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Cellular Trafficking
Published in Martin Berry, Ann Logan, CNS Injuries: Cellular Responses and Pharmacological Strategies, 2019
This family is often referred to as the leucocyte integrins. There are three main groups: CDlla/CD18 is present on virtually all leucocytes, whereas CD11b/CD18 and CD11c/CD18 are mainly confined to phagocytic cells (see Table 6.1). Anti-CD11a antibodies prevent the increased adhesion of leucocytes to cytokine-treated endothelium, and in experimental models of non-CNS inflammation, antibodies against CD11a, CD11b, or CD18 impede the entry of leucocyte infiltrates.33–35 Regulation of integrin expression and binding efficiency is linked to haemopoietic maturation36 and to the state of cell activation. Associated with the transition from naive to memory T cells is an increase in CD11a expression, and it is the memory T cells that preferentially migrate to inflammatory lesions.37,38
Human Blood Dendritic Cells
Published in Brian J. Nickoloff, Dermal Immune System, 2019
Peter S. Freudenthal, Gary S. Wood
Dendritic cells express neither CD2 (the LFA-3 ligand) nor CD 1a nor CD 1b, but trace expression of CD1c has been reported.7 Human epidermal Langerhans cells express CD 1a and CD1c, but these antigens are down-modulated in culture as these cells become more like blood dendritic cells. In terms of NK cell markers, blood dendritic cells do not express either CD56 or CD57, and as described above, CD 16 (Fc-γ-RIII) is also not detected by FACS.7 Surface molecules in the family of the integrins, adhesion molecules involved in many aspects of cell-to-cell adhesions and interactions, are expressed at very high levels on the surface of the blood dendritic cell. These extracellular matrix and cell-adhesion receptors integrate the extracellular environment with the cytoskeleton.28 Three separate subgroups of integrins have been identified within the family, and these are distinguished on the basis of the beta chain of these dimeric molecules. Interestingly, blood dendritic cells express both LFA-1 (CD11a) and its ligand ICAM-1 (CD54) at fairly high levels, and they also express high levels of LFA-3 (CD58) which is the receptor for the CD2 molecule on T cells.7 Additionally, CD 18 (the β-2 integrin), CD29 (the β-1 integrin), and CD11c (p150/90) are expressed at relatively high levels, and there is trace expression of CD11b (the C3bi receptor).7 The high levels of expression of a large number of different integrins/adhesins on the surface of dendritic cells correlates with their formidable ability to bind T cells (see Figure 4).
Immunophenotypic Markers
Published in Wojciech Gorczyca, Atlas of Differential Diagnosis in Neoplastic Hematopathology, 2014
CD11b is expressed by monocytes (macrophages), granulocytes, dendritic cells, and NK cells. It is negative in mature B and T cells, but activated CD8+ T cells (e.g., in viral infections) and some T-LGL leukemia cells are often CD11b+ (at least partially). AMLs with monocytic differentiation are usually CD11b+, whereas myeloblasts from AML with or without maturation only sporadically display aberrant expression of CD11b. The CD11b+ AML is seen more often in cases with unfavorable cytogenetics, and the expression of CD11b correlates with monosomal karyotype (defined as two or more autosomal monosomies or one monosomy with other structural aberrations) and predicts an extremely poor prognosis [54]. APLs are CD11b negative. Lack of CD11b and CD13 expression in transient myeloproliferative disorder helps to differentiate it from AML in infants with Down syndrome, which are usually CD11b+/CD13+ [55].
ADAM12 abrogation alters immune cell infiltration and improves response to checkpoint blockade therapy in the T11 murine model of triple-negative breast cancer
Published in OncoImmunology, 2023
Guanpeng Wang, Yeni Romero, Indhujah Thevarajan, Anna Zolkiewska
We next compared the numbers and composition of tumor-infiltrating immune cells in A12-KO (g1) versus control T11 tumors. When tumors reached a similar size, they were resected, enzymatically digested, and single cell suspensions were stained and analyzed by flow cytometry. First, we observed that the total number of tumor-infiltrating CD45+ immune cells in A12-KO (g1) tumors was decreased by 25–30% compared to T11 tumors (Figure 2a). This decrease was due to the reduction of the myeloid CD11b+ cell population, from ~2.4x106 to ~1.6x106 cells/g, or from ~90% to ~83% of all CD45+ cells (Figure 2b). In contrast, the absolute number of CD11b- cells was slightly, but not significantly, higher in A12-KO (g1) cells and amounted to ~3x105 cells/g of tumor tissue. The percentage of CD11b- cells among CD45+ cells rose from 10% in T11 tumors to 16% in A12-KO (g1) tumors, and this increase was significant (Figure 2c).
An Improved Ocular Impression Cytology Method: Quantitative Cell Transfer to Microscope Slides Using a Novel Polymer
Published in Current Eye Research, 2022
Adam Master, Wei Huang, Liqun Huang, Robert Honkanen, Basil Rigas
All general solvents and reagents were of HPLC grade or of the highest grade commercially available. Nitrocellulose membranes: mixed cellulose nitrate and acetate esters, 0.22 µm pore size, (cat. no. GSTF14250, Millipore Corp. Bedford, MA). Glutaraldehyde 50% aqueous solution (16320, Electron Microscopy Sciences, Hatfield, PA). Bovine collagen type I 5 mg/mL (A1064401, Thermo Fisher Scientific, CA). Reagents: Sodium metasulfite (161519), Ponceau S (141194), ethanol (T038181000), 1-butanol (B7906), poly-L-lysine 0.1% (w/v) in H2O (P8920), polyethylenimine branched Mn~10,000 (408727), polyethylene glycol 400 (202398), periodic Acid-Schiff PAS kit (395B), hematoxylin (HHS16) and eosin (HT110316), Rhodamine B isothiocyanate 283924 and fluorescein isothiocyanate (46950) were from Sigma (St Louis, MO). VECTASHIELD® Antifade Mounting Medium with DAPI (H-1500, Vector Laboratories, Burlingame, CA). S100A8/9 antibody (48M7C7, Norvus, St Louis, MO). ATF4 (11815, Cell Signalling, Beverly, MA). NFAT5 antibody (GTX23446, GeneTex). Antibodies: CD11b/ITGAM (ab133357, Abcam, Cambridge, MA). HRP-anti-rabbit IgG (ab7090), HRP-anti-mouse (ab47827), FITC-anti-rabbit (ab6717), FITC-anti-mouse (ab6785), Texas Red anti-mouse (ab6787), Texas Red anti-rabbit (ab6719) antibodies, as well as goat IgG (ab37373), rabbit IgG (ab37415) and mouse IgG (ab37355) Isotype controls were from Abcam (Cambridge, MA). Histostain Plus Bulk kit (85–8943, Invitrogen, Frederick, MD). In all instances, we used the antibody dilutions recommended by their respective manufacturers; they ranged between 1:200 and 1:2,000.
Cepharanthine loaded nanoparticles coated with macrophage membranes for lung inflammation therapy
Published in Drug Delivery, 2021
Caihong Lu, Jinpeng Zheng, Yaning Ding, Yuanyuan Meng, Fangyun Tan, Wei Gong, Xiaoyang Chu, Xiaolong Kong, Chunsheng Gao
The successfully coating MMs on the surface of NLCs was further confirmed by the confocal microscopy (Figure 2(E) and Supplementary Figure 3). Cy5.5 (green) encapsulated NLCs were coated with DiI (red) labeled MMs and were observed in captured images. Yellow color was observed when these two images were overlapped, illustrating that the green color and red color were in the same particle, proving that NLCs were successfully covered by MMs. In addition, the protein profiles in the MMs and MM-NLCs were determined by SDS-PAGE. The protein composition in the MMs was mostly retained in the MM-NLCs, but no protein signal was detected from the NLCs (Supplementary Figure S2), suggesting the successful translocation and retention of natural macrophage cell membranes onto the NLCs surface. Specific membrane proteins are signs of the functional integrity of the cell membrane. According to previous reports, CD44 and CD11b are related to the adhesion and signal transduction in inflammation (Worthen et al., 1989; Li et al., 2019). Furthermore, the inflamed endothelium highly expresses P-selectin and intercellular cell adhesion molecule-1 (ICAM-1), which are corresponding ligands to CD44 and CD11b (Bullard et al.,1999; Volin, 2005). Western blot analysis was carried out to confirm that the expression of CD44 and CD11b was maintained in the MM-NLCs, similar to that of MMs (Figure 2(C)). Collectively, all these representative proteins could be found in MMs and MM-NLCs, which indicated that the coating process did not affect the biological properties of MMs.