Changes on lysosomal compartment during PMA-induced differentiation of THP-1 monocytic cells: Influence of type I and type IV collagens

Abstract

In this work, the influence of different substrate adhesion during phorbol-12-myristate-13-acetate (PMA)-induced differentiation of THP-1 monocytic cell line was studied. In particular, by morphocytochemical and cytometric approaches, the influence of type I and type IV collagens in an experimental model representative of three phases (initial, intermediate and terminal) of monocyte-macrophage transition was analyzed. The cells in these three phases of differentiation were obtained by using 6, 30 e 60 nM PMA. In this experimental model, referring to adhesion to glass as control, by using the azo-dye coupling method, we have considered the analysis of Acid Phosphatase (AcP) activity as a marker of differentiated status expression, in relation to the acquisition of macrophagic phenotype. Endosomal/lysosomal system was further characterized by taking into account the uptake of fluorescent probe LysoTracker Red. Fluorochromization in the various experimental conditions was analyzed morphologically (fluorescence microscopy) and quantitatively (static cytometry). Data related to lysosome compartment were integrated, from a cytokinetic point of view, by flow cytometry measurements of DNA/protein content. Our results have indicated that type I and type IV collagens were able to influence, with respect to glass adhesion, various differentiation phases. Type I collagen showed the higher effects in the condition of high differentiation (60 nM PMA), causing an increase in AcP activity and lysosomal system. Type IV collagen, besides determining effects on lysosomal compartment of intermediate and terminally differentiated cells, influenced mainly proliferative activity of cells with initial differentiation level (6 nM PMA).

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Spano, A. , Barni, S. , Bertone, V. and Sciola, L. (2013) Changes on lysosomal compartment during PMA-induced differentiation of THP-1 monocytic cells: Influence of type I and type IV collagens. Advances in Bioscience and Biotechnology, 4, 8-18. doi: 10.4236/abb.2013.48A3002.

Conflicts of Interest

The authors declare no conflicts of interest.

References

[1] Andreesen, R., Brugger, W., Scheinbenbogen, C., Kreutz, M., Leser, H.G., Rehm, A. and Lohr, G.W. (1990) Surface phenotype analysis of human monocyte to macrophage maturation. Journal of Leukocyte Biology, 47, 490-497.
[2] Anegon, I., Blottiere, H., Cuturi, M.C., Blottiere, H., Cuturi, M.C., Lenne, Y., Trinchieri, G., Faust, J. and Perussia, B. (1993) Characterization of a human monocyte antigen, B148.4, regulated during cell differentiation and activation Journal of Leukocyte Biology, 53, 390-398.
[3] Huh, H.Y., Pearce, S.F., Yesner, L.M., Schindler, J.L. and Silverstein, R.L. (1996) Regulated expression of CD36 during monocyte-to-macrophage differentiation: potential role of CD36 in foam cell formation. Blood, 87, 2020-2028.
[4] Kreutz, M., Krause, S.W., Hennemann, B., Rehm, A. and Andreesen, R. (1992) Macrophage heterogeneity and differentiation: Defined serum-free culture conditions induce different types of macrophages in vitro. Research in Immunology, 143, 107-115. doi:10.1016/0923-2494(92)80087-2
[5] Prieto, J., Eklund, A. and Patarroyo, M. (1994) Regulated expression of integrins and other adhesion molecules during differentiation of monocytes into macrophages. Cellular Immunology, 156, 191-211. doi:10.1006/cimm.1994.1164
[6] Poli, G., Wang, J.M., Ruco, L., Rossini, S., Biondi, A., Mantovani, A. and Uccini, S. (1993) Expression and modulation of a mononuclear phagocyte differentiation antigen (PAM-1) during in vitro maturation of peripheral blood monocytes. International Journal of Clinical and Laboratory Research, 23, 83-87. doi:10.1007/BF02592288
[7] Kreutz, M., Andreesen, R., Krause, S.W., Szabo, A., Ritz, E. and Reichel, H. (1993) 1,25-dihydroxyvitamin D3 production and vitamin D3 receptor expression are developmentally regulated during differentiation of human monocytes into macrophages. Blood, 82, 1300-1307.
[8] Cleary, J.A., Kelly, G.E. and Husband, A.J. (1999) The effect of molecular weight and -1,6-linkages on priming of macrophage function in mice by (1,3)—D-glucan. Immunology and. Cell Biology, 77, 395-403. doi:10.1046/j.1440-1711.1999.00848.x
[9] Murao, S., Gemmell, M.A., Callaham, M.F., Anderson, N.L. and Huberman, E. (1983) Control of macrophage cell differentiation in human promyelocytic HL-60 leukemia cells by 1,25-dihydroxyvitamin D3 and phorbol12-myristate-13-acetate. Cancer Research, 43, 4989-4996.
[10] Olsson, I., Gullberg, U., Ivhed, I. and Nilsson, K. (1983) Induction of differentiation of the human histiocytic lymphoma cell line U-937 by 1 alpha,25-dihydroxycholecalciferol. Cancer Research, 43, 5862-5867.
[11] Fleit, H.B. and Kobasiuk, C.D. (1991) The human monocyte-like cell line THP-1 expresses Fc gamma RI and Fc gamma RII. Journal of Leukocyte Biology, 49, 556-565.
[12] Rovera, G., O’Brien, T.G. and Diamond, L. (1979) Induction of differentiation in human promyelocytic leukemia cells by tumor promoters. Science, 204, 868-870. doi:10.1126/science.286421
[13] Kohro, T., Tanaka, T., Murakami, T., Wada, Y., Aburatani, H., Hamakubo, T., Kodama, T. (2004) A compareson of differences in the gene expression profiles of phorbol 12-myristate 13-acetate differentiated THP-1 cells and human monocyte-derived macrophage. Journal of Atherosclerosis and Thrombosis, 11, 88-97. doi:10.5551/jat.11.88
[14] Park, E.K., Jung, H.S., Yang, H.I., Yoo, M.C., Kim, C., et al. (2007) Optimized THP-1 differentiation is required for the detection of responses to weak stimuli. Inflammation Research, 56, 45-50. doi:10.1007/s00011-007-6115-5
[15] Schwende, H., Fitzke, E., Ambs, P. and Dieter, P. (1996) Differences in the state of differentiation of THP-1 cells induced by phorbol ester and 1,25-dihydroxyvitamin D3. Journal of Leukocyte Biology, 59, 555-561.
[16] Spano, A., Barni, S. and Sciola, L. (2013) PMA withdrawal in PMA-treated monocytic THP-1 cells and subsequent retinoic acid stimulation, modulate induction of apoptosis and appearance of dendritic cells. Cell Proliferation, 46, 328-347. doi:10.1111/cpr.12030
[17] Gantner, F., Kupferschmidt, R., Schudt, C., Wendel, A, Hatzelmann, A. (1997) In vitro differentiation of human monocytes to macrophages: Change of PDE profile and its relationship to suppression of tumour necrosis factoralpha release by PDE inhibitors. British Journal of Pharmacology, 121, 221-231. doi:10.1038/sj.bjp.0701124
[18] Spano, A., Monaco, G., Barni, S. and Sciola L. (2007) Expression of cell kinetics and death during monocytemacrophage differentiation: Effects of Actinomycin D and Vinblastine treatment. Histochemistry and Cell Biology, 127, 79-94. doi:10.1007/s00418-006-0227-9
[19] De Fougerolles, A.R. and Koteliansky, V.E. (2002) Regulation of monocyte gene expression by the extracellular matrix and its functional implications. Immunological Reviews, 186, 208-220. doi:10.1034/j.1600-065X.2002.18617.x
[20] Robinson, J.M. and Karnovsky, M.J. (1983) Ultrastructural localization of several phosphatases with cerium. Journal of Histochemistry and Cytochemistry, 31, 1197-1208. doi:10.1177/31.10.6309949
[21] Wiese, M., Berger, O., Stierhof, Y.D., Wolfram, M., Fuchs, M. and Overath, P. (1996) Gene cloning and cellular localization of a membrane-bound acid phosphatase of Leishmania mexicana. Molecular and Biochemical Parasitology, 82, 153-165. doi:10.1016/0166-6851(96)02729-6
[22] Karnovsky, M.L. and Lazdins, J.K. (1978) Biochemical criteria for activated macrophages. Journal of Immunology, 121, 809-813.
[23] Matsubara, S. (2002) Glucose-6-phosphate dehydrogenase and mouse Kupffer cell activation: An ultrastructural dual staining enzyme-cytochemical study. Histochemistry and Cell Biology, 118, 345-350.
[24] Campbell, G.R. and Spector, S.A. (2011) Hormonally active vitamin D3 (1alpha,25-dihydroxycholecalciferol) triggers autophagy in human macrophages that inhibits HIV-1 infection. Journal of Biological Chemistry, 286, 18890-18902. doi:10.1074/jbc.M110.206110
[25] Barka, T. and Anderson, P.J. (1962) Histochemical methods for acid phosphatase using hexazonium pararosanilin as coupler. Journal of Histochemistry and Cytochemistry, 10, 741-753. doi:10.1177/10.6.741
[26] Jacob, S.S., Shastry, P. and Sudhakaran, P.R. (2002) Monocyte-macrophage differentiation in vitro: Modulation by extracellular matrix protein substratum. Molecular and Cellular Biochemistry, 233, 9-17. doi:10.1023/A:1015593232347
[27] Siljander, P.R., Hamaia, S., Peachey, A.R., Slatter, D.A., Smethurst, P.A., Ouwehand, W.H., Knight, C.G. and Farndale, R.W. (2004) Integrin activation state determines selectivity for novel recognition sites in fibrillar collagens. Journal of Biological Chemistry, 279, 47763-47772. doi:10.1074/jbc.M404685200
[28] Wang, P., Ballestrem, C. and Streuli, C.H. (2011) The C terminus of talin links integrins to cell cycle progression. Journal of Cell Biology, 195, 499-513. doi:10.1083/jcb.201104128
[29] Assoian, R.K. and Schwartz, M.A. (2001) Coordinate signaling by integrins and receptor tyrosine kinases in the regulation of G1 phase cell-cycle progression. Current Opinion in Genetics & Development, 11, 48-53. doi:10.1016/S0959-437X(00)00155-6
[30] Sondag, C.M. (2010) Adhesion of monocytes to type I collagen stimulates an APP-dependent proinflammatory signaling response and release of Aβ1-40. Journal of Neuroinflammation, 7, 22-31. doi:10.1186/1742-2094-7-22
[31] Auwerx, J. (1991) The human leukemia cell line, THP-1: A multifacetted model for the study of monocyte-macrophage differentiation. Experientia, 47, 22-31. doi:10.1007/BF02041244
[32] Zhu, L. and Skoultchi, A.I. (2001) Coordinating cell proliferation and differentiation. Current Opinion in Genetics & Development, 10, 91-97. doi:10.1016/S0959-437X(00)00162-3
[33] Hollenbeck, S.T., Itoh, H., Louie, O., Faries, P.L., Liu, B. and Kent, K.C. (2004) Type I collagen synergistically enhances PDGF-induced smooth muscle cell proliferation through pp60src-dependent crosstalk between the alpha2beta1 integrin and PDGFbeta receptor. Biochemical and Biophysical Research Communications, 325, 328-337. doi:10.1152/ajpgi.00262.2003
[34] Wesley, R.B. 2nd, Meng, X., Godin, D. and Galis, Z.S. (1998) Extracellular matrix modulates macrophage functions characteristic to atheroma: Collagen type I enhances acquisition of resident macrophage traits by human peripheral blood monocytes in vitro. Arteriosclerosis, Thrombosis, and Vascular Biology, 18, 432-440. doi:10.1161/01.ATV.18.3.432
[35] Sanders, M.A. and Basson, M.D. (2004) Collagen IV regulates Caco-2 migration and ERK activation via α1β1- and α2β1-integrin-dependent Src kinase activation. American Journal of Physiology. Gastrointestinal and Liver Physiology, 286, G547-557. doi:10.1152/ajpgi.00262.2003
[36] Adiguzel, E., Ahmad P.J., Franco, C., Michelle, P. and Bendeck, M.P. (2009) Collagens in the progression and complications of Atherosclerosis. Vascular Medicine, 14, 73-89.
[37] Armstrong, J.W. and Chapes, S.K. (1994) Effects of extracellular matrix proteins on macrophages differentiation, growth and function: Comparison of liquid and agar culture system. Journal of Experimental Zoology, 269, 178-187. doi:10.1002/jez.1402690303
[38] Matheson, L.A., Maksym, G.N., Santerre, J. P., Rosalind, S. and Labow, R.S. (2006) The functional response of U937 macrophage-like cells is modulated by extracellular matrix proteins and mechanical strain. Biochemistry and Cell Biology, 84, 763-773. doi:10.1139/o06-093
[39] Miranda, M.B., McGuire, T.F. and Johnson, D.E. (2002) Importance of MEK-1/-2 signaling in monocytic and granulocytic differentiation of myeloid cell lines. Leukemia, 16, 683-692. doi:10.1038/sj.leu.2402400
[40] Galt, S.W., Lindemann, S., Medd, D., Allen, L.L., Kraiss, L.W., Harris, E.S., Prescott, S.M., McIntyre, T.M., Weyrich, A.S. and Zimmerman, G.A. (2001) Differential regulation of matrix metalloproteinase-9 by monocytes adherent to collagen and platelets. Circulation Research, 89, 509-516. doi:10.1161/hh1801.096339
[41] Shapiro, S.D., Kobayashi, D.K., Pentland, A.P. and Welgus, H.G. (1993) Induction of macrophage metalloproteinases by extracellular matrix. Evidence for enzyme- and substratespecific responses involving prostaglandin-dependent mechanisms. Journal of Biological Chemistry, 268, 8170-8175.
[42] Lepidi, S., Kenagy, R.D., Raines, E.W., Chiu, E.S., Chait, A., Ross, R. and Clowes, A.W. (2001). MMP9 production by human monocyte-derived macrophages is decreased on polymerized type I collagen. Journal of Vascular Surgery, 34, 1111-1118. doi:10.1067/mva.2001.119401
[43] McDowell, E.M. (1973) Acid phosphatase activity in Golgi apparatus and related structures in pars recta of rat kidney studied by thin and semi-thin section cytochemistry. Histochemie, 34, 281-291. doi:10.1007/BF00306300
[44] Goel, G., Makkar, H.P.S., Francis, G. and Becker, K. (2007) Phorbol esters: Structure, biological activity, and toxicity in animals. International Journal of Toxicology, 26, 279-288. doi:10.1080/10915810701464641

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