Human ceruminous gland: Ultrastructure and histochemical analysis of antimicrobial and cytoskeletal components

Stoeckelhuber, Mechthild; Matthias, Christoph; Andratschke, Michaela; Stoeckelhuber, Beate M.; Koehler, Claudia; Herzmann, Sabine; Sulz, Astrid; Welsch, Ulrich

doi:10.1002/ar.a.20356

Cited by 47 publications

(46 citation statements)

References 33 publications

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“…Using the method of immunohistochemistry, β-defensin-1 was constitutively expressed in different glandular structures such as the human mammary gland, 36 ceruminous gland, 27,37 and human glands of Moll. 38 Human β-defensin-1 mRNA was detected in minor salivary glands.…”

Section: Discussionmentioning

confidence: 99%

Labial Salivary Glands in Infants

Stoeckelhuber

Loeffelbein

Olzowy

et al. 2016

J Histochem Cytochem.

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SummaryHuman labial glands secrete mucous and serous substances for maintaining oral health. The normal microbial flora of the oral cavity is regulated by the acquired and innate immune systems. The localization and distribution of proteins of the innate immune system were investigated in serous acinar cells and the ductal system by the method of immunohistochemistry. Numerous antimicrobial proteins could be detected in the labial glands: β-defensin-1, -2, -3; lysozyme; lactoferrin; and cathelicidin. Cytoskeletal components such as actin, myosin II, cytokeratins 7 and 19, α-and β-tubulin were predominantly observed in apical cell regions and may be involved in secretory activities. (J Histochem Cytochem 64:502-510, 2016)

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Section: Discussionmentioning

confidence: 99%

Labial Salivary Glands in Infants

Stoeckelhuber

Loeffelbein

Olzowy

et al. 2016

J Histochem Cytochem.

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“…Mammary glands bear developmental and structural resemblance to apocrine glands, which led to the hypothesis that mammary glands are derived from ancient apocrine-like glands (Oftedal, 2002b). One can imagine a scenario in which an ancestral apocrine secretion entailed the secretion of apical blebs containing cytoplasm, secretory vesicles and perhaps cytoplasmic lipid droplets, similar to the process described for some specialized apocrine glands, such as human axillary apocrine glands, glands of Moll, ceruminous glands in the outer ear canal, and rodent Harderian glands (Gesase and Satoh, 2003;Stoeckelhuber et al, 2003;Stoeckelhuber et al, 2006;Stoeckelhuber et al, 2011). With an upregulation of mammary fat synthesis, mechanisms may have evolved to minimize cytoplasmic loss to a few cytoplasmic crescents, as in milk secretion.…”

Section: Evolution Of Milk Secretionmentioning

confidence: 99%

The evolution of milk secretion and its ancient origins

Oftedal

2012

Animal

203

142

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Lactation represents an important element of the life history strategies of all mammals, whether monotreme, marsupial, or eutherian. Milk originated as a glandular skin secretion in synapsids (the lineage ancestral to mammals), perhaps as early as the Pennsylvanian period, that is, approximately 310 million years ago (mya). Early synapsids laid eggs with parchment-like shells intolerant of desiccation and apparently dependent on glandular skin secretions for moisture. Mammary glands probably evolved from apocrine-like glands that combined multiple modes of secretion and developed in association with hair follicles. Comparative analyses of the evolutionary origin of milk constituents support a scenario in which these secretions evolved into a nutrient-rich milk long before mammals arose. A variety of antimicrobial and secretory constituents were co-opted into novel roles related to nutrition of the young. Secretory calcium-binding phosphoproteins may originally have had a role in calcium delivery to eggs; however, by evolving into large, complex casein micelles, they took on an important role in transport of amino acids, calcium and phosphorus. Several proteins involved in immunity, including an ancestral butyrophilin and xanthine oxidoreductase, were incorporated into a novel membrane-bound lipid droplet (the milk fat globule) that became a primary mode of energy transfer. An ancestral c-lysozyme lost its lytic functions in favor of a role as a-lactalbumin, which modifies a galactosyltransferase to recognize glucose as an acceptor, leading to the synthesis of novel milk sugars, of which free oligosaccharides may have predated free lactose. An ancestral lipocalin and an ancestral whey acidic protein four-disulphide core protein apparently lost their original transport and antimicrobial functions when they became the whey proteins b-lactoglobulin and whey acidic protein, which with a-lactalbumin provide limiting sulfur amino acids to the young. By the late Triassic period (ca 210 mya), mammaliaforms (mammalian ancestors) were endothermic (requiring fluid to replace incubatory water losses of eggs), very small in size (making large eggs impossible), and had rapid growth and limited tooth replacement (indicating delayed onset of feeding and reliance on milk). Thus, milk had already supplanted egg yolk as the primary nutrient source, and by the Jurassic period (ca 170 mya) vitellogenin genes were being lost. All primary milk constituents evolved before the appearance of mammals, and some constituents may have origins that predate the split of the synapsids from sauropsids (the lineage leading to 'reptiles' and birds). Thus, the modern dairy industry is built upon a very old foundation, the cornerstones of which were laid even before dinosaurs ruled the earth in the Jurassic and Cretaceous periods.Keywords: evolution, lactation, milk composition, casein, milk fat globule ImplicationsLactation has an evolutionary origin and biological context within which its secretory processes and milk constituents evolved. This revi...

