Journal
JOURNAL OF DENTAL RESEARCH
Volume 82, Issue 12, Pages 944-950Publisher
INT AMER ASSOC DENTAL RESEARCHI A D R/A A D R
DOI: 10.1177/154405910308201202
Keywords
bactericidal/permeability-increasing protein (BPI); endotoxin; host defense; innate immunity; lipid binding protein (LBP); lipopolysaccharide (LPS); palate/lung/nasal epithelium clone (PLUNC); parotid secretory protein (PSP); sepsis; von Ebner minor salivary gland protein (VEMSGP)
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Funding
- NHLBI NIH HHS [R15 HL067220] Funding Source: Medline
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R15HL067220] Funding Source: NIH RePORTER
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An expanding number of innate immune molecules occupy the epithelial frontier. This review introduces a recently recognized class of mammalian proteins with similarity to PLUNC ((p) under bar alate, (l) under bar ung and (n) under bar asal epithelium (c) under bar lone), which is itself related to the host defense protein BPI ((b) under bar actericidal/(p) under bar ermeability-(i) under bar ncreasing protein). Four emerging lines of evidence unite the PLUNC-like proteins: conserved genetic structure, epithelial expression, three-dimensional protein similarity, and a physiological response to injury or inflammation. By analogy to known proteins of the innate immune system, an emerging hypothesis for this family is that they act as sensors of Gram-negative bacteria in the oral cavity, among other areas.
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