Summary
This report deals with the expression of stress-response (heat-shock) protein 72 (srp 72) in a series of 95 primary human brain tumors and 21 carcinoma metastases to the central nervous system (CNS). Immunohistochemical procedures were employed; cells of the human cervical cancer line HeLa S3 were used as positive controls. The protein was detected in 14/22 meningiomas and in 6/13 glioblastomas. Tumor cells expressing srp 72 were also found in 4/17 astrocytomas, 2/9 pituitary tumors, 2/14 primitive neuroectodermal tumors and 1/10 medulloblastomas. Whereas the majority (8/10) of the breast carcinoma metastases had tumor cells that expressed srp 72, only 2/11 lung tumor metastases were positively stained. These results document srp 72 expression by a variety of primary and metastatic tumors of the CNS.
Similar content being viewed by others
References
Arrigo A-P, Suhan JP, Welch WJ (1988) Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat-shock protein. Mol Cell Biol 8:5059–5071
Brown IR (1990) Induction of heat shock (stress) genes in the mammalian brain by hyperthermia and other traumatic events: a current perspective. J Neurosci Res 27:247–255
Brown IR, Rush S, Ivy GO (1989) Induction of a heat shock gene at the site of tissue injury in the rat brain. Neuron 2:1559–1564
Chirico WJ, Waters MG, Blobel G (1988) 70K heat shockrelated proteins stimulate protein translocation into microsomes. Nature 332:805–810
Cosgrove JW, Brown IR (1983) Heat shock protein in mammalian brain and other organs after a physiologically relevant increase in body temperature induced by D-lysergic acid diethylamide. Proc Natl Acad Sci USA 80:569–573
Dwyer BE, Nishimura RN, Brown IR (1989) Synthesis of the major inducible heat shock protein in rat hippocampus after neonatal hypoxia-ischemia. Exp Neurol 104:28–31
Ellis RJ, van der Vies SM (1991) Molecular chaperones. Annu Rev Biochem 60:321–347
Finlay CA, Hinds PW, Tan T-H, Eliyahu D, Oren M, Levine AJ (1988) Activating mutations for transformation by p53 produce a gene product that forms an hsc 70-p53 complex with an altered half-life. Mol Cell Biol 8:531–539
Flaherty KM, DeLuca-Flaherty C, McKay DB (1990) Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346:623–628
Garofalo O, Kennedy PGE, Swash M, Martin JE, Luthert P, Anderton BH, Leigh PN (1991) Ubiquitin and heat shock protein expression in amyotrophic lateral sclerosis. Neuropathol Appl Neurobiol 17:39–45
Gonzalez MF, Shiraishi K, Hisanaga K, Sagar SM, Mandabach M, Sharp FR (1989) Heat shock proteins as markers of neural injury. Mol Brain Res 6:93–100
Gower DJ, Hollman C, Lee KS, Tytell M (1989) Spinal cord injury and the stress protein response. J Neurosurg 70:605–611
Hamos JE, Oblas B, Pulaski-Salo D, Welch WJ, Bole DG, Drachman DA (1991) Expression of heat shock proteins in Alzheimer's disease. Neurology 41:345–350
Hatayama T, Honda K-I, Yukioka M (1986) Effects of sodium butyrate and dibutyryl cyclic AMP on thermosensitivity of HeLa cells and their production of heat shock proteins. Biochem Int 13:793–798
Herz F, Miller OJ, Miller DA, Auersperg N, Koss LG (1977) Chromosome analysis and alkaline phosphatase of C4I, a cell line of human cervical origin distinct from HeLa. Cancer Res 37:3209–3213
Herz F, Gazivoda P, Papenhausen PR, Katsuyama J, Koss LG (1985) Normal human urothelial cells in culture. Subculture procedure, flow cytometric and chromosomal analyses. Lab Invest 53:571–574
Hsu S-M, Raine L, Fanger H (1981) Use of avidin-biotinperoxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures. J Histochem Cytochem 29:577–580
Itoh H, Tashima Y (1991) The stress (heat shock) proteins. Int J Biochem 11:1185–1191
Jacewicz M, Kiessling M, Pulsinelli WA (1986) Selective gene expression in focal cerebral ischemia. J Cereb Blood Flow Metab 6:263–272
Kang P-J, Ostermann J, Shilling J, Neupert W, Craig EA, Pfanne N (1990) Requirement for hsp 70 in the mitochomdrial matrix for translocation and folding of precursor proteins. Nature 348:137–143
