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Murine monocyte chemoattractant protein (MCP)-5: a novel CC chemokine that is a structural and functional homologue of human MCP-1.

Sarafi MN, Garcia-Zepeda EA, MacLean JA, Charo IF, Luster AD - J. Exp. Med. (1997)

Bottom Line: Consistent with these results, MCP-5 induced a calcium flux in human embryonic kidney (HEK)-293 cells transfected with human and murine CCR2, a CC chemokine receptor expressed on monocytes.MCP-5 did not induce a calcium flux in HEK-293 cells transfected with CCR1, CCR3, or CCR5.These data indicate that MCP-5 is a novel and potent monocyte active chemokine that is involved in allergic inflammation and the host response to pathogens.

View Article: PubMed Central - PubMed

Affiliation: Infectious Disease Unit, Massachusetts General Hospital, Boston, USA.

ABSTRACT
The chemokines are a large family of cytokines that control the recruitment of leukocytes in immune and inflammatory responses. We describe the isolation of a novel murine CC chemokine that, based on its biological and structural features, we have named monocyte chemoattractant protein (MCP)-5. MCP-5 mapped to the CC chemokine cluster on mouse chromosome 11 and was most closely related to human MCP-1 in structure (66% amino acid identity). Purified recombinant MCP-5 protein was a potent chemoattractant for peripheral blood monocytes, was only weakly active on eosinophils at high doses, and was inactive on neutrophils. MCP-5 induced a calcium flux in peripheral blood mononuclear cells, but not in purified murine eosinophils or neutrophils. Consistent with these results, MCP-5 induced a calcium flux in human embryonic kidney (HEK)-293 cells transfected with human and murine CCR2, a CC chemokine receptor expressed on monocytes. MCP-5 did not induce a calcium flux in HEK-293 cells transfected with CCR1, CCR3, or CCR5. Constitutive expression of MCP-5 mRNA was detected predominantly in lymph nodes, and its expression was markedly induced in macrophages activated in vitro and in vivo. Moreover, MCP-5 expression was up-regulated in the lungs of mice following aerosolized antigen challenge of sensitized mice, and during the host response to infection with Nippostrongylus brasiliensis. These data indicate that MCP-5 is a novel and potent monocyte active chemokine that is involved in allergic inflammation and the host response to pathogens.

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Expression of MCP-5 in normal mouse organs. Northern  analysis of 10 μg total RNA isolated from various tissues of a normal  BALB/c mouse. Salivary gland and breast tissue contained lymph nodes.  The blot was hybridized sequentially with MCP-5, JE, and rpL32 cDNA  probes and exposed for 29 d, 21 d, and 18 h, respectively. The positions  of 18s and 28s RNA are indicated on the left.
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Figure 6: Expression of MCP-5 in normal mouse organs. Northern analysis of 10 μg total RNA isolated from various tissues of a normal BALB/c mouse. Salivary gland and breast tissue contained lymph nodes. The blot was hybridized sequentially with MCP-5, JE, and rpL32 cDNA probes and exposed for 29 d, 21 d, and 18 h, respectively. The positions of 18s and 28s RNA are indicated on the left.

Mentions: To investigate the expression of murine MCP-5 in normal murine tissues, a Northern analysis of mRNA obtained from mouse organs was performed (Fig. 6). This analysis revealed an ∼550-bp transcript that corresponds to the mature mouse MCP-5 mRNA. The highest levels of constitutive MCP-5 expression were observed in normal lymph nodes. MCP-5 mRNA levels were also seen in breast and salivary glands containing lymph nodes, heart, lung, thymus, brain, small intestines, kidney, and colon. However, no expression was detected in spleen, skeletal muscle, bone marrow, or liver. The expression of MCP-5 and JE were compared in these mouse tissues since MCP-5 had a similar biological profile to JE and signaled through the same receptor. Highest constitutive expression of JE was seen in the salivary gland with low levels detected in other organs (e.g., lymph nodes) (Fig. 6). The ∼550- and 800-bp JE transcripts correspond to known 3′ splice variants (4).


