Lysozyme in human body fluids

Hankiewicz, Jan; Swierczek, Ewa

doi:10.1016/0009-8981(74)90398-2

Cited by 180 publications

(131 citation statements)

References 9 publications

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“…In the serum of healthy people, concentrations in the range of 0.462-2.958 mg/L have been reported [33,35].…”

Section: Properties Of Lysozyme and Its Importance For Daily Lifementioning

confidence: 99%

“…In the human body, lysozyme is indeed widely distributed in tissues and body fluids with the lowest levels found in urine (1.7-123 ng/mL) [32] and cerebrospinal fluid (7.7-84 µg/L) [33] and the highest in gastric juice or mothers' milk (300 mg/L) [34] and tears (1267˘58 mg/L) [35]. In the serum of healthy people, concentrations in the range of 0.462-2.958 mg/L have been reported [33,35].…”

Section: Properties Of Lysozyme and Its Importance For Daily Lifementioning

confidence: 99%

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Aptamer-Based Electrochemical Sensing of Lysozyme

Vasilescu

Wang

et al. 2016

Chemosensors

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Protein analysis and quantification are required daily by thousands of laboratories worldwide for activities ranging from protein characterization to clinical diagnostics. Multiple factors have to be considered when selecting the best detection and quantification assay, including the amount of protein available, its concentration, the presence of interfering molecules, as well as costs and rapidity. This is also the case for lysozyme, a 14.3-kDa protein ubiquitously present in many organisms, that has been identified with a variety of functions: antibacterial activity, a biomarker of several serious medical conditions, a potential allergen in foods or a model of amyloid-type protein aggregation. Since the design of the first lysozyme aptamer in 2001, lysozyme became one of the most intensively-investigated biological target analytes for the design of novel biosensing concepts, particularly with regards to electrochemical aptasensors. In this review, we discuss the state of the art of aptamer-based electrochemical sensing of lysozyme, with emphasis on sensing in serum and real samples.

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“…In the serum of healthy people, concentrations in the range of 0.462-2.958 mg/L have been reported [33,35].…”

Section: Properties Of Lysozyme and Its Importance For Daily Lifementioning

confidence: 99%

Section: Properties Of Lysozyme and Its Importance For Daily Lifementioning

confidence: 99%

Aptamer-Based Electrochemical Sensing of Lysozyme

Vasilescu

Wang

et al. 2016

Chemosensors

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“…counts when incubated with serum, suggests that the serum germination factor has peptidoglycan hydrolysing activity. To our knowledge, the only host enzyme with peptidoglycan hydrolysing activity identified to date is lysozyme (Hankiewicz & Swierczek, 1974;Pier et al, 2004;Prager & Jolles, 1996;Reitamo et al, 1978), which hydrolyses the bacterial cell wall through cleavage of the linkage bond of N-acetylmuramic acid and N-acetyl-D-glucosamine residues of the peptidoglycan (Cole & Ganz, 2005). Our Western blot analyses using monoclonal anti-human lysozyme antibody detected lysozyme-specific immunoreactive bands in HS and HMM fractions, but not in the LMM fraction, results that are consistent with the peptidoglycan hydrolysis activity observed in HS and HMM fractions.…”

Section: Discussionmentioning

confidence: 99%

Host serum factor triggers germination of Clostridium perfringens spores lacking the cortex hydrolysis machinery

Paredes-Sabja

Sarker

2011

Journal of Medical Microbiology

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Clostridium perfringens type A is the causative agent of a variety of histotoxic and enteric diseases. The ability of C. perfringens spores to germinate in vivo might be due to the presence of nutrient germinants in the host tissue and blood. In the current study, we investigated the ability of spores of C. perfringens wild-type and mutation strains to germinate in blood. Results indicate that spores of all three surveyed C. perfringens wild-type isolates germinated better in blood than in brain heart infusion (BHI) broth. However, as expected, spores lacking germinant receptor (GR) protein GerAA or GerKB germinated like wild-type spores in BHI broth and blood. Strikingly, while spores lacking GR proteins GerKA and GerKC showed significantly decreased germination in BHI broth, these spores germinated well in blood, suggesting that blood factor(s) can trigger spore germination through a GR-independent pathway. Using C. perfringens spores lacking cortex lytic enzymes (DcspB or DsleC DsleM), we were able to identify a host serum germination factor with peptidoglycan hydrolysing activity that (i) restored the colony-forming efficiencies of DcspB and DsleC DsleM spores up to~5-20 % of that of total colony-forming spores; (ii) increased the number of c.f.u. of decoated DcspB and DsleC DsleM spores to~99 % of that of colony-forming spores; (iii) and finally lost enzymic activity after heat inactivation, consistent with serum germination factor being an enzyme. Further characterization demonstrated that serum germination factor is very likely lysozyme, which can form a stable high molecular mass complex of 120 kDa in serum.In conclusion, the current study indicates that a host serum germination factor with peptidoglycan hydrolysing activity is capable of triggering germination of C. perfringens spores by directly degrading the spore peptidoglycan cortex. Collectively, this study contributes to our understanding of the mechanism of in vivo germination of spores of C. perfringens. INTRODUCTIONClostridium perfringens is a Gram-positive, spore forming, anaerobic bacterium, which is highly associated with a wide array of gastrointestinal (GI) and histotoxic diseases in both humans and animals (Amimoto et al., 2007; Keyburn et al., 2008;McClane, 2007). However, the most common cause of C. perfringens-associated food poisoning in humans is the consumption of C. perfringens vegetative cells followed by sporulation in the gut (McClane, 2007;Paredes-Sabja & Sarker, 2009). The early steps in the development of C. perfringens-associated gas gangrene and other non-food-borne GI illnesses, such as antibioticassociated diarrhoea, occur when C. perfringens spores ubiquitously found in the environment come in contact with the host, where spores undergo germination followed by outgrowth, cell proliferation and toxin secretion. Therefore, C. perfringens spore germination can be considered as the most essential and earliest step in the progression of gas gangrene and antibiotic-associated diarrhoea.Bacterial spores break their dormancy wh...

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“…The structure of lysozyme was elucidated by Canfield (1963), which consisting of 129 amino acid residues, including 10 carboxyl and 7 amino groups, 11 arginine residues, 6 tryptophan residues and 4 disulfide bonds. Lysozyme is produced by glandular serous cells, surface epithelial cells and macrophages in the human airway (Ganz, 2004;Konstan et al, 1982;Prager and Jollès, 1996) and is present at high concentration in tears, gastric juice and breast milk (Hankiewicz and Swierczek, 1974). Lysozyme catalyzes the hydrolysis of the b (1-4) glycosidic bond of the bacterial peptidoglycan, a major component of the bacterial cell wall (Phillips, 1996).…”

Section: Introductionmentioning

confidence: 99%

The effect of extract from leaves and stalks of Angelica gigas on the innate immunity

Kang¹,

Byeon²,

Kang³

et al. 2013

Korean Journal of Veterinary Service

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The dried root of Angelica gigas (A. gigas) has been traditionally used as an oriental medicine, which is known to improve blood circulation and blood stasis. In the present study, leaves and stalks of A. gigas were used to investigate their effects on the innate immunity. The extracts were prepared from leaves and stalks of A. gigas and were fed to mice. The numbers of blood cells, total WBCs, neutrophils, lymphocytes, eosinophils and basophils were increased by 50% in mice fed with leaves extract of A. gigas compared to control mice. However, the numbers of blood cells were decreased when treated with stalks extract of A. gigas. The level of cholesterol and triglyceride in serum was markedly reduced in both mice group fed with leaves extract and stalks extract of A. gigas compared to control group (P＜0.01). There was no significant change in the level of albumin, total protein, phosphate and calcium in serum. Activity of cationic peptide was found to be diffused in the testicles of mice fed with leaves extract of A. gigas compared to control group, which might be due to increased lysozyme in testicle. The lysoplate assay and immunohistochemistry assay suggest that the extract of leaves and stalks of A. gigas are immunogenic, but the effects might be related with acquired immune response rather than innate immunity.

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Lysozyme in human body fluids

Cited by 180 publications

References 9 publications

Aptamer-Based Electrochemical Sensing of Lysozyme

Aptamer-Based Electrochemical Sensing of Lysozyme

Host serum factor triggers germination of Clostridium perfringens spores lacking the cortex hydrolysis machinery

The effect of extract from leaves and stalks of Angelica gigas on the innate immunity

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