Tear Film and Ocular Surface Surfactants

Bräuer, Lars; Paulsen, Friedrich

doi:10.2174/1875044300801010062

Cited by 16 publications

(17 citation statements)

References 68 publications

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“…These domains and the palmitoylation of the protein also support the hypothesis that SP-G may be integrated into and anchored within a lipid phase, as can be found within actual accepted models of the tear film [78], [79]. Our calculations showed that SP-G is able to reside in vicinity of lipid systems and may also interact with them.…”

Section: Discussionsupporting

confidence: 85%

“SP-G”, a Putative New Surfactant Protein – Tissue Localization and 3D Structure

et al. 2012

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Surfactant proteins (SP) are well known from human lung. These proteins assist the formation of a monolayer of surface-active phospholipids at the liquid-air interface of the alveolar lining, play a major role in lowering the surface tension of interfaces, and have functions in innate and adaptive immune defense. During recent years it became obvious that SPs are also part of other tissues and fluids such as tear fluid, gingiva, saliva, the nasolacrimal system, and kidney. Recently, a putative new surfactant protein (SFTA2 or SP-G) was identified, which has no sequence or structural identity to the already know surfactant proteins. In this work, computational chemistry and molecular-biological methods were combined to localize and characterize SP-G. With the help of a protein structure model, specific antibodies were obtained which allowed the detection of SP-G not only on mRNA but also on protein level. The localization of this protein in different human tissues, sequence based prediction tools for posttranslational modifications and molecular dynamic simulations reveal that SP-G has physicochemical properties similar to the already known surfactant proteins B and C. This includes also the possibility of interactions with lipid systems and with that, a potential surface-regulatory feature of SP-G. In conclusion, the results indicate SP-G as a new surfactant protein which represents an until now unknown surfactant protein class.

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Section: Discussionsupporting

confidence: 85%

“SP-G”, a Putative New Surfactant Protein – Tissue Localization and 3D Structure

et al. 2012

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“…As saliva plays an important role in maintaining the health of the oral cavity, an immunological function of the detected surfactant proteins SP-A and SP-D, well known from lung and other mucosal surfaces (for review see Bräuer and Paulsen 2008), is not astonishing. In this context, Lee et al (2005) demonstrated that SP-A is up-regulated in forms of chronic sialadenitis, which is caused by microorganisms.…”

Section: Discussionmentioning

confidence: 99%

Human parotid and submandibular glands express and secrete surfactant proteins A, B, C and D

Bräuer

Möschter

Beileke

et al. 2009

Histochem Cell Biol

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The oral cavity and the salivary glands are open to the oral environment and are thus exposed to multiple microbiological, chemical and mechanical influences. The existence of an efficient defense system is essential to ensure healthy and physiological function of the oral cavity. Surfactant proteins play an important role in innate immunity and surface stability of fluids. This study aimed to evaluate the expression and presence of surfactant proteins (SP) A, B, C, and D in human salivary glands and saliva. The expression of mRNA for SP-A, -B, -C and -D was analyzed by RT-PCR in healthy parotid and submandibular glands. Deposition of all surfactant proteins was determined with monoclonal antibodies by means of Western blot analysis and immunohistochemistry in healthy tissues and saliva of volunteers. Our results show that all four surfactant proteins SP-A, SP-B, SP-C and SP-D are peptides of saliva and salivary glands. Based on the known direct and indirect antimicrobial effects of collectins, the surfactant-associated proteins A and D appear to be involved in immune defense inside the oral cavity. Furthermore, by lowering surface tension between saliva and the epithelial lining of excretory ducts, SP-B and SP-C may assist in drainage and outflow into the oral cavity. Further functions such as pellicle formation on teeth have yet to be determined.

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“…In innate host defense, ANG is a component of tears and protects the ocular surface as an antimicrobial peptide [114,115]. ANG is also abundantly induced in Paneth cells and has been demonstrated to act as a factor for innate antimicrobial defense of the intestine [13].…”

Section: Ang Participates In Immune Responsesmentioning

confidence: 99%

Three decades of research on angiogenin: a review and perspective

Sheng¹,

Xu²

2016

ABBS

182

201

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As a member of the vertebrate-specific secreted ribonucleases, angiogenin (ANG) was first isolated and identified solely by its ability to induce new blood vessel formation, and now, it has been recognized to play important roles in various physiological and pathological processes through regulating cell proliferation, survival, migration, invasion, and/or differentiation. ANG exhibits very weak ribonucleolytic activity that is critical for its biological functions, and exerts its functions through activating different signaling transduction pathways in different target cells. A series of recent studies have indicated that ANG contributes to cellular nucleic acid metabolism. Here, we comprehensively review the results of studies regarding the structure, mechanism, and function of ANG over the past three decades. Moreover, current problems and future research directions of ANG are discussed. The understanding of the function and mechanism of ANG in a wide context will help to better delineate its roles in diseases, especially in cancer and neurodegenerative diseases.

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Tear Film and Ocular Surface Surfactants

Cited by 16 publications

References 68 publications

“SP-G”, a Putative New Surfactant Protein – Tissue Localization and 3D Structure

“SP-G”, a Putative New Surfactant Protein – Tissue Localization and 3D Structure

Human parotid and submandibular glands express and secrete surfactant proteins A, B, C and D

Three decades of research on angiogenin: a review and perspective

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