearbeitet: 2014-03-10 12:10:33 Graf Isolan
Fragment, Gesichtet, Mag, SMWFragment, Schutzlevel sysop, Verschleierung, Wright 2005

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Through the carbohydrate-recognition domains (CRD) and the collagen-like regions it is possible for SP-A and SP-D, as well as MBL, to bind DNA from a variety of origins, including mice and bacteria (Palaniyar et al., 2004). SP-D effectively binds and aggregates alveolar macrophages DNA and it enhances the uptake of DNA by human monocytic cells (Palaniyar et al., 2003). Binding of the collectins to cell-surface DNA might be one mechanism by which they mediate enhanced phagocytosis of apoptotic cells.

Uptake of apoptotic cells by macrophages results in release of anti-inflammatory mediators, such as transforming growth factors-β (TGF-β), IL-10 and prostaglandin E2 (Fadok et al., 1998). This response is in contrast to the release of pro-inflammatory cytokines that occurs when phagocytes ingest microorganisms. In addition to enhancing the uptake of apoptotic cells, SP-A also enhances the release of TGF-β by macrophages (Reidy and Wright, 2003), indicating that SP-A can promote resolution of inflammation at several levels of the apoptotic-cell clearance process and that surfactant proteins can indirectly induce anti-inflammatory responses by phagocytes.

As discussed above, surfactant is linked to innate immunity. However, surfactant is also linked to adaptive immunity in the lung by modulating functions of both dendritic cells and T cells.

It has been shown that SP-A and SP-D have different effects on DC functions. The uptake and presentation of antigens is enhanced by SP-D (Brinker et al., 2001), but only SP-A can inhibit maturation of DC, as assessed by cell-surface marker expression, and functional activity, such as phagocytosis and chemotaxis (Brinker et al., 2003).

The proliferation of T cells stimulated with plant lectins, CD3-specific antibodies or phorbol esters is inhibited by SP-A and SP-D. It has been suggested that the inhibition of IL-2 production might mediate this process (Borron et al., 1996; Borron et al, 1998). In addition, both the collagen-like region and the CRD of SP-A have been implicated in the inhibition of lymphocyte function, probably due to inhibition of calcium signalling (Borron et al., 2002). These data indicate that SP-D and SP-A might provide an important link between innate and adaptive immunity, by modulation of both DC and T cell functions.


Borron P, Veldhuizen RA, Lewis JF, Possmayer F, Caveney A, Inchley K, McFadden RG, Fraher LJ. Surfactant associated protein-A inhibits human lymphocyte proliferation and IL-2 production. Am J Respir Cell Mol Biol. 1996 Jul; 15 (1): 115-21.

Borron P, McCormack FX, Elhalwagi BM, Chroneos ZC, Lewis JF, Zhu S, Wright JR, Shepherd VL, Possmayer F, Inchley K, Fraher LJ. Surfactant protein A inhibits T cell proliferation via its collagen-like tail and a 210-kDa receptor. Am J Physiol. 1998 Oct; 275 (4 Pt 1): L679-86.

Borron PJ, Crouch EC, Lewis JF, Wright JR, Possmayer F, Fraher LJ. Recombinant rat surfactant-associated protein D inhibits human T lymphocyte proliferation and IL-2 production. J Immunol. 1998 Nov 1; 161 (9): 4599-603.

Borron PJ, Mostaghel EA, Doyle C, Walsh ES, McHeyzer-Williams MG, Wright JR. Pulmonary surfactant proteins A and D directly suppress CD3+/CD4+ cell function: evidence for two shared mechanisms. J Immunol. 2002 Nov 15; 169 (10): 5844-50.

Brinker KG, Martin E, Borron P, Mostaghel E, Doyle C, Harding CV, Wright JR. Surfactant protein D enhances bacterial antigen presentation by bone marrow-derived dendritic cells. Am J Physiol Lung Cell Mol Physiol. 2001 Dec; 281 (6): L1453-63.

Brinker KG, Garner H, Wright JR. Surfactant protein A modulates the differentiation of murine bone marrow-derived dendritic cells. Am J Physiol Lung Cell Mol Physiol. 2003 Jan; 284 (1): L232-41. Epub 2002 Sep 13.

Fadok VA, Bratton DL, Konowal A, Freed PW, Westcott JY, Henson PM. Macrophages that have ingested apoptotic cells in vitro inhibit proinflammatory cytokine production through autocrine/paracrine mechanisms involving TGF-beta, PGE2, and PAF. J Clin Invest. 1998 Feb 15; 101 (4): 890-8.

Palaniyar N, Clark H, Nadesalingam J, Hawgood S, Reid KB. Surfactant protein D binds genomic DNA and apoptotic cells, and enhances their clearance, in vivo. Ann N Y Acad Sci. 2003 Dec; 1010: 471-5.

Palaniyar N, Nadesalingam J, Clark H, Shih MJ, Dodds AW, Reid KB. Nucleic acid is a novel ligand for innate, immune pattern recognition collectins surfactant proteins A and D and mannose-binding lectin. J Biol Chem. 2004 Jul 30; 279 (31): 32728-36. Epub 2004 May 15.

