Mouse and human CD14 (myeloid cell-specific leucine-rich glycoprotein) primary structure deduced from cDNA clones

Setoguchi, Mihoko; Nasu, Nobuyoshi; Yoshida, Seiji; Higuchi, Yasunori; Akizuki, Shin’ichiro; Yamamoto, Shunsuke

doi:10.1016/0167-4781(80)90012-3

Cited by 83 publications

(59 citation statements)

References 30 publications

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“…CD14 is a surface protein, which is expressed in monocytes/macrophages (41,42), being often used, in the literature, as a stem cell marker (11). This protein is one of the useful markers used to identify mouse mammary progenitor cells (43).…”

Section: Discussionmentioning

confidence: 99%

Differential expression of CD90 and CD14 stem cell markers in malignant breast cancer cell lines

et al. 2012

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The recently emerged concept of cancer stem cell (CSC) has led to a new hypothesis on the basis for tumor progression. Basically, the CSC theory hypothesizes the presence of a hierarchically organized and relatively rare cell population, which is responsible for tumor initiation, self-renewal, and maintenance, in addition to accumulation of mutation and resistance to chemotherapy. CSCs have recently been described in breast cancer. Different genetic markers have been used to isolate breast CSCs, none of which have been correlated with the tumorigenicity or metastatic potential of the cells, limiting their precise characterization and clinical application in the development of therapeutic protocols. Here, we sought for subpopulations of CSCs by analyzing 10 judiciously chosen stem cell markers in a normal breast cell line (MCF10-A) and in four human breast cancer cell lines (MCF-7, MDA-MB-231, MDA-MB-435, and Hs578-T) displaying different degrees of metastatic and invasiveness potential. We were able to identify two markers, which are differentially expressed in nontumorigenic versus tumor cells. The CD90 marker was highly expressed in the malignant cell lines. Interestingly, the CD14 molecule displayed higher expression levels in the nontumorigenic cell line. Therefore, we demonstrated that these two markers, which are more commonly used to isolate and characterize stem cells, are differentially expressed in breast tumor cells, when compared with nontumorigenic breast cells. ' 2012 International Society for Advancement of Cytometry Key terms CD90; Thy-1; breast cancer; cancer stem cell; CD14; breast cancer stem cell

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Section: Discussionmentioning

confidence: 99%

Differential expression of CD90 and CD14 stem cell markers in malignant breast cancer cell lines

et al. 2012

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“…Expression of human and murine CD14 mRNAs in HT29, T84, and CMT93 cells, respectively, were also assessed by RT-PCR (36). PCR primers used for human CD14 were 5Ј-GGT GCC GCT GTG TAG GAA AGA and 5Ј-GGT CCT CGA GCG TCA GTT CCT (450 bp).…”

Section: Assessment Of Lps Receptor Mrna Expression: Rt-pcr Analysismentioning

confidence: 99%

Lipopolysaccharide Activates Distinct Signaling Pathways in Intestinal Epithelial Cell Lines Expressing Toll-Like Receptors

Cario

Rosenberg

Brandwein

et al. 2000

The Journal of Immunology

680

464

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LPS elicits several immediate proinflammatoy responses in peripheral blood leukocytes via a recently described pathway including CD14, Toll-like receptors (TLR), serine-threonine kinases, and NF-κB transcription factor. However, the functional responses of intestinal epithelial cells (IEC) to stimulation with LPS are unknown. Expression of mRNA and protein for CD14 and TLRs were assessed by RT-PCR, immunoblotting, and immunohistochemistry in mouse and human IEC lines. LPS-induced activation of signaling pathways (p42/p44 mitogen-activated protein kinase (MAPK), c-Jun NH2-terminal kinase (JNK), p38, p65, NF-κB) were assessed by immunoblotting and gel shifts. CD14 mRNA and protein expression were not detectable in IEC. However, human TLR2, TLR3, and TLR4 mRNA were present in IEC. TLR4 protein was expressed in all cell lines; however, TLR2 protein was absent in HT29 cells. Immunofluorescent staining of T84 cells demonstrated the cell-surface presence of the TLRs. LPS-stimulation of IEC resulted in activation (>1.5-fold) of the three members of the MAPK family. In contrast, LPS did not significantly induce activation of JNK and p38 in CMT93 cells, p38 in T84 cells and MAPK and JNK in HT29 cells. Downstream, LPS activated NF-κB in IEC in a time-, dose-, and serum-dependent manner. IEC express TLRs that appear to mediate LPS stimulation of specific intracellular signal transduction pathways in IEC. Thus, IEC may play a frontline role in monitoring lumenal bacteria.

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“…In higher concentrations sCD14 blocks the binding of LPS to monocytes and inhibits the LPS-induced oxidative burst of human mononuclear cell preparations [16, 171. The mature human CD14 sequence deduced from cDNA contains 356 amino acid residues [18,191. CD14 has four potential N-linked glycosylation sites (Asnl8, Asnl32, Asn263 and Asn304) which are conserved in mice and rabbits [20,211. The carbohydrate content accounts for about 20% of the total molecular mass of the mature glycoprotein [22].…”

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confidence: 99%

The Myeloid Differentiation Antigen CD14 is N‐ and O‐Glycosylated

Stelter¹,

Pfister²,

Bernheiden³

et al. 1996

European Journal of Biochemistry

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The myeloid differentiation antigen CD14 acts as the major receptor for bacterial lipopolysaccharide (LPS). A soluble form of the protein (sCD14) is present in human serum which functions as a soluble LPS receptor. We have compared the isoform patterns of soluble CD14 derived from human serum and of the recombinant proteins produced by CHO cells transfected with either the wild-type CD14 gene or with a cDNA coding for a truncated protein which lacks the C-terminal 21 amino acids [sCD14-(1-335)-peptide]. Using SDSRAGE, two dominant isoforms (53 and 50 kDa) and two minor forms (46 and 43 kDa) can be detected in serum as well as in the supernatants of both transfectants. sCD14 is a glycoprotein which carries N-and 0-linked carbohydrates. The different isoforms of sCD14-(1-335)-peptide are due to differences in the content of N-linked sugars. However after the removal of N-and 0-linked carbohydrates from serum-and CHO-derived wild-type proteins, two isoforms are still present. These results indicate that N-linked glycosylation contributes to but does not fully explain the different forms of soluble CD14. We further examined whether the mutation of individual N-linked glycosylation sites influences the expression of membrane-bound and soluble CD14 forms and the ability of the membranebound molecule to bind LPS. As with the wild-type proteins, the different isoforms of the soluble mutants are partially due to differences in N-linked glycosylation. A truncated mutant which lacks the two Nterminal glycosylation sites { [Asplg, Asp132]CD14-(1-335)peptide) does not give rise to multiple forms on SDS gels. Like CD14-(I -335)-peptide, this mutant is not expressed on the cell surface suggesting that a smaller isoform present in the wild-type preparations results from proteolytic cleavage of the membrane-bound molecule. N-linked carbohydrates do not seem to be important for the binding of LPS to membrane-bound CD14.

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Mouse and human CD14 (myeloid cell-specific leucine-rich glycoprotein) primary structure deduced from cDNA clones

Cited by 83 publications

References 30 publications

Differential expression of CD90 and CD14 stem cell markers in malignant breast cancer cell lines

Differential expression of CD90 and CD14 stem cell markers in malignant breast cancer cell lines

Lipopolysaccharide Activates Distinct Signaling Pathways in Intestinal Epithelial Cell Lines Expressing Toll-Like Receptors

The Myeloid Differentiation Antigen CD14 is N‐ and O‐Glycosylated

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