Murine peptidoglycan recognition proteins PglyrpIalpha and PglyrpIbeta are encoded in the epidermal differentiation complex and are expressed in epidermal and hematopoietic tissues.
Peptidoglycan recognition proteins (PGRPs or PGLYRPs) are pattern recognition molecules that are found in insects and mammals and are critical for innate immune responses. PGRPs bind peptidoglycan, a ubiquitous component of bacterial cell walls, and are involved in killing bacteria, degrading peptidoglycan, and initiating host defense reactions. Relatively little is known about the four mammalian PGRPs. In this article, we report the sequences of mouse PglyrpIalpha and PglyrpIbeta and provide details of their expression in wild-type mouse tissues. PglyrpIalpha and PglyrpIbeta are encoded within the epidermal differentiation complex on mouse chromosome 3F. Both genes are expressed in epidermal and hematopoietic tissues. PglyrpIbeta is expressed in each of 16 tissues tested, while PglyrpIalpha expression is limited to fewer tissues, including the lung and spleen as well as several tissues of the digestive system. Both proteins are expressed in epithelial cells throughout the gut, and immunohistochemical staining shows expression in salivary glands, the squamous epithelium of the stomach, and the villi of the jejunum. Immunohistochemical staining further shows expression of both PglyrpIalpha and PglyrpIbeta in macrophages in the spleen. PglyrpIalpha is not expressed in resting RAW264.7 macrophage-like cells, but is induced by stimulation with lipopolysaccharide. PglyrpIbeta is constitutively expressed in RAW264.7 cells and is unaffected by lipopolysaccharide or peptidoglycan stimulation. Computational and experimental data suggest that these proteins are secreted. This work provides a step toward understanding the roles of PglyrpIalpha and PglyrpIbeta in host defense and chronic inflammatory conditions induced by bacteria or their components.
Mathur
Punam
P
Department of Discovery Biology, Biogen Idec, Inc., 14 Cambridge Center, Cambridge, MA 02142, USA. john_carulli@biogen.idec.com
Murray
Beth
B
Crowell
Thomas
T
Gardner
Humphrey
H
Allaire
Normand
N
Hsu
Yen-Ming
YM
Thill
Greg
G
Carulli
John P
JP
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002352:Carrier Proteins / Q000032:analysis / Q000235:genetics* / Q000378:metabolism*; D002432:Cecum / Q000648:ultrastructure; D002460:Cell Line; D003001:Cloning, Molecular; D016207:Cytokines / Q000235:genetics* / Q000378:metabolism; D004817:Epidermis / Q000254:growth & development / Q000378:metabolism*; D004847:Epithelial Cells / Q000378:metabolism; D004943:Esophagogastric Junction / Q000648:ultrastructure; D015870:Gene Expression; D005786:Gene Expression Regulation; D006413:Hematopoietic System / Q000378:metabolism*; D008070:Lipopolysaccharides / Q000494:pharmacology; D051379:Mice; D008969:Molecular Sequence Data; D010457:Peptidoglycan / Q000378:metabolism / Q000494:pharmacology; D012333:RNA, Messenger / Q000032:analysis; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013154:Spleen / Q000648:ultrastructure; D014162:Transfection
D002352:Carrier Proteins; D016207:Cytokines; D008070:Lipopolysaccharides; D010457:Peptidoglycan; C113582:Pglyrp1 protein, mouse; D012333:RNA, Messenger; C118897:peptidoglycan recognition protein