Heat shock proteins (HSPs) are expressed or increased in response to various biological stresses. Moreover, these ‘stress proteins’ seem to be expressed by some cells living in physiological conditions. From then on, they could play an important physiological role in normal cell functioning. The best-known physiological role of these HSP proteins is to act as ‘molecular chaperones’. In this context, we have investigated the immunohistochemical expression of HSP27, HSP70, HSP90 and HSP110 in 10 human adult salivary glands. To highlight the presence of RNAm encoding HSP70, an in situ hybridization was performed. In our material, HSP27 was strongly expressed in the cytoplasm of striated duct cells and in some myoepithelial cells. The same localization was less stained for HSP70 and HSP90. The immunocytochemical reaction was weak or negative for HSP110 in striated ducts. HSPs were not expressed in acinic cells. In situ hybridization gave a positive signal in striated ducts with a probe encoding HSP70. Epithelial cells of the striated ducts and myoepithelial cells expressed HSP27, HSP70 and HSP90. These HSPs probably act in part as molecular chaperones for protein synthesis, transport and for several interactions between HSPs and different proteins.

Keywords:
Salivary gland, Heat shock protein, Chaperone, molecular, Immunohistochemistry
1.
Adams, D.J., W.L. McGuire (1983) Detection of a Mr 24,000 estrogen-regulated protein in human breast cancer by monoclonal antibodies. Cancer Res 43: 4297–4301.
2.
Adams, D.J., W.L. McGuire (1985) Quantitative enzyme-like immunosorbent assay for the estrogen regulated Mr 24,000 protein in human breast tumors: Correlation with estrogen and progesterone receptors. Cancer Res 45: 2445–2449.
3.
Alexandrov, V. (1994) Functional aspects of cell response to heat shock. Int Rev Cytol 148: 171–227.
4.
Angelov, A., K. Dirkranian, M. Trosheva (1996) Immunomorphological characteristics of pleomorphic adenoma of salivary glands. Bull Group Int Rech Sci Stomatol Odontol 39: 67–75.
5.
Beckmann, R.P., L.A. Mizzen, W.J. Welch (1990) Interaction of HSP70 with newly synthesized proteins: Implications for protein folding and assembly. Science 248: 850–854.
6.
Bitar, K.H., M.S. Kaminski, N. Hailat, K.B. Cease, J.R. Strahler (1991) HSP27 is a mediator of sustained smooth muscle contraction in response to bombesin. Biochem Biophys Res Commun 181: 1192–1200.
7.
Blake, M.J., T.S. Nowak Jr, N.J. Holbrook (1990) In vivo hyperthermia induces expression of HSP70 mRNA in brain regions controlling the neuroendocrine response to stress. Brain Res Mol Brain Res 8: 89–92.
8.
Born, I.A., K. Schwechheimer, H. Maier, H.F. Otto (1987) Cytokeratin expression in normal salivary glands and in cystadenolymphomas demonstrated by monoclonal antibodies against selective cytokeratin polypeptides. Virchows Arch 411: 583–589.
9.
Burdon, R.H. (1986) Heat shock and the heat shock proteins. Biochem J 240: 313–324.
10.
Bussolati, G., G. Botta, P. Gugliotta (1980) Actin-rich (myoepithelial) cells in ductal carcinoma in-situ of the breast. Virchows Arch 34: 251–259.
11.
Caselitz, J., M. Osborn, K. Hamper, J. Wustrow, B. Rauchu, K. Weber (1986a) Pleomorphic adenomas, adenoid cystic carcinoma and adenolymphomas of salivary glands analysed by a monoclonal antibody against myoepithelial/basal cells. Virchows Arch 409: 805–816.
12.
Caselitz, J., M. Osborn, G. Seifert, K. Weber (1981) Intermediate-sized filament proteins (prekeratin, vimentin, desmin) in the normal parotid gland and parotid gland tumours. Virchows Arch 393: 273–286.
13.
Caselitz, J., B. Walther, J. Wustrow, G. Seifert, K. Weber, M. Osborn (1986b) A monoclonal antibody that detects myoepithelial cells in exocrine glands, basal cells in other epithelia and basal and suprabasal cells in certain hyperplastic tissues. Virchows Arch 409: 725–738.
14.
Clarck, B.D., I.R. Brown (1986) A retinal heat shock protein is associated with elements of cytoskeleton and binds to calmodulin. Biochem Biophys Res Commun 139: 974–981.
15.
Czar, M.J., M.J. Welsh, W.B. Pratt (1996) Immunofluorescence localization of the 90-kDa heat-shock protein to cytoskeleton. Eur J Cell Biol 70: 322–330.
16.
Dodd, S.M., J.E. Martin, M. Swash, K. Mather (1993) Expression of heat shock protein epitopes in renal disease. Clin Nephrol 39: 239–244.
17.
Draeger, A., W.B.J. Nathrath, E.B. Lane, B.E. Sundström, T.I. Stigbrand (1991) Cytokeratins, smooth muscle actin and vimentin in human normal salivary gland and pleomorphic adenomas. Immunohistochemical studies with particular reference to myoepithelial and basal cells. APMIS 99: 405–415.
18.
Ellis, R.J. (1987) Proteins as molecular chaperones. Nature 328: 378–379.
19.
Ellis, R.J. (1990) Molecular chaperones: The plant connection. Science 250: 954–959.
20.
