Detection of Antimicrobial Peptides in Human Nasolacrimal Ducts.

Paulsen, Friedrich; Schaudig, Ulrich; Held‐Feindt, Janka; Lehmann, Jan; Schröder, Jens‐M.; Tillmann, Bernhard

doi:10.1097/00003226-200011002-00142

Cited by 29 publications

(38 citation statements)

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“…Constitutive expression of BPI on the mRNA and protein level has also been demonstrated for human gastrointestinal epithelial cells [38], dermal fibroblasts [39] as well as for basal epithelial cells of the excretory lacrimal gland ducts [40,41] and human genital tract epithelial cells [42]. A role for transcription factors of the Sp1/3 and C/EBP group in BPI expression by the human gastrointestinal epithelial tumor cell line CaCo-2 has been suggested.…”

Section: Bpi: Expression and Localizationmentioning

confidence: 87%

“…ATLa is an anti-inflammatory lipid metabolite, deriving from short-lived arachidonic acid metabolites, that accumulate in the late (resolution) phase of tissue-based inflammatory responses [43,44]. The effects on BPI expression of ATLa are apparently specific (i.e., treatment of CaCo-2 cells with proinflammatory cytokines (TNF, interferon gamma, IL-4, IL-1) or Gram-negative or Grampositive bacteria did not increase BPI expression in CaCo-2 cells) and also demonstrable in other epithelia [38,40,45]. In contrast, in dermal fibroblasts only IL-4 could raise BPI protein levels above baseline levels [39].…”

Section: Bpi: Expression and Localizationmentioning

confidence: 99%

“…The extent to which basal expression of BPI in tissue by other cells (e.g., epithelia, connective tissue) could be functionally significant is unclear [38,39,42,[77][78][79]. Tissue-derived BPI has been found on apical and basolateral epithelial surfaces [38,40,42] and on dermal fibroblasts [39] derived from subcutaneous connective tissue, however, its quantitative contribution to the initial host interactions with GNB in tissue are as yet unknown. The presence of BPI at these sites could enhance the ability of local defenses to eliminate small amounts of invading bacteria and also diminish the availability of endotoxin for stimulation of sub-epithelial host cells via the LBP/CD14/MD-2/TLR4 pathway [80][81][82].…”

Section: Bpi Actions During Host: Gnb Interactionsmentioning

confidence: 99%

“…The sub-lethal effects of BPI can be amplified by synergistic actions with other neutrophil granule proteins [91][92][93][94][95] and with extracellular antimicrobial proteins that are mobilized in neutrophil-rich inflammatory exudates, including group IIA phospholipase A2 (gIIA PLA2) and complement [96][97][98]. These combined actions can take place both within neutrophils after uptake of the PLA2 and complement with bacteria during phagocytosis [97,98] and in the extracellular inflammatory fluid [40,86,[99][100][101]. Levels of BPI in cell-free inflammatory fluid of neutrophil-rich exudates are functionally significant (≥10 nM) and co-exist with other antimicrobial host factors that can act in concert with BPI [76,86,[100][101][102][103][104].…”

Section: Bpi Actions During Host: Gnb Interactionsmentioning

confidence: 99%

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The bactericidal/permeability-increasing protein (BPI) in infection and inflammatory disease

Schultz

Weiss

2007

Clinica Chimica Acta

114

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Gram-negative bacteria (GNB) and their endotoxin present a constant environmental challenge. Endotoxins can potently signal mobilization of host defenses against invading GNB but also potentially induce severe pathophysiology, necessitating controlled initiation and resolution of endotoxin-induced inflammation to maintain host integrity. The bactericidal/permeability-increasing protein (BPI) is a pluripotent protein expressed, in humans, mainly neutrophils. BPI exhibits strong anti-microbial activity against GNB and potent endotoxin-neutralizing activity. BPI mobilized with neutrophils in response to invading GNB can promote intracellular and extracellular bacterial killing, endotoxin neutralization and clearance, and delivery of GNB outer membrane antigens to dendritic cells. Tissue expression by dermal fibroblasts and epithelia could further amplify local levels of BPI and local interaction with GNB and endotoxin, helping to constrain local tissue infection and inflammation and prevent systemic infection and systemic inflammation. This review article focuses on the structural and functional properties of BPI with respect to its contribution to host defense during GNB infections and endotoxin-induced inflammation and the genesis of auto-antibodies against BPI that can blunt BPI activity and potentially contribute to chronic inflammatory disease.

