Antimicrobial skin peptides and proteins

Schröder, Jens‐M.; Harder, Jürgen

doi:10.1007/s00018-005-5364-0

Cited by 226 publications

(233 citation statements)

References 138 publications

(227 reference statements)

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“…In addition to the physical barrier of intact skin, the existence of a chemical barrier consisting of antimicrobial peptides/proteins (AMPs) 2 in a wide variety of organisms might contribute to the natural defense of skin against microbial infections (2)(3)(4). For example, secretion of defensins, psoriasin (S100A7), and hRNase 7 usually protects human skin against infection by most bacteria (5)(6)(7)(8).…”

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confidence: 99%

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Outer Membrane Protein I of Pseudomonas aeruginosa Is a Target of Cationic Antimicrobial Peptide/Protein

Lin

Chang

et al. 2010

Journal of Biological Chemistry

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Cationic antimicrobial peptides/proteins (AMPs) are important components of the host innate defense mechanisms against invading microorganisms. Here we demonstrate that OprI (outer membrane protein I) of Pseudomonas aeruginosa is responsible for its susceptibility to human ribonuclease 7 (hRNase 7) and ␣-helical cationic AMPs, instead of surface lipopolysaccharide, which is the initial binding site of cationic AMPs. The antimicrobial activities of hRNase 7 and ␣-helical cationic AMPs against P. aeruginosa were inhibited by the addition of exogenous OprI or anti-OprI antibody. On modification and internalization of OprI by hRNase 7 into cytosol, the bacterial membrane became permeable to metabolites. The lipoprotein was predicted to consist of an extended loop at the N terminus for hRNase 7/lipopolysaccharide binding, a trimeric ␣-helix, and a lysine residue at the C terminus for cell wall anchoring. Our findings highlight a novel mechanism of antimicrobial activity and document a previously unexplored target of ␣-helical cationic AMPs, which may be used for screening drugs to treat antibiotic-resistant bacterial infection.

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confidence: 99%

“…These AMPs have multiple modes of action that differ from those of conventional antibiotics (2,8,13). Until now, most studies have proceeded on the tacit assumption that cationic AMPs act on bacteria through electrostatic interactions and that lipopolysaccharide (LPS) is the initial AMP-binding site in Gram-negative bacteria.…”

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confidence: 99%

Outer Membrane Protein I of Pseudomonas aeruginosa Is a Target of Cationic Antimicrobial Peptide/Protein

Lin

Chang

et al. 2010

Journal of Biological Chemistry

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“…S100A7 has been well studied and owes its name to the fact that it is detected in high quantity in psoriatic skin lesions compared with normal skin 55) . S100A7 (psoriasin) is believed to be the principal AMP/HDP constitutively expressed in normal skin 56) , although its expression is also inducible by Th1-, Th17-and Th22-cytokines, EGF, IGF-1, vitamin D, calcium, sodium butyrate, bacteria and microbial products 57)-60) .…”

Section: Human Cathelicidin Ll-37mentioning

confidence: 99%

Novel Insight Into the Role of Antimicrobial (Host Defense) Peptides/Proteins in Human Skin Diseases

Niyonsaba

2016

Juntendo Medical Journal

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In addition to functioning as a physical barrier, the skin has evolved several innate defense mechanisms for the rapid recognition of and protection against harmful microorganisms. As a part of this process, the skin releases a vast and powerful arsenal of antimicrobial peptides/proteins (AMPs), also called host defense peptides/proteins (HDPs), which are key players in the cutaneous immune system. Although originally named antimicrobial peptides, recent evidence has demonstrated that AMPs/HDPs play additional roles in orchestrating the adaptive immune response, such as the regulation of inflammation, induction of cell proliferation and differentiation, regulation of cytokine/chemokine production, facilitation of cell migration, promotion of wound healing and regulation of tight junction barriers. Additionally, numerous skin diseases show altered expression of AMPs/HDPs in the lesional skin, suggesting the crucial roles of these molecules in the pathophysiology of skin diseases. The purpose of this review is to describe the current knowledge regarding some of the most common and well-known AMPs/HDPs derived from the skin, to discuss the regulation of their expression and their antimicrobial and immunomodulatory functions, and to outline their roles in various skin diseases. We believe that understanding the basic knowledge of skin-derived AMPs/HDPs would provide new insight into the pathophysiology of skin disorders and offer novel therapeutic opportunities for skin infectious diseases.

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“…While some are expressed very focally within tissues and induced more generally only under stress conditions, others are not expressed in normal tissues but are highly inducible by cytokines. The S100A7 protein is an inducible antimicrobial peptide, known to be involved in innate immunity and epithelial defense (Glaser et al 2005, Schroder & Harder 2006, Harder et al 2007, Arnett & Seveau 2011. S100A7 was originally identified in skin but was subsequently shown to be expressed in certain tumour types and stages.…”

Section: Cd68mentioning

confidence: 99%

Intratumoural inflammation and endocrine resistance in breast cancer

Murray¹,

West²,

Murphy³

et al. 2014

Endocrine-Related Cancer

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It is becoming clear that inflammation-associated mechanisms can affect progression of breast cancer and modulate responses to treatment. Estrogen receptor alpha (ERa (ESR1)) is the principal biomarker and therapeutic target for endocrine therapies in breast cancer. Over 70% of patients are ESR1-positive at diagnosis and are candidates for endocrine therapy. However, ESR1-positive tumours can become resistant to endocrine therapy. Multiple mechanisms of endocrine resistance have been proposed, including suppression of ESR1. This review discusses the relationship between intratumoural inflammation and endocrine resistance with a particular focus on inflammation-mediated suppression of ESR1.

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Antimicrobial skin peptides and proteins

Cited by 226 publications

References 138 publications

Outer Membrane Protein I of Pseudomonas aeruginosa Is a Target of Cationic Antimicrobial Peptide/Protein

Outer Membrane Protein I of Pseudomonas aeruginosa Is a Target of Cationic Antimicrobial Peptide/Protein

Novel Insight Into the Role of Antimicrobial (Host Defense) Peptides/Proteins in Human Skin Diseases

Intratumoural inflammation and endocrine resistance in breast cancer

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