PMID- 10540231
OWN - NLM
STAT- MEDLINE
DCOM- 19991130
LR  - 20191210
IS  - 0019-2805 (Print)
IS  - 0019-2805 (Linking)
VI  - 98
IP  - 2
DP  - 1999 Oct
TI  - Structural characterization of mouse CD97 and study of its specific interaction
      with the murine decay-accelerating factor (DAF, CD55).
PG  - 303-11
AB  - CD97 is a newly identified, activation-associated human leucocyte antigen with
      seven putative transmembrane domains. It has an extended extracellular segment
      containing several adhesion molecule structure motifs, and has been shown to
      interact with the human complement regulator, decay-accelerating factor (DAF,
      CD55). To understand further the interaction between CD97 and DAF, as well as the
      structure and function of CD97 in general, we have cloned the mouse CD97 cDNA and
      studied the encoded protein for its membrane association property and ability to 
      interact specifically with the murine decay-accelerating factor. The full-length 
      mouse CD97 cDNA that we have cloned and characterized encodes a protein that is
      60% identical to the three epidermal growth factor (EGF) domain-containing form
      of human CD97 but does not contain the Arg-Gly-Asp (RGD) motif which is present
      in human CD97. Two other alternatively spliced forms of mouse CD97 were also
      identified. These forms differ by the number of EGF-like sequence repeats present
      in the N-terminal region. Northern blot analysis revealed that CD97 is expressed 
      widely in mouse tissues and in resting as well as activated cultured mouse
      splenocytes. Transient transfection of human embryonic kidney (HEK) 293 cells
      with the mouse CD97 cDNA in a green-fluorescence protein vector (pEGFP-N1) showed
      plasma membrane targeting of the expressed protein. Western blot analysis
      confirmed its membrane association and identified the existence of a processed
      C-terminal fragment, supporting the notion that CD97 on the cell membrane is
      composed of post-translationally generated subunits. Adhesion studies
      demonstrated that normal, but not DAF knockout mouse erythrocytes and splenocytes
      adhered to mouse CD97-transfected HEK cells. The interaction of CD97 and DAF was 
      found to be species-restrictive in that human erythrocytes were unable to bind to
      mouse CD97-transfected HEK cells. These results indicate that the general
      structure, membrane association property and DAF-binding ability of CD97 are
      conserved and that the adhesive interaction between CD97 and DAF is independent
      of the RGD motif. The finding that CD97 is distributed widely among various mouse
      tissues suggests that CD97 may have other roles beyond lymphocyte activation.
FAU - Qian, Y M
AU  - Qian YM
AD  - Center for Experimental Therapeutics and Department of Pharmacology, University
      of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.
FAU - Haino, M
AU  - Haino M
FAU - Kelly, K
AU  - Kelly K
FAU - Song, W C
AU  - Song WC
LA  - eng
SI  - GENBANK/AF146344
PT  - Journal Article
PL  - England
TA  - Immunology
JT  - Immunology
JID - 0374672
RN  - 0 (ADGRE5 protein, human)
RN  - 0 (Adgre5 protein, mouse)
RN  - 0 (Antigens, CD)
RN  - 0 (CD55 Antigens)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Receptors, G-Protein-Coupled)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antigens, CD
MH  - Base Sequence
MH  - Blotting, Northern
MH  - Blotting, Western
MH  - CD55 Antigens/*metabolism
MH  - Cell Adhesion/immunology
MH  - Cell Line
MH  - Cell Membrane/immunology
MH  - Cells, Cultured
MH  - Erythrocytes/immunology
MH  - Humans
MH  - Membrane Glycoproteins/*genetics/metabolism
MH  - Mice
MH  - Mice, Knockout
MH  - Molecular Sequence Data
MH  - Receptors, G-Protein-Coupled
MH  - Sequence Alignment
MH  - Species Specificity
MH  - Spleen/*immunology
PMC - PMC2326925
EDAT- 1999/12/14 00:00
MHDA- 1999/12/14 00:01
CRDT- 1999/12/14 00:00
PHST- 1999/12/14 00:00 [pubmed]
PHST- 1999/12/14 00:01 [medline]
PHST- 1999/12/14 00:00 [entrez]
AID - imm859 [pii]
AID - 10.1046/j.1365-2567.1999.00859.x [doi]
PST - ppublish
SO  - Immunology. 1999 Oct;98(2):303-11. doi: 10.1046/j.1365-2567.1999.00859.x.