Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Keywords: EXPRESSION ; IN-VITRO ; DISTINCT ; DIFFERENTIATION ; MESSENGER-RNA ; murine ; KERATINOCYTES ; EPIDERMAL DIFFERENTIATION ; ARACHIDONIC-ACID ; calcium gradient ; ENHANCING FACTOR ; epidermal barrier ; GROUP-II ; GROUP-V ; GROUP-X ; hyperproliferation ; INVITRO CULTIVATION ; LOW-MOLECULAR-WEIGHT ; neonatal mouse ; NEONATAL MOUSE KERATINOCYTES ; PERMEABILITY BARRIER HOMEOSTASIS ; epidermis
    Abstract: The action of secreted phospholipases A(2) in skin is thought to be essential for epidermal barrier homeostasis. The incomplete knowledge of presence and functions of the novel secreted phospholipase A(2) subtypes in skin prompted us to explore their expression in epidermis and primary keratinocytes from murine neonatal skin. We detected secreted phospholipases A(2) -IB, -IIA, -IIC, -IID, -IIE, -IIF, -V, -X, and -XII. To study secreted phospholipase A(2) expression during epidermal differentiation, primary keratinocytes from the basal, suprabasal, and upper differentiated layers of neonatal mouse epidermis were obtained by density gradient centrifugation. mRNA for secreted phospholipases A(2) -IB, -IIE, -IIF, -V, and -XII-1 are mainly expressed in the upper differentiated layers, whereas the most prominent enzymes in the basal and suprabasal layers are secreted phospholipases A(2) -IIA, -IID, and -X. The mRNA for secreted phospholipase A(2) -IIC was found in all fractions. Immunohistochemical analysis in mouse skin sections reflected the mRNA distribution patterns in the different epidermal cell fractions. After in vitro induction of keratinocyte differentiation by increasing the calcium concentration of the medium, secreted phospholipases A(2) -IB, -IIE, -IIF, -V, and -XII-1 were upregulated, whereas secreted phospholipases A(2) -IIA, -IIC, -IID, and -X were mainly expressed in proliferating keratinocytes. The specific secreted phospholipase A(2) expression profile in the skin suggests a distinct function for each enzyme in the epidermis
    Type of Publication: Journal article published
    PubMed ID: 12839576
    Signatur Availability
    BibTip Others were also interested in ...
  • 2
    Keywords: CELLS ; EXPRESSION ; tumor ; Germany ; ENZYMES ; PROTEIN ; DIFFERENTIATION ; RELEASE ; PATIENT ; KERATINOCYTES ; SKIN ; antibodies ; antibody ; MAMMALIAN-CELLS ; HUMAN KERATINOCYTES ; HEALTHY ; ARACHIDONIC-ACID ; calcium gradient ; epidermal barrier ; GROUP-V ; GROUP-X ; epidermis ; LOCATION ; HUMAN EPIDERMIS ; inflammation ; HUMAN SKIN ; PSORIASIS ; keratinocyte ; regulation ; SUBTYPE ; SUBTYPES ; VITAMIN-C ; COMPLETE SET ; GROUP IB ; GROUP-IIA
    Abstract: Secreted phospholipases A(2) (sPLA(2)) expressed in the skin are thought to be involved in epidermal barrier homeostasis as well as in inflammation. We investigated the expression of the novel sPLA(2) subtypes in human skin at mRNA and protein levels in the epidermis and primary keratinocytes from healthy human skin, and in skin sections from patients with psoriasis, where the integrity of the epidermis is drastically affected. Immunofluorescence studies using specific antibodies for the different sPLA(2) enzymes show that sPLA(2)-IB, -IIF, and -X are predominantly expressed in suprabasal layers, whereas sPLA(2)-V and -IID are detected in the basal and spinous layers. sPLA(2)-IIA is weakly expressed, and sPLA(2)-IIE and XIIA are not detectable. Accordingly, in differentiated human primary keratinocyte cultures, the expression of sPLA(2)-IB, -IIF and -X was increased, whereas that of sPLA(2)-V and -IID was markedly decreased. In psoriatic skin, sPLA(2)-X was dramatically downregulated in the epidermis, whereas increased amounts of this enzyme together with sPLA(2)-IIA, -IID, and -IB appeared in the dermis. An enhanced release of these enzymes with the exception of sPLA(2)-IID was also observed after treatment of HaCaT keratinocytes with tumor necrosis factor-alpha/interferon-gamma. Treatment of HaCaT cells with sPLA(2)-X and -IB resulted in an increase in prostaglandin E-2 formation, suggesting a proinflammatory role of these enzymes during psoriasis. sPLA(2)-V completely disappeared. The differential locations of the sPLA(2) enzymes propose distinct roles of individual enzymes in skin
    Type of Publication: Journal article published
    PubMed ID: 15654975
    Signatur Availability
    BibTip Others were also interested in ...
  • 3
    ISSN: 0014-5793
    Keywords: Myotoxin ; Neurotoxin ; Phospholipase A"2 ; Skeletal muscle ; Snake venom
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 4
    Publication Date: 2018-07-24
    Description: Human innate immunity employs cellular and humoral mechanisms to facilitate rapid killing of invading bacteria. The direct killing of bacteria by human serum is attributed mainly to the activity of the complement system, which forms pores in Gram-negative bacteria. Although Gram-positive bacteria are considered resistant to killing by serum, we uncover here that normal human serum effectively kills Enterococcus faecium . Comparison of a well-characterized collection of commensal and clinical E. faecium isolates revealed that human serum specifically kills commensal E. faecium strains isolated from normal gut microbiota but not clinical isolates. Inhibitor studies show that the human group IIA secreted phospholipase A2 (hGIIA), but not complement, is responsible for killing of commensal E. faecium strains in human normal serum. This is remarkable since the hGIIA concentration in "noninflamed" serum was considered too low to be bactericidal against Gram-positive bacteria. Mechanistic studies showed that serum hGIIA specifically causes permeabilization of commensal E. faecium membranes. Altogether, we find that a normal concentration of hGIIA in serum effectively kills commensal E. faecium and that resistance of clinical E. faecium to hGIIA could have contributed to the ability of these strains to become opportunistic pathogens in hospitalized patients.
    Print ISSN: 0019-9567
    Electronic ISSN: 1098-5522
    Topics: Medicine
    Signatur Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...