Reidy MF, Wright JR. Surfactant protein A enhances apoptotic cell uptake and TGF-beta1 release by inflammatory alveolar macrophages. Am J Physiol Lung Cell Mol Physiol. 2003 Oct; 285 (4): L854-61. Epub 2003 Jun 6.

SP-A and SP-D, as well as MBL, bind DNA from a variety of origins, including mice and bacteria82. Binding occurs through both the CRDs and the collagen-like regions. SP-D effectively binds and aggregates alveolarmacrophage DNA83, and it enhances the uptake of DNA by human monocytic cells84. Binding of the collectins to cell-surface DNA might be one mechanism by which they mediate enhanced phagocytosis of apoptotic cells.

A consequence of apoptotic-body uptake by a phagocyte is induction of an anti-inflammatory response by the phagocyte. For example, macrophage uptake of apoptotic cells results in release of antiinflammatory mediators, such as transforming growth factor-β (TGF-β), IL-10 and prostaglandin E2 (REF. 85)[sic]. This response is in contrast to the release of proinflammatory cytokines that occurs when phagocytes ingest a microorganism. In addition to enhancing the uptake of apoptotic cells, SP-A also enhanced the release of TGF-β by macrophages86, indicating that SP-A can promote resolution of inflammation at several levels of the apoptotic-cell clearance process.

Surfactant links innate and adaptive immunity

Recent studies have provided support for the concept that surfactant might have a role in linking innate and adaptive immunity in the lung by modulating functions of both DCs and T cells. [...]

Recent studies have shown that SP-A and SP-D have different effects on DC functions. For example, SP-D enhances the uptake and presentation of a model antigen expressed by Escherichia coli95. SP-A, but not SP-D, inhibits maturation of DCs, as assessed by cell-surface marker expression, and functional activity, such as phagocytosis and chemotaxis96.

[...] Subsequent studies by Borron and colleagues99,100 showed that SP-A and SP-D inhibit proliferation of T cells that have been stimulated with plant lectins, CD3-specific antibodies or phorbol esters, by a process that is thought to be mediated (at least, in part) by inhibition of IL-2 production. In addition, both the collagen-like region46 and the CRD101 of SP-A have been implicated in the inhibition of lymphocyte function, probably owing to inhibition of calcium signalling102.

[...]

As noted by Shepherd55 in an invited commentary, these studies indicate that SP-D and SP-A might provide an important link between innate and adaptive immunity, by modulation of DC and T-cell functions (FIG. 5).


46. Borron, P. et al. Surfactant protein A inhibits T cell proliferation via its collagen-like tail and a 210-kDa receptor. Am. J. Physiol. Lung Cell. Mol. Physiol. 275, L679–L686 (1998).

82. Palaniyar, N. et al. Nucleic acid is a novel ligand for innate immune pattern recognition collectins surfactant proteins A and D and mannose-binding lectin. J. Biol. Chem. 279, 32728–32736 (2004).

83. Palaniyar, N., Clark, H., Nadesalingam, J., Hawgood, S. & Reid, K. B. Surfactant protein D binds genomic DNA and apoptotic cells, and enhances their clearance, in vivo. Ann. NY Acad. Sci. 1010, 471–475 (2003).

84. Palaniyar, N., Nadesalingam, J. & Reid, K. B. Innate immune collectins bind nucleic acids and enhance DNA clearance in vitro. Ann. NY Acad. Sci. 1010, 467–470 (2003).

85. Fadok, V. A. et al. Macrophages that have ingested apoptotic cells in vitro inhibit proinflammatory cytokine production through autocrine/paracrine mechanisms involving TGF-β, PGE2, and PAF. J. Clin. Invest. 101, 890–898 (1998).

86. Reidy, M. F. & Wright, J. R. Surfactant protein A enhances apoptotic cell uptake and TGF-β1 release by inflammatory alveolar macrophages. Am. J. Physiol. Lung Cell Mol. Physiol. 285, L854–L861 (2003).

95. Brinker, K. G. et al. Surfactant protein D enhances bacterial antigen presentation by bone marrow-derived dendritic cells. Am. J. Physiol. Lung Cell. Mol. Physiol. 281, L1453– L1463 (2001).

96. Brinker, K. G., Garner, H. & Wright, J. R. Surfactant protein A modulates the differentiation of murine bone marrow-derived dendritic cells. Am. J. Physiol. Lung Cell. Mol. Physiol. 284, L232–L241 (2003).

99. Borron, P. et al. Surfactant associated protein-A inhibits human lymphocyte proliferation and IL-2 production. Am. J. Respir. Cell Mol. Biol. 15, 115–121 (1996).

100. Borron, P. J. et al. Recombinant rat surfactant-associated protein D inhibits human T lymphocyte proliferation and IL-2 production. J. Immunol. 161, 4599–4603 (1998).

101. Wang, J. Y., Shieh, C. C., You, P. F., Lei, H. Y. & Reid, K. B. Inhibitory effect of pulmonary surfactant proteins A and D on allergen-induced lymphocyte proliferation and histamine release in children with asthma. Am. J. Respir. Crit. Care Med. 158, 510–518 (1998).

