Disease relevance of LOC396881

• Purification and binding properties of porcine plasma ficolin that binds Actinobacillus pleuropneumoniae [1].
• Binding of porcine ficolin-alpha to lipopolysaccharides from Gram-negative bacteria and lipoteichoic acids from Gram-positive bacteria [2].

High impact information on LOC396881

• It is possible that a specific posttranslational modification of ficolin or interaction with another component is needed for TGF-beta 1 binding [3].
• On the other hand, ficolin-beta was mainly expressed in skeletal muscle [3].
• The cDNA-derived amino acid sequence of human ficolin has approx. 75% identity with, and a similar domain organization to, the two pig ficolin sequences, which are characterized by the presence of a leader peptide, a short N-terminal segment followed by a collagen-like region and then by a C-terminal fibrinogen-like domain [4].
• From the present findings, purified porcine serum protein reactive with GlcNAc is concluded to be ficolin-alpha playing an important role(s) in innate immunity against microbial infection with Gram-positive and -negative bacteria [2].
• An N-acetylated amine-activated Toyopearl matrix bound ficolin, and ficolin was dissociated from this matrix with acetamide [1].

Chemical compound and disease context of LOC396881

• Previous studies demonstrated that porcine plasma ficolin binds the important pig pathogen Actinobacillus pleuropneumoniae (APP) in an N-acetylglucosamine-dependent manner [1].
• Ficolin alpha in porcine plasma binds Actinobacillus pleuropneumoniae serotype 5 (APP) in a GlcNAc-dependent manner [5].

Anatomical context of LOC396881

• Expression and secretion of ficolin beta by porcine neutrophils [5].

Associations of LOC396881 with chemical compounds

• Mouse plasma ficolin was purified by GlcNAc affinity and anion-exchange chromatography [6].
• Acetate, acetamide, and GlcNAc, but not glucose or glucosamine, dissociated plasma ficolin from the surface of intact APP serotype 5b, which contains N-acetylated saccharides in the capsule [1].

Other interactions of LOC396881

• Neutrophil ficolin was consistent with ficolin beta by pI and peptide mass fingerprinting with matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry [5].

Analytical, diagnostic and therapeutic context of LOC396881

• Molecular cloning and characterization of ficolin, a multimeric protein with fibrinogen- and collagen-like domains [3].
• Analysis by Northern blotting revealed that the expression of ficolin-alpha mRNA is relatively restricted and most abundant in placenta and lung [3].
• Gel-filtration chromatography and gradient sedimentation indicated that mouse plasma ficolin is a 12-mer of approximately 35 kDa subunits, and electron microscopy showed the same parachute-like structure previously characterized for the pig ficolin 12-mer [6].
• Subunit bands separated by 2D-PAGE were consistent with porcine ficolin alpha [7].
• In the present study, we discovered that porcine neutrophils, but not platelets or mononuclear cells, contained a different ficolin that migrated as a 39-kDa band on SDS-PAGE and resembled a minor component of plasma ficolins that binds APP [5].

References