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“…On the other hand there are several reports describing an antimicrobial effect of ear wax with an effect against a wide range of bacteria including Haemophilus influenzae, Staphylococcus aureus, Escherichia coli and fungi [61][62][63][64][65][66]. Stoeckelhuber et al reported the detection of the antimicrobial proteins ß-defensin-1, ß-defensin-2, cathelicidin, lysozyme, lactoferrin, MUC1 and the secretory component of IgA in the ceruminous glandular cells by histochemical analysis [67]. It could be shown that not only the glands but also the skin of the EAC produce antimicrobial peptides like human ß-Defensin 1 (hBD1) and human ß-Defensin 2 (hBD2) [68][69].…”

Section: Discussionmentioning

confidence: 99%

“…These 9 samples consist of cells and not cell bound proteins. The sources for hBD1-2 and lactoferrin have been reported to be in the ceruminous glands, the skin of the external canal and the tympanic membrane [67][68][69]. HNP 1-3 are released into the extracellular space by exocytosis from the azurophilic granules of neutrophiles in general [42] although this is the first report on the existence of HNP 1-3 as well as hBD3 in the human EAC.…”

Section: Discussionmentioning

confidence: 99%

Human antimicrobial proteins in ear wax

Schwaab

Gurr

Neumann

et al. 2011

Eur J Clin Microbiol Infect Dis

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Introduction Antimicrobial peptides (AMP)Generally speaking surfaces like the skin or the oral mucosa are protected by several factors including the adaptive and innate immune systems against invading bacteria and fungi. The antimicrobial mucosal shield of the human airways has been subject of several studies and is well investigated [1][2][3]. A growing number of different human antimicrobial peptides (AMP) have been described which are produced e. g. by surface epithelial cells or by neutrophil granulocytes. The AMPs have a broad, but not identical spectrum of antimicrobial activity against bacteria, virus or fungi. A synergistic and additive effect of different AMPs has been reported [4]. In addition to their antimicrobial charactics, AMPs play a major part in inflammation, immune activation, and wound healing [5][6][7]. Some of the well described AMPs are subject to this study and therefore will be further described. The human ß-Defensins (hBD)The family of human ß-Defensins (hBD) is named after their beta-sheet structure which is stabilised by intramolecular disulfide bonds. Human ß-Defensin 1 (hBD1) was first isolated from hemofiltrate [8] and is expressed in epithelial cells of the urinary, respiratory tract and in keratinocytes [9][10]. It has a strong antimicrobial effect on Gram-negative bacteria [11][12]. Human ß-Defensin 2 (hBD2) is an inducible (by Escherichia coli, Pseudomonas aeruginosa, Helicobacter pylori, Lipoprotienacid, Candida albicans, TumorNecrosis-Factor-α, Interleucine1-ß) peptide [13][14][15] with a strong antimicrobial effect on Escherichia coli, Pseudomonas aeruginosa and Candida albicans, and a relatively weak effect on Staphylococcus aureus [13]. The human ß-Defensin 3 (hBD3) can be induced by tumor necrosis factor α and contact with Pseudmonas aeruginosa or Staphalyococcus aureus e. g. in keratinocytes [16]. HBD3 has antimicrobial activity against Staphylococcus aureus, including Methicillin restistant Staphylococcus aureus (MRSA), Streptococcus pyogenes, Pseudomonas aeruginosa, Escherichia coli, Vancomycin-resistant Enterococcus faecium, Candida albicans and Haemophilus influenza [9; 12; 17]. Human LL-37 (LL-37)LL-37 is the 37-amino acid long C-terminus and the antimicrobial active component of the human Cathelicidin antimicrobial peptide 18 (hCAP-18). It is expressed in leukocytes (monocytes, neutrophiles, T-cells, B-cells), epithelial cells (skin, gastrointestinal and respiratory tract) and secreted into wound and airway surface fluid [18][19][20][21]. LL-37 alone and in combination with other AMPs is bactericidal against a broad spectrum of [21][22][23]. Apart from the antimicrobial activity LL-37 plays a role in angiogenesis, cancer development, neutralisation of bacterial lipopolysaccharide and is chemotactic for human monocytes, neutrophils and CD 4 T-lymphocytes [24-26.]. Human Secretory Leucoprotease Inhibitor (hSLPI)hSLPI is a 11.7-kDa heavy protein which is expressed in macrophages, neutrophils and epithelial cells [27-28.].The antimicrobial activity against Gram-negativ...

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Human ceruminous gland: Ultrastructure and histochemical analysis of antimicrobial and cytoskeletal components

Cited by 47 publications

References 33 publications

Labial Salivary Glands in Infants

Labial Salivary Glands in Infants

The evolution of milk secretion and its ancient origins

Human antimicrobial proteins in ear wax

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