Kato M, Herz F, Kato S, Hirano A (1992) Expression of stress-response (heat-shock) protein 27 in human brain tumors: an immunohistochemical study. Acta Neuropathol 83:420–422
Koskinen PJ, Sistonen L, Evan G, Morimoto R, Alitalo K (1991) Nuclear colocalization of cellular and viral myc proteins with HSP70 in myc-overexpressing cells. J Virol 65:842–851
Lindquist S, Craig EA (1988) The heat-shock proteins. Annu Rev Genet 22:631–677
Luo Y, Amin J, Voellmy R (1991) Ecdysterone receptor is a sequence-specific transcription factor involved in the developmental regulation of heat shock genes. Mol Cell Biol 11:3660–3675
Marini AM, Kozuka M, Lipsky RH, Nowak TS Jr (1990) 70-Kilodalton heat shock protein induction in cerebellar astrocytes and cerebellar granule cells in vitro: comparison with immunocytochemical localization after hyperthermia in vivo. J Neurochem 54:1509–1516
Martin JE, Mather K, Swash M, Garofalo O, Leigh PN, Anderton BH (1991) Heat shock protein expression in corpora amylacea in the central nervous system: clues to their origin. Neuropathol Appl Neurobiol 17:113–119
Michishita M, Satoh M, Yamaguchi M, Hirayoshi K, Okuma M, Nagata K (1991) Phosphorylation of the stress protein hsp 27 is an early event in murine myelomonocytic leukemic cell differentiation induced by leukemia inhibitory factor/D-factor. Biochem Biophys Res Commun 176:979–984
Milarski KL, Morimoto RI (1989) Mutational analysis of the human hsp 70 protein: distinct domains for nucleolar localization and adenosine triphosphate binding. J Cell Biol 109:1947–1962
Morandi A, Fried V, Smith H, Welch W, Perry G, Autilio-Gambetti L, Gambetti P (1988) Ubiquitin and other stress proteins in cultured nervous tissue after heat shock and aluminum intoxication. J Neuropathol Exp Neurol 47:331
Morimoto RI (1991) Heat shock: the role of transient inducible responses in cell damage, transformation, and differentiation. Cancer Cells 3:295–301
Nishimura RN, Dwyer BE, Vinters HV, De Vellis J, Cole R (1991) Heat shock in cultured neurons and astrocytes: correlation of ultrastructure and heat shock protein synthesis. Neuropathol Applied Neurobiol 17:139–147
Pechan PM (1991) Heat shock proteins and cell proliferation. FEBS Lett 280:1–4
Pinhasi-Kimhi O, Michalovitz D, Ben-Zeev A, Oren M (1986) Specific interaction between the p53 cellular tumour antigen and major heat shock proteins. Nature 320:182–185
Rattner JB (1991) Hsp 70 is localized to the centrosome of dividing HeLa cells. Exp Cell Res 195:110–113
Sprang GK, Brown IR (1987) Selective induction of a heat shock gene in fibre tracts and cerebellar neurons of the rabbit brain detected by in situ hybridization. Mol Brain Res 3: 89–93
Tandon AK, Clark GM, Chamness GC, Fuqua SAW, Welch WJ, Riehl RM, McGuire WL (1990) Heat shock/stress response proteins: biological and clinical significance in breast cancer. Proc Am Soc Clin Oncol 9:23
Vass K, Welch WJ, Nowak TS Jr (1988) Localization of 70-kDa stress protein induction in gerbil brain after ischemia. Acta Neuropathol 77:128–135
Vass K, Berger ML, Nowak TS Jr, Welch WJ, Lassmann H (1989) Induction of stress protein HSP 70 in nerve cells after status epilepticus in the rat. Neurosci Lett 100:259–264
Welch WJ, Suhan JP (1986) Cellular and biochemical events in mammalian cells during and after recovery from physiological stress. J Cell Biol 103:2035–2052
Wu BJ, Morimoto RI (1985) Transcription of the human hsp 70 gene is induced by serum stimulation. Proc Natl Acad Sci USA 82:6070–6074
Zülch KJ (1979) Histological typing of tumors of the central nervous system. World Health Organization, Geneva
Author information
Authors and Affiliations
Additional information
Supported in part by NIH grant CA47512 (to FH)
Rights and permissions
About this article
Cite this article
Kato, S., Hirano, A., Kato, M. et al. Stress-response (heat-shock) protein 72 expression in tumors of the central nervous system: an immunohistochemical investigation. Acta Neuropathol 84, 261–264 (1992). https://doi.org/10.1007/BF00227818
Received:
Revised:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00227818