Murine monocyte chemoattractant protein (MCP)-5: a novel CC chemokine that is a structural and functional homologue of human MCP-1.

Sarafi MN, Garcia-Zepeda EA, MacLean JA, Charo IF, Luster AD - J. Exp. Med. (1997)

Expression of MCP-5 in normal mouse organs. Northern  analysis of 10 μg total RNA isolated from various tissues of a normal  BALB/c mouse. Salivary gland and breast tissue contained lymph nodes.  The blot was hybridized sequentially with MCP-5, JE, and rpL32 cDNA  probes and exposed for 29 d, 21 d, and 18 h, respectively. The positions  of 18s and 28s RNA are indicated on the left.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2196097&req=5

Figure 6: Expression of MCP-5 in normal mouse organs. Northern analysis of 10 μg total RNA isolated from various tissues of a normal BALB/c mouse. Salivary gland and breast tissue contained lymph nodes. The blot was hybridized sequentially with MCP-5, JE, and rpL32 cDNA probes and exposed for 29 d, 21 d, and 18 h, respectively. The positions of 18s and 28s RNA are indicated on the left.
Mentions: To investigate the expression of murine MCP-5 in normal murine tissues, a Northern analysis of mRNA obtained from mouse organs was performed (Fig. 6). This analysis revealed an ∼550-bp transcript that corresponds to the mature mouse MCP-5 mRNA. The highest levels of constitutive MCP-5 expression were observed in normal lymph nodes. MCP-5 mRNA levels were also seen in breast and salivary glands containing lymph nodes, heart, lung, thymus, brain, small intestines, kidney, and colon. However, no expression was detected in spleen, skeletal muscle, bone marrow, or liver. The expression of MCP-5 and JE were compared in these mouse tissues since MCP-5 had a similar biological profile to JE and signaled through the same receptor. Highest constitutive expression of JE was seen in the salivary gland with low levels detected in other organs (e.g., lymph nodes) (Fig. 6). The ∼550- and 800-bp JE transcripts correspond to known 3′ splice variants (4).

Bottom Line: Consistent with these results, MCP-5 induced a calcium flux in human embryonic kidney (HEK)-293 cells transfected with human and murine CCR2, a CC chemokine receptor expressed on monocytes.MCP-5 did not induce a calcium flux in HEK-293 cells transfected with CCR1, CCR3, or CCR5.These data indicate that MCP-5 is a novel and potent monocyte active chemokine that is involved in allergic inflammation and the host response to pathogens.

View Article: PubMed Central - PubMed

Affiliation: Infectious Disease Unit, Massachusetts General Hospital, Boston, USA.

ABSTRACT
The chemokines are a large family of cytokines that control the recruitment of leukocytes in immune and inflammatory responses. We describe the isolation of a novel murine CC chemokine that, based on its biological and structural features, we have named monocyte chemoattractant protein (MCP)-5. MCP-5 mapped to the CC chemokine cluster on mouse chromosome 11 and was most closely related to human MCP-1 in structure (66% amino acid identity). Purified recombinant MCP-5 protein was a potent chemoattractant for peripheral blood monocytes, was only weakly active on eosinophils at high doses, and was inactive on neutrophils. MCP-5 induced a calcium flux in peripheral blood mononuclear cells, but not in purified murine eosinophils or neutrophils. Consistent with these results, MCP-5 induced a calcium flux in human embryonic kidney (HEK)-293 cells transfected with human and murine CCR2, a CC chemokine receptor expressed on monocytes. MCP-5 did not induce a calcium flux in HEK-293 cells transfected with CCR1, CCR3, or CCR5. Constitutive expression of MCP-5 mRNA was detected predominantly in lymph nodes, and its expression was markedly induced in macrophages activated in vitro and in vivo. Moreover, MCP-5 expression was up-regulated in the lungs of mice following aerosolized antigen challenge of sensitized mice, and during the host response to infection with Nippostrongylus brasiliensis. These data indicate that MCP-5 is a novel and potent monocyte active chemokine that is involved in allergic inflammation and the host response to pathogens.

Show MeSH
Related in: MedlinePlus