Inhibition of growth and cysteine proteinase activity of <i>Staphylococcus aureus</i> V8 by phosphorylated cystatin α in skin cornified envelope

Takahashi, Masahide; Tezuka, Tadashi; Katunuma, Nobuhiko

doi:10.1016/0014-5793(94)01196-6

Cited by 48 publications

(22 citation statements)

References 19 publications

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“…We observed that the activity of cysteine proteases decreased significantly when the microorganisms were cultured in the presence of various concentrations of chicken cystatin and compared to cultures without inhibitor added. Naito et al (1995) showed the growth of Porphyromonas gingivalis, an oral pathogen secreting a large number of proteolytic enzymes, including cysteine proteases, is inhibited by rat cystatin S. In line with this, the phosphorylated rat cystatin A was used successfully to inhibit the growth of Staphylococcus aureus and its cysteine protease activity (Takahashi et al 1994). A number of studies have shown that the N-terminal part of the inhibitor, in particular of members of the cystatin family, is important in interaction with cysteine proteases (Bjork et al 1994).…”

Section: Discussionmentioning

confidence: 91%

Antimicrobial activity of chicken egg white cystatin

Węsierska

Saleh

Trziszka

et al. 2005

World J Microbiol Biotechnol

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The cysteine protease inhibitor cystatin was purified from chicken egg white and its antimicrobial activity determined for a series of pathogenic bacteria. The results indicate that Acinetobacter lwoffii, Escherichia coli, Oligella sp. and Pseudomonas aeruginosa are highly sensitive to low concentrations of cystatin, which possesses bactericidal activity. No inhibition was observed with a Citrobacter freundii strain. Fifty percent growth inhibition (IC 50 ) was observed at cystatin concentrations in the range of 80 and 100 lg/ml, and the growth was completely inhibited at concentrations in the range of 100 and 200 lg/ml. Fifty percent growth inhibition (IC 50 ) for Staphylococcus aureus, Staphylococcus gallinarum, and Staphylococcus xylosus strains was observed at 150 and 200 lg of cystatin/ml respectively, and growth was completely inhibited at cystatin concentrations in the range of 300 and 1000 lg/ml. The activity of cysteine proteases was significantly decreased in the culture supernatant of microorganisms when chicken cystatin was added. In this study, we observed that chicken cystatin may be a candidate for antibacterial drug development aiming at controlling bacterial pathogens including Escherichia coli, Pseudomonas aeruginosa, and another possible application might be as a therapeutic agent for health improvement.

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Section: Discussionmentioning

confidence: 91%

Antimicrobial activity of chicken egg white cystatin

Węsierska

Saleh

Trziszka

et al. 2005

World J Microbiol Biotechnol

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“…Cystatin A has been identified as a minor (2-5%) crosslinked component of CE and suggested to contribute to bacteriostatic properties of skin [7][8][9]. Indeed, Takahashi et al [10] were able to demonstrate that cystatin a (a rat counterpart of cystatin A) depleted rat skin is more sensitive to Staphylococcus aureus colony formation compared to normal skin.…”

Section: Cystatin a (Stefin A)mentioning

confidence: 96%

Proteinaceous cysteine protease inhibitors

Dubin

2005

CMLS, Cell. Mol. Life Sci.

121

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Studies of proteinaceous cysteine protease inhibitors originated with the discovery of cystatins in the 1960s. Since that time, a rich and fascinating world of proteins that control and regulate a multitude of important physiological processes, ranging from the basics of protein turnover to development and brain function, has been uncovered. Failures in such important and complex systems inevitably lead to pathologies. Many threatening diseases such as cancer or neurological disorders, to mention only some, are attributed to deregulation of protease-inhibitor balance. Moreover, important aspects of infection pathology and host defense rely on proteolysis and protease inhibition. Recent advances in the field of protease inhibitors have drawn attention to the possible use of this collected knowledge to control related pathological processes. This review attempts to familiarize the reader with proteinaceous cysteine protease inhibitors by providing an overview of current knowledge. The work primarily highlights biological processes in which the inhibitors are involved and focuses on pathologies resulting from aberrant protease-inhibitor balance, pointing out emerging possibilities for their correction.

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“…Filaggrin [14] is thought to be a precursor protein which is degraded by epidermal proteinases, such as cathepsin D to free amino acids in the stratum corneum [9,12,[19][20][21]. In addition, cystatin A(α) [24], also known as stefin A [27], which is a cysteine protease inhibitor, suppresses the colonization of the skin by S. aureus [25], and both Ted-H-1 antigen [26] and involucrin are present on the stratum corneum cell membrane and play some role on the defence mechanism of the stratum corneum. Therefore, the expressions of these four proteins in lesional and nonlesional skin of AD patients were determined in this study.…”

Section: Introductionmentioning

confidence: 99%

Decreased expression of filaggrin in atopic skin

et al. 1996

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The amounts of the epidermal proteins filaggrin, involucrin, cystatin A and Ted-H-1 antigen produced during the terminal differentiation of keratinocytes were immunohistochemically measured in lesional and nonlesional skin of atopic dermatitis (AD) patients. In addition, the amount of filaggrin in the skin of the inner surface of the upper arm of AD patients (nonlesional skin) and normal controls, obtained by punch biopsy, was measured by an enzyme-linked immunosorbent assay (ELISA) technique. The immunohistochemical study showed that all four proteins were decreased in lesional skin. By contrast, only filaggrin was decreased in nonlesional skin of AD patients. The ELISA showed that the amount of filaggrin in the skin of the inner surface of the upper arm was 2.48 +/- 0.45 microgram/7 mm2 (n = 8) in AD patients, which was 32% of that in the normal controls (7.7 +/- 0.55 microgram/7 mm2; n = 4). This decrease in filaggrin production in atopic skin may be one of the reasons why atopic skin can easily become dry, because filaggrin is thought to be the precursor protein of the emollient factors in the stratum corneum. The evidence that only the expression of filaggrin was suppressed in AD patients, though the genes of filaggrin and involucrin are localized to a very restricted portion of the same gene 1q21, indicates that the filaggrin gene does not share regulatory elements with the involucrin gene.

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Inhibition of growth and cysteine proteinase activity of Staphylococcus aureus V8 by phosphorylated cystatin α in skin cornified envelope

Cited by 48 publications

References 19 publications

Antimicrobial activity of chicken egg white cystatin

Antimicrobial activity of chicken egg white cystatin

Proteinaceous cysteine protease inhibitors

Decreased expression of filaggrin in atopic skin

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