TY - JOUR
T1 - Isolation of ALP, a novel divergent murine CC chemokine with a unique carboxy terminal extension
AU - Hromas, Robert
AU - Broxmeyer, Hal E.
AU - Kim, Chang
AU - Christopherson, Kent
AU - Hou, Yong Hao
N1 - Funding Information:
H.B. is supported by NIH RO1 CHL56416 and DK53674. R.H. is supported by NIH RO1 48914 and the Leukemia Society of America.
PY - 1999/5/19
Y1 - 1999/5/19
N2 - Chemokines are a family of related proteins that regulate leukocyte infiltration into inflamed tissue and play important roles in many disease processes. Chemokines are divided into two major groups, CC or CXC, based on their sequence around the amino terminal cysteines. We report here, the isolation of a novel murine CC chemokine termed ALP for its amino terminal peptide sequence. This novel chemokine is distantly related to other CC chemokines (37% identity with murine Exodus-1/LARC/Mip-3α), but has a unique carboxy terminal extension. It is expressed preferentially in testis, heart, and liver, which is atypical for CC chemokines.
AB - Chemokines are a family of related proteins that regulate leukocyte infiltration into inflamed tissue and play important roles in many disease processes. Chemokines are divided into two major groups, CC or CXC, based on their sequence around the amino terminal cysteines. We report here, the isolation of a novel murine CC chemokine termed ALP for its amino terminal peptide sequence. This novel chemokine is distantly related to other CC chemokines (37% identity with murine Exodus-1/LARC/Mip-3α), but has a unique carboxy terminal extension. It is expressed preferentially in testis, heart, and liver, which is atypical for CC chemokines.
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U2 - 10.1006/bbrc.1999.0507
DO - 10.1006/bbrc.1999.0507
M3 - Article
C2 - 10329455
AN - SCOPUS:0033583808
SN - 0006-291X
VL - 258
SP - 737
EP - 740
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -