Histone H4 is a major component of the antimicrobial action of human sebocytes.

Antimicrobial peptides, such as cathelicidin and beta defensins, directly kill microbes and have been detected in human sebaceous glands and cell lines. Despite the presence of several such peptides, the apparent abundance of these is insufficient for direct killing of most skin pathogens. In this study, we sought to determine which molecules provide the majority of antimicrobial peptide activity in human sebocytes.

A peptide with a ProGln C terminus in the human saliva peptidome exerts bactericidal activity against Propionibacterium acnes.

Nine proline-rich peptides ending with a proline-glutamine C terminus in a salivary peptidome were sequenced by matrix-assisted laser desorption ionization time of flight time of flight tandem mass spectrometry. A GPPPQGGRPQ peptide binds gram-positive Propionibacterium acnes and considerably inhibits bacterial growth. The peptide exhibiting innate immunity may be applied for treatment of various P.

Topical vaccination: the skin as a unique portal to adaptive immune responses.

Skin is an ideal tissue for vaccine administration, as it is comprised of immunocompetent cells such as keratinocytes and Langerhans cells and elicits both innate and adaptive immune responses. In this paper, we summarize the immune responses induced by topical vaccination of the skin and review the effects of adjuvants on skin vaccination. We also summarize the existing techniques for skin vaccination.

Expression and potential function of cathelicidin antimicrobial peptides in dermatophytosis and tinea versicolor.

Objectives: This study was designed to characterize the role of the human cathelicidin LL-37 in fungal skin infections such as dermatophytosis and tinea versicolor.

Methods: The in vitro antimicrobial activity of synthetic antimicrobial peptides including the human cathelicidin LL-37 against Malassezia furfur and several dermatophytes was determined. Immunostaining was performed to determine expression of cathelicidin in skin biopsies from patients with tinea pedis, tinea corporis and tinea versicolor.

The mammalian ionic environment dictates microbial susceptibility to antimicrobial defense peptides.

Antimicrobial peptides (AMPs) have been shown in animal and human systems to be effective natural antibiotics. However, it is unclear how they convey protection; they often appear inactive when assayed under culture conditions applied to synthetic antibiotics. This inactivation has been associated with loss of function in physiological concentrations of NaCl or serum.

Anti-fungal activity of cathelicidins and their potential role in Candida albicans skin infection.

Cathelicidins have broad anti-microbial capacity and are important for host defense against skin infections by some bacterial and viral pathogens. This study investigated the activity of cathelicidins against Candida albicans. The human cathelicidin LL-37, and mouse cathelicidin mCRAMP, killed C.

Biology and clinical relevance of naturally occurring antimicrobial peptides.

Within the last decade, several peptides have been discovered on the basis of their ability to inhibit the growth of potential microbial pathogens. These so-called antimicrobial peptides participate in the innate immune response by providing a rapid first-line defense against infection. Recent advances in this field have shown that peptides belonging to the cathelicidin and defensin gene families are of particular importance to the mammalian immune defense system.

Cathelicidin anti-microbial peptide expression in sweat, an innate defense system for the skin.

The eccrine gland is one of the major cutaneous appendages and secretes sweat. Its principal function is thermoregulation during exposure to a hot environment or physical exercise. In addition to this function, we show that LL-37, a member of cathelicidin family of anti-microbial peptides, is expressed in sweat.

Dermatan sulfate: new functions from an old glycosaminoglycan.

Glycosaminoglycans constitute a considerable fraction of the glycoconjugates found on cellular membranes and in the extracellular matrix of virtually all mammalian tissues. Their ability to bind and alter protein-protein interactions or enzymatic activity has identified them as important determinants of cellular responsiveness in development, homeostasis, and disease. Although heparan sulfate tends to be emphasized as the most biologically active glycosaminoglycan, dermatan sulfate is a particularly attractive subject for further study because it is expressed in many mammalian tissues and it is the predominant glycan present in skin.

Cutaneous injury induces the release of cathelicidin anti-microbial peptides active against group A Streptococcus.

Cathelicidins are a family of peptides thought to provide an innate defensive barrier against a variety of potential microbial pathogens. The human and mouse cathelicidins (LL-37 and CRAMP, respectively) are expressed at select epithelial interfaces where they have been proposed to kill a number of gram-negative and gram-positive bacteria. To determine if these peptides play a part in the protection of skin against wound infections, the anti-microbial activity of LL-37 and CRAMP was determined against the common wound pathogen group A Streptococcus, and their expression was examined after cutaneous injury.