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Section: Bpi: Expression and Localizationmentioning

confidence: 87%

Section: Bpi: Expression and Localizationmentioning

confidence: 99%

Section: Bpi Actions During Host: Gnb Interactionsmentioning

confidence: 99%

Section: Bpi Actions During Host: Gnb Interactionsmentioning

confidence: 99%

See 2 more Smart Citations

The bactericidal/permeability-increasing protein (BPI) in infection and inflammatory disease

Schultz

Weiss

2007

Clinica Chimica Acta

114

View full text Add to dashboard Cite

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“…Gueze et al (7) considered that the broad distribution of GP2 along the entire length of the plasma membrane is explained by two mechanisms: GP2 originates from exocytosis-derived apical GP2 or is added directly to the basolateral the stratified squamous epithelium, though it has been described as "a multilayered epithelium" in the rat (30). Epithelium of the human nasolacrimal ducts is known to have an active secretory function of antimicrobial peptides, such as defensins, secretory phospholipase A 2 , lysozyme, and lactoferrin (29). The present study added another peptide to the list.…”

Section: Gp2-producing Cells In the Lacrimal Canaliculi Lacrimal Sacmentioning

confidence: 99%

<b>GP2-expressing cells in the conjunctiva and tear ducts of mice: identification of a novel type of cells in the squamous stratified </b><b>epithelium </b>

et al. 2015

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GP2 is a membrane-associated secretory protein originally identified in zymogen granules of pancreatic acinar cells. Recently, this glycoprotein has attracted attention as a marker substance of M cells of Peyer's patches and for its involvement in the selective uptake of pathological bacteria via M cells. When we stained the conjunctiva and tear ducts of mice using a GP2 antibody, all goblet cells in the squamous stratified epithelium of the conjunctiva were intensely immunolabeled, while goblet cells in the intestine and airway were devoid of the immunoreactivity, indicating that the conjunctiva contains a special type of goblet cell. Further immunostaining for GP-2 labeled dispersed cells of peculiar shapes within the stratified squamous epithelium in the lacrimal canaliculi, lacrimal sac, and nasolacrimal duct. The GP2-immunoreactive cells in the tear duct projected arched or branched processes toward the basement membrane. Electron-microscopically, immunogold particles for GP2 outlined the basolateral plasma membrane of both the conjuntival goblet cells and the peculiarly shaped cells in the tear duct. Intracellularly, GP2 products of the goblet cells were localized around secretory granules in the apical cytoplasm and those of the tear duct cells inside the vesicles. The luminal contents close to apical plasma membrane were heavily labeled with immunogold particles, suggesting an exocytosis-based targeting of GP2 to the plasma membrane and its release into the lumen. The possible function of GP2 in tear ducts is discussed in relation to a defense system against invasive microoranisms and antigens.Tears contain various substances, such as lipids, mucins, ions, enzymes, and immunoglobulins. Mucins originate mostly in conjunctival goblet cells and the lacrimal glands (1, 13, 36), the latter being mucous in nature in some animals. The main and accessory lacrimal glands also secrete antimicrobial substances including lysozyme, lactoferrin, and lipocalin in both basal and reflex tear secretions (for review, 24). Secretory immunoglobulin A, the major antibody present in the tear film and tear fluid, is produced by plasma cells in cooperation with lacrimal glands and conjunctival lymphoid tissues (24). The antimicrobial enzymes, immunoglobulins, and complement factors assure immunologic functions against microorganisms and antigens. It is generally believed that conjunctival goblet cells are not directly involved in the ocular defense system. In the intestine, however, morphological studies for longer than 100 years have reported the existence of intermediate cells between goblet cells and Paneth cells, the latter a predominant cell source of antimicrobial substances in the small intestine (3). Numbers of the intermediate cells increased in the intestine of mice with abnormal Notch signaling (37) or with the infection of parasitic nematodes (15). Furthermore, goblet cells in the small intestine possess an ability to uptake luminal antigens and present them to sub-

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Human Antimicrobial Peptides in Bodily Fluids: Current Knowledge and Therapeutic Perspectives in the Postantibiotic Era

Bastos

Trindade

Costa

et al. 2017

Medicinal Research Reviews

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Antimicrobial peptides (AMPs) are an integral part of the innate immune defense mechanism of many organisms. Due to the alarming increase of resistance to antimicrobial therapeutics, a growing interest in alternative antimicrobial agents has led to the exploitation of AMPs, both synthetic and isolated from natural sources. Thus, many peptide-based drugs have been the focus of increasing attention by many researchers not only in identifying novel AMPs, but in defining mechanisms of antimicrobial peptide activity as well. Herein, we review the available strategies for the identification of AMPs in human body fluids and their mechanism(s) of action. In addition, an overview of the distribution of AMPs across different human body fluids is provided, as well as its relation with microorganisms and infectious conditions.

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Detection of Antimicrobial Peptides in Human Nasolacrimal Ducts.

Cited by 29 publications

References 0 publications

The bactericidal/permeability-increasing protein (BPI) in infection and inflammatory disease

The bactericidal/permeability-increasing protein (BPI) in infection and inflammatory disease

<b>GP2-expressing cells in the conjunctiva and tear ducts of mice: identification of a novel type of cells in the squamous stratified </b><b>epithelium </b>

Human Antimicrobial Peptides in Bodily Fluids: Current Knowledge and Therapeutic Perspectives in the Postantibiotic Era

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