Growth and characterization of human monocytes (macrophages)

We have defined the cell surface molecules of human monocytes and PMN that bind to the chymotryptic cell binding domain of Fn and to a synthetic peptide, KYAVTGRGDS, based on the sequence of Fn, by affinity chromatography. Monocytes express two receptors that differ in their affinity for CBD-Sepharose and peptide-Sepharose, but that both recognize the RGD sequence. Only a single receptor is purified from PMN, which resembles the monocyte surface molecule that binds to peptide-Sepharose. These receptors are not part of the Mac-1, LFA-1, p(150,95) family, but do have homology to the platelet Fn receptor, gpIIb/IIIa. Interestingly, the antigenic crossreactivity between gpIIb/IIIa and the phagocyte receptors purified on peptide-Sepharose is largely in the beta chain of the receptors. The alpha chains appear to be distinct, based on molecular weight, antigenic analysis, and ligand specificity. This receptor also seems to be the surface molecule on monocytes that is critical for phagocytosis enhancement by Fn. Thus, we have defined the phagocyte Fn receptor that transduces the signal for increased phagocytosis by monocytes; it may be a third member of a family of adhesion molecules that includes the gpIIb/IIIa of platelets and the vitronectin receptor of fibroblasts.

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Biochemical and morphological characterization of the killing of human monocytes by a leukotoxin derived from Actinobacillus actinomycetemcomitans.

Infection and Immunity ◽

10.1128/iai.28.1.258-268.1980 ◽

1980 ◽

Vol 28 (1) ◽

pp. 258-268 ◽

Cited By ~ 132

Author(s):

N S Taichman ◽

R T Dean ◽

C J Sanderson

Keyword(s):

Morphological Characterization ◽

Actinobacillus Actinomycetemcomitans ◽

Human Monocytes

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Characterization of a Novel CC Chemokine, HCC-4, Whose Expression Is Increased by Interleukin-10

Blood ◽

10.1182/blood.v91.11.4242.411k18_4242_4247 ◽

1998 ◽

Vol 91 (11) ◽

pp. 4242-4247 ◽

Cited By ~ 1

Author(s):

Joseph A. Hedrick ◽

Allison Helms ◽

Alain Vicari ◽

Albert Zlotnik

Keyword(s):

Interleukin 10 ◽

Chemotactic Activity ◽

Prior Exposure ◽

Northern Analysis ◽

Human Monocytes ◽

Cc Chemokine ◽

Activated Monocytes ◽

Resting Lymphocytes

We have identified and characterized a human β (CC) chemokine, designated HCC-4, that is most closely related to HCC-1 and which demonstrates chemotactic activity for monocytes. Northern analysis of multiple tissue blots and of activated monocytes mRNA shows expression of a 500-bp mRNA. A 1,500-bp mRNA was highly expressed in monocytes activated 12 hours in the presence of interleukin-10 (IL-10) but was absent in monocytes activated for only 1 hour regardless of the presence or absence of IL-10. The upregulation of expression in the presence of IL-10 is in contrast to the downregulatory effects of IL-10 on expression of most other chemokines. Recombinant HCC-4 demonstrated chemotactic activity for human monocytes and THP-1 monocyte cells but not for resting lymphocytes or neutrophils. HCC-4 also induced a Ca2+ flux in THP-1 cells that was desensitized by prior exposure to RANTES. Taken together, these data indicate that HCC-4 is a novel chemokine whose expression is uniquely upregulated by IL-10.

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