PMID- 7504015
OWN - NLM
STAT- MEDLINE
DCOM- 19940106
LR  - 20071115
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 151
IP  - 11
DP  - 1993 Dec 1
TI  - cDNA cloning and expression of guinea pig neutrophil attractant protein-1 
      (NAP-1). NAP-1 is highly conserved in guinea pig.
PG  - 6225-36
AB  - cDNA for neutrophil attractant protein-1 (NAP-1, also known as IL-8) was cloned 
      from Con A-stimulated guinea pig spleen cells with human NAP-1 cDNA as a probe. 
      Guinea pig NAP-1 cDNA is composed of 1433 bp with an open reading frame which 
      encodes for a 101-amino-acid protein. Guinea pig NAP-1 had 70% amino acid 
      sequence similarity to human NAP-1, which was much higher than a similarity 
      between human and guinea pig monocyte chemoattractant protein-1 (MCP-1) (56%). 
      Nucleotide sequence similarity within the coding region was 75%. To confirm its 
      biological activity in guinea pig, recombinant guinea pig NAP-1 was expressed in 
      COS-7 cells then purified. N-terminal sequence analysis gave two different 
      N-termini at position 23 (Met) or 24 (Val). The two proteins showed their peak 
      activity for guinea pig neutrophils at the concentration of 1 microgram/ml (10-7 
      M). Despite its high similarity to human NAP-1, the responsiveness of human 
      neutrophils to guinea pig NAP-1 was minimum. Recombinant guinea pig NAP-1 caused 
      strong neutrophil infiltration after intradermal injection into guinea pig skin. 
      Since guinea pig is classified as a rodent, it was of interest to know whether 
      human NAP-1 cDNA hybridizes to genomic DNA of other rodents such as mouse or rat, 
      in which a NAP-1 homologue has not been found. Under low stringency conditions, 
      human NAP-1 cDNA hybridized to human, rabbit, and guinea pig DNA, but not to 
      mouse or rat DNA. Unlike NAP-1, human MCP-1 cDNA hybridized to genomic DNA of 
      rabbit, guinea pig, mouse, and rat; MCP-1 cDNA have been cloned from these 
      species. The apparent absence of a NAP-1 gene in mouse or rat makes this 
      chemoattractant unique among the members of the protein family to which NAP-1 and 
      MCP-1 belong.
FAU - Yoshimura, T
AU  - Yoshimura T
AD  - Immunopathology Section, National Cancer Institute-Frederick Cancer Research and 
      Development Center MD 21702.
FAU - Johnson, D G
AU  - Johnson DG
LA  - eng
SI  - GENBANK/L04986
PT  - Journal Article
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Chemokine CCL2)
RN  - 0 (Chemokine CCL5)
RN  - 0 (Chemotactic Factors)
RN  - 0 (DNA, Complementary)
RN  - 0 (Interleukin-8)
RN  - 0 (Lymphokines)
RN  - 0 (Recombinant Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Cells, Cultured
MH  - Chemokine CCL2
MH  - Chemokine CCL5
MH  - Chemotactic Factors/genetics
MH  - Cloning, Molecular
MH  - Conserved Sequence
MH  - DNA, Complementary/*isolation & purification
MH  - Guinea Pigs
MH  - Humans
MH  - Interleukin-8/chemistry/*genetics/pharmacology
MH  - Lymphokines/genetics
MH  - Molecular Sequence Data
MH  - Neutrophils/drug effects
MH  - Recombinant Proteins/biosynthesis/isolation & purification/pharmacology
EDAT- 1993/12/01 00:00
MHDA- 1993/12/01 00:01
CRDT- 1993/12/01 00:00
PHST- 1993/12/01 00:00 [pubmed]
PHST- 1993/12/01 00:01 [medline]
PHST- 1993/12/01 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1993 Dec 1;151(11):6225-36.