102. Borron, P. J. et al. Pulmonary surfactant proteins A and D directly suppress CD3+/CD4+ cell function: evidence for two shared mechanisms. J. Immunol. 169, 5844–5850 (2002).

Anmerkungen

The source is not given here. Continuation of Fragment_020_08.

Note: there are two publications "Borron et al. 1998" listed in the bibliography.

Sichter
(Hindemith), PlagProf:-)

[9.] Mag/Fragment 023 01 - Diskussion
Zuletzt bearbeitet: 2014-03-10 11:46:35 Graf Isolan
Fragment, KeineWertung, Mag, SMWFragment, Schutzlevel, Wright 2005, ZuSichten

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Figure 4: Collectin receptors. Surfactant protein A (SP-A) and SP-D potentially bind several receptors, including SP-R210, Toll-like receptor 2 (TLR2), TLR4, signal-inhibitory regulatory protein-α (SIRP-α) and CD91-calreticulin. SP-A binds SIRP-α and inhibits production of inflammatory mediators. In contrast, when SP-A is bound to a pathogen or cellular debris, its collagen-like region is bound to CD91-calreticulin and induces inflammatory-mediator production. Nuclear factor κB, (NF-κB); protein kinase C (PKC); SRC homology 2 (SH2)-domain-containing protein tyrosine phosphatase 1 (SHP1) (adapted from Wright, 2005).


Wright JR. Immunoregulatory functions of surfactant proteins. Nat Rev Immunol. 2005 Jan; 5 (1): 58-68. Review.

23a source Mag.png

Figure 4 Collectin receptors. Surfactant protein A (SP-A) and SP-D potentially bind several receptors, including SP-R210, Toll-like receptor 2 (TLR2), TLR4, signal-inhibitory regulatory protein-α (SIRP-α) and CD91-calreticulin. SP-A binds SIRP-α and inhibits production of inflammatory mediators. By contrast, when SP-A is bound to a pathogen or cellular debris, its collagen-like region is bound to CD91-calreticulin and induces inflammatory-mediator production. NF-κB, nuclear factor-κB; PKC, protein kinase C; SHP1, SRC homology 2 (SH2)-domain-containing protein tyrosine phosphatase 1.

Anmerkungen

The source is given, but it is not clear to the reader that the extensive figure caption is taken literally from it. Neither is it clear that "adapted from" actually means "copied from".

Sichter
(Hindemith)

[10.] Mag/Fragment 079 11 - Diskussion
Zuletzt bearbeitet: 2014-03-10 12:22:13 Graf Isolan
Fragment, Gesichtet, KomplettPlagiat, Mag, SMWFragment, Schutzlevel sysop, Wright 2005

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Pulmonary surfactant was initially identified as a lipoprotein complex that reduces surface tension at the air–liquid interface of the lung (Clements, 1957; Pattle, 1955). This definition has been reassessed in light of recent studies that show that surfactant also functions in pulmonary host defence and that surfactant proteins are expressed also in non-pulmonary sites. The host defence functions of surfactant are primarily mediated by SP-A and SP-D, which are members of the collectin family of [proteins.]

Clements JA. Surface tension of lung extracts. Proc Soc Exp Biol Med. 1957 May; 95 (1): 170-2.

Pattle RE. Properties, function and origin of the alveolar lining layer. Nature. 1955 Jun 25; 175 (4469): 1125-6.

Pulmonary surfactant was initially identified as a lipoprotein complex that reduces surface tension at the air–liquid interface of the lung1,2.This definition has been reassessed in light of recent studies that show that surfactant also functions in pulmonary host defence and that surfactant proteins are expressed in non-pulmonary sites. [...]

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


1. Pattle, R. E. Properties, function and origin of the lining layer. Nature 175, 1125–1126 (1955).

2. Clements, J. A. Surface tension of lung extracts. Proc. Soc. Exp. Biol. Med. 95, 170–172 (1957).

Anmerkungen

Though nearly identical nothing has been marked as a citation.

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(Graf Isolan) Schumann

[11.] Mag/Fragment 080 01 - Diskussion
Zuletzt bearbeitet: 2014-03-10 12:18:27 Graf Isolan
BauernOpfer, Fragment, Gesichtet, Mag, SMWFragment, Schutzlevel sysop, Wright 2005

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An emphasis is placed on recent studies showing that, in addition to their well-established role as opsonsins [sic], SP-A and SP-D also have novel functions in initiating parturition, facilitating clearance of apoptotic cells and directly killing bacteria. Furthermore, immunoregulatory functions of the surfactant proteins A und D on T cells are discussed (Wright, 2005).

Wright JR. Immunoregulatory functions of surfactant proteins. Nat Rev Immunol. 2005 Jan; 5 (1): 58-68. Review.

In this review, the structure and immunoregulatory functions of the surfactant proteins SP-A and SP-D are discussed. 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.
Anmerkungen

The source is named at the end. Nevertheless: nothing has been marked as a citation.

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(Graf Isolan) Schumann

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