PMID- 11570872
OWN - NLM
STAT- MEDLINE
DCOM- 20011025
LR  - 20190613
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 40
IP  - 39
DP  - 2001 Oct 2
TI  - Gene cloning of a new plasma CC chemokine, activating and attracting myeloid 
      cells in synergy with other chemoattractants.
PG  - 11715-22
AB  - Chemokines are important mediators of cell migration during inflammation and 
      normal leukocyte trafficking. Inflammatory chemokines are induced in multiple 
      cell types at sites of infection. Here, we describe a novel bovine CC chemokine, 
      designated regakine-1, that is constitutively present at high concentrations in 
      plasma. Cloning of its gene revealed an expected two intron/three exon 
      organization, with a rather long first intron. In addition to a 21-residue signal 
      peptide, the coding sequence corresponded to a 71-residue secreted protein. 
      However, the natural regakine-1 protein missed the COOH-terminal lysine residue. 
      Regakine-1 has only weak sequence similarity (<50% identical residues) with other 
      animal or human chemokines. Northern blot analysis demonstrated regakine-1 RNA 
      expression in spleen and lung. At physiological concentrations (30-100 ng/mL), 
      natural 7.5 kDa regakine-1 stimulated gelatinase B release from neutrophils and 
      chemoattracted immature myeloid HL-60 cells, as well as mature granulocytes. 
      Regakine-1 was more potent on human myeloid cells than the human plasma CC 
      chemokine hemofiltrate CC chemokine-1 (HCC-1). Moreover, regakine-1 synergized 
      with the bacterial peptide N-formylmethionylleucylphenylalanine (fMLP), yielding 
      a 10-fold increase in neutrophil chemotactic response above their additive 
      effect. Regakine-1 did not compete with interleukin-8 (IL-8) for binding to 
      neutrophils, nor did it affect fMLP-induced calcium signaling, suggesting that 
      regakine-1 recognizes a different receptor. In view of its high constitutive 
      plasma concentration, regakine-1 is believed to recruit myeloid cells into the 
      circulation, whereas its synergy with other neutrophil chemoattractants suggests 
      that it also enhances the inflammatory response to infection.
FAU - Struyf, S
AU  - Struyf S
AD  - Laboratory of Molecular Immunology, Rega Institute for Medical Research, 
      University of Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium.
FAU - Stoops, G
AU  - Stoops G
FAU - Van Coillie, E
AU  - Van Coillie E
FAU - Gouwy, M
AU  - Gouwy M
FAU - Schutyser, E
AU  - Schutyser E
FAU - Lenaerts, J P
AU  - Lenaerts JP
FAU - Fiten, P
AU  - Fiten P
FAU - Van Aelst, I
AU  - Van Aelst I
FAU - Proost, P
AU  - Proost P
FAU - Opdenakker, G
AU  - Opdenakker G
FAU - Van Damme, J
AU  - Van Damme J
LA  - eng
SI  - GENBANK/AJ313203
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Chemokines, CC)
RN  - 0 (DNA, Complementary)
RN  - 0 (regakine 1)
RN  - 59880-97-6 (N-Formylmethionine Leucyl-Phenylalanine)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Blotting, Northern
MH  - Cattle
MH  - Cell Line
MH  - Chemokines, CC/blood/chemistry/*genetics
MH  - Chemotaxis, Leukocyte
MH  - Cloning, Molecular
MH  - DNA, Complementary
MH  - Humans
MH  - Molecular Sequence Data
MH  - N-Formylmethionine Leucyl-Phenylalanine/metabolism
EDAT- 2001/09/26 10:00
MHDA- 2001/10/26 10:01
CRDT- 2001/09/26 10:00
PHST- 2001/09/26 10:00 [pubmed]
PHST- 2001/10/26 10:01 [medline]
PHST- 2001/09/26 10:00 [entrez]
AID - bi010224+ [pii]
AID - 10.1021/bi010224+ [doi]
PST - ppublish
SO  - Biochemistry. 2001 Oct 2;40(39):11715-22. doi: 10.1021/bi010224+.