Green, L.A., R.K. Liem (1989) β-Internexin is a microtubule-associated protein identical to the 70 kDa heat-shock cognate protein and the clathrin uncoating ATPase. J Biol Chem 264: 15210–15215.
21.
Gupta, R.S. (1990) Mitochondria, molecular chaperone proteins and the in vivo assembly of microtubules. Trends Biochem Sci 15: 415–418.
22.
Kato, K., H. Shinohara, S. Goto, Y. Inaguma, R. Morhisita, T. Asano (1992) Copurification of small heat shock protein with αB crystallin from human skeletal muscle. J Cell Biol 267: 7118–7125.
23.
Langer, T., C. Lu, H. Echols, J. Flanagan, M.K. Hayer, F.U. Hartl (1992) Successive action of DnaK, DnaJ, and GroEL along the pathway of chaperone-mediated protein folding. Nature 356: 683–689.
24.
Lee, W.-C., Y.-C. Lee, M.-D. Perng, C.-M. Chen, Y.-K. Lai (1993) Induction of vimentin modification and vimentin-HSP72 association by withangulatin A in 9L rat brain tumor cells. J Cell Biochem 52: 253–265.
25.
Liao, J., L.A. Lowthert, N. Ghori, M.B. Omary (1995) The 70-kDa heat shock proteins associated with glandular intermediate filaments in an ATP-dependent manner. J Biol Chem 270: 915–922.
26.
Lindquist, S., E.A. Craig (1988) The heat-shock proteins. Annu Rev Genet 22: 631–677.
27.
Matsubara, O., T. Kasuga, F. Marumo, H. Itoh, Y. Tashima (1990) Localisation of 90-kDa heat shock protein in the kidney. Kidney Int 38: 830–834.
28.
Maytin, E.V. (1995) Heat shock proteins and molecular chaperones: Implications for adaptative responses in the skin. J Invest Dermatol 104: 448–455.
29.
Mori, M., K. Yamada, T. Tanaka, Y. Okada (1990) Multiple expression of keratins, vimentin, and S-100 protein in pleomorphic salivary adenomas. Virchows Arch 58: 435–444.
30.
Napolitano, E.W., J.S. Pacher, S.S.M. Chin, R.K.H. Liem (1985) Beta-internexin, a ubiquitous intermediate filament-associated protein. J Cell Biol 101: 1323–1331.
31.
Nicholl, I.D., R.A. Quinlan (1994) Chaperone activity of α-crystallins modulates intermediate filament assembly. EMBO J 13: 945–953.
32.
Ohtsuka, K., K. Tanabe, H. Nakamura, C. Sato (1986) Possible association of 69,000- and 68,000-dalton heat shock proteins and structural relations among heat shock proteins in murine mastocytoma cells. Radiat Res 108: 34–42.
33.
Orito, T., H. Shinohara, Y. Okada, M. Mori (1989) Heterogeneity of keratin expression in epithelial tumor cells of adenolymphoma in paraffin sections. Pathol Res Pract 184: 600–608.
34.
Palmer R.M. (1986) The identification of myoepithelial cells in human salivary glands. A review and comparison of light microscopical methods. J Oral Pathol 15: 221–229.
35.
Palmer, R.M., R.B. Lucas, J. Knight, B. Gusterson (1985) Immunocytochemical identification of cell types in pleomorphic adenoma with particular reference to myoepithelial cells. J Pathol 146: 213–220.
36.
Parsell, D.A., Y. Sanchez, J.D. Stitzel, L. Lindquist (1991) HSP104 is a highly conserved protein with two essential nucleotide-binding sites. Nature 353: 270–273.
37.
Perdew, G.H., N. Hord, C.E. Hollenback, M. Welch (1993) Localization and characterization of the 86- and 84-kDa heat shock proteins in Hepa 1c1c7 cells. Exp Cell Res 209: 350–356.
38.
Saku, T., H. Okabe, Y. Yagi, E. Sato, N. Tsuda (1984) A comparative study on the immunolocalization of keratin and myosin in salivary gland tumors. Acta Pathol Jpn 34: 1031–1040.
39.
Schlesinger, M.J. (1990) Heat shock proteins. J Biol Chem 265: 12111–12114.
40.
Slater, S., R. Jalleh, J. Gilbertson, I. Lampert, R. Williamson, C.S. Foster (1997) Expression of heat shock proteins in chronic pancreatitis: Protective or pathogenic roles? Lab Invest 76: 533–545.
41.
Su, L., P.R. Morgan, D.L. Harrisson, A. Waseem, B. Lane (1993) Expression of keratin mRNAs and proteins in normal salivary epithelia and pleomorphic adenomas. J Pathol 171: 173–181.
42.
Takai, Y., Y. Noda, S. Sumitoma, K. Kawamura, M. Mori (1985) Immunohistochemical detection of keratin proteins in salivary gland ducts of mammals. Acta Histochem Cytochem 18: 353–361.
43.
Venkataseshan, V.S., E. Marquet (1996) Heat shock protein 72/73 in normal and diseased kidneys. Nephron 73: 442–449.
44.
Welch, W.J. (1992) Mammalian stress response: Cell physiology, structure/function of stress proteins, and implications for medicine and disease. Physiol Rev 72: 1063–1081.
45.
Welch, W.J. (1993) How cells respond to stress. Sci Am 286: 34–41.
46.
Wilkinson, J.M., I. Pollard (1993) Immunohistochemical localization of the 25 kDa heat shock protein in unstressed rats: Possible functional implications. Anat Rec 237:453–457.
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2000
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