Journal of Cancer Research and Treatment
ISSN (Print): 2374-1996 ISSN (Online): 2374-2003 Website: Editor-in-chief: Jean Rommelaere
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Journal of Cancer Research and Treatment. 2016, 4(2), 21-25
DOI: 10.12691/jcrt-4-2-1
Open AccessArticle

Histone H1.5 Expression in Prostatic Carcinoma: An Immunohistochemical Study

Mohamed A. El-Rashidy1, Asmaa E. Bedeer1 and Ahmed M. Kabel2, 3,

1Pathology Department, Faculty of Medicine, Tanta University, Tanta, Egypt

2Pharmacology department, Faculty of Medicine, Tanta University, Tanta, Egypt

3Department of clinical pharmacy, College of Pharmacy, Taif University, Taif, Saudi Arabia

Pub. Date: April 16, 2016

Cite this paper:
Mohamed A. El-Rashidy, Asmaa E. Bedeer and Ahmed M. Kabel. Histone H1.5 Expression in Prostatic Carcinoma: An Immunohistochemical Study. Journal of Cancer Research and Treatment. 2016; 4(2):21-25. doi: 10.12691/jcrt-4-2-1


Background and Aim: Histone H1.5 (HH1.5) is a subtype of histone H1, a family of linker proteins that is known to determine chromatin structure, alter gene expression and DNA repair. It also contributes to regulation of cell proliferation in breast cancer. In this study, we aimed to investigate the immunohistochemical expression of HH1.5 in various prostatic lesions. Methods: A total 50 cases of various prostatic biopsies were studied. Histone H1.5 expression was evaluated in all cases. HH1.5 expression was scored as negative (<11%), 1+ (11-50%), or 2+ (>50%). Correlations between the intensity and differential localization of these markers and Gleason patterns were evaluated. Results: HH1.5 immunohistochemistry revealed positive nuclear reactivity in all cases (100%) of prostate adenocarcinomas, compared to only 2 (11%) of 18 cases of benign prostatic glands (P ≤ 0.001). In all positive benign prostate epithelium, HH1.5 was limited to focal and weak reactivity. Similarly, both the two cases of high-grade prostatic intraepithelial neoplasia exhibited focal weak nuclear reactivity. Increased HH1.5 reactivity was observed in Gleason patterns 5 and 4 as compared to Gleason pattern 3, 100%, 64.7% and 50%, respectively (P ≤ 0.002). Conclusion: HH1.5 may be a useful diagnostic tool in evaluating prostatic biopsies, particularly with small foci of cancer. Further studies are needed to support these findings and investigate the possible prognostic significance of HH1.5 in prostatic adenocarcinomas.

histone expression prostate carcinoma

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[1]  Stein J, Majores M, Rohde M, Lim S, Schneider S, Perner S, Jung K, Kristiansen G and Kirfel J. KDM5C Is Overexpressed in Prostate Cancer and Is a Prognostic Marker for Prostate-Specific Antigen-Relapse Following Radical Prostatectomy .Am J Pathol 2014; 184: 2430-2437.
[2]  Lu Z, Qi L, Bo XJ, Liu GD, Wang JM, and Li G. Expression of CD26 and CXCR4 in prostate carcinoma and its relationship with clinical parameters J Res Med Sci 2013; 18(8): 647–652.
[3]  Epstein JI. Mimickers of prostatic intraepithelial neoplasia. Int J Surg Pathol 2010; 18:142S-8S.
[4]  Hameed O, Sublett J, Humphrey PA. Immunohistochemical stains for p63 and alpha-methyl acyl-CoA racemase, versus a cocktail comprising both, in the diagnosis of prostatic carcinoma a comparison of the immunohistochemical staining of 430 foci in radical prostatectomy and needle biopsy tissues. Am J Surg Pathol 2005;29:579-87.
[5]  Evans AJ. α-Methyl acyl CoA racemase (P504S): overview and potential uses in diagnostic pathology as applied to prostate needle biopsies. J Clin Pathol 2003; 56:892-7.
[6]  Zhou M, Chinnaiyan AM, Kleer CG, Lucas PC, RubinMA. α-Methyl acyl CoA racemase: a novel tumor marker over-expressed in several human cancers and their precursor lesions. Am J Surg Pathol 2002; 26:926-31.
[7]  Happel N, Doenecke D. Histone H1 and its isoforms: contribution to chromatin structure and function. Gene 2008; 431:1-12.
[8]  Sancho M, Diani E, Beato M, Jordan A. Depletion of human H1 variants uncovers specific roles in gene expression and cell growth. PLoS Genet 2008;4:1-17.
[9]  Li JY, Patterson M, Mikkola HK, Lowry WE, Kurdistani SK. Dynamic distribution of liner histone H1.5 in cellular differentiation. PLoS Genet 2012; 8:1-13.
[10]  Hechtman JF, Beasley MB, Kinoshita Y, Ko HM, Hao K, Burstein DE. Promyelocytic leukemia zinc finger and histone H1.5 differentially stain low- and high-grade pulmonary neuroendocrine tumors: a pilot immunohistochemical study. Human Pathol 2013; 44:1400-5.
[11]  Sato S, Takahashi S, Asamoto M, et al. Histone H1 expression in human prostate cancer tissues and cell lines. Pathol Int 2012;62:84-92.
[12]  Epstein JI, Allsbrook WC Jr, Amin MB, Egevad LL, ISUP Grading Committee. The 2005 International Society of Urological Pathology (ISUP) Consensus Conference on Gleason Grading of Prostatic Carcinoma. Am J Surg Pathol 2005; 1:228- 42.
[13]  Khachaturov V, Xiao GQ, PhD, Kinoshita Y, Unger P, Burstein DE. Histone H1.5, a novel prostatic cancer marker: an immunohistochemical study. Human Pathol 2014; 45: 2115–2119.
[14]  Izzo A, Kamieniarz K, Schneider R. The histone H1 family: specific members, specific functions?. Biol Chem 2008; 389:333-43.
[15]  Terme JM, Sesé B, Millán-Ariño L, et al. Histone H1 variants are differentially expressed and incorporated into chromatin during differentiation and reprogramming to pluripotency. J Biol Chem 2011; 286:35347-57.
[16]  Sato S, Takahashi S, Asamoto M, et al. Histone H1 expression in human prostate cancer tissues and cell lines. Pathol Int 2012; 62:84-92.
[17]  Li JY, Patterson M, Mikkola HK, Lowry WE, Kurdistani SK. Dynamic distribution of liner histone H1.5 in cellular differentiation. PLoS Genet 2012; 8:1-13.
[18]  Sjöblom T, Jones S, Wood LD, et al. The consensus coding sequences of human breast and colorectal cancers. Science 2006; 314:268-74.
[19]  Gaudin PB, Epstein JI. Adenosis of the prostate: histologic features in needle biopsy specimens. Am J Surg Pathol 1995; 19: 737-47.
[20]  Beach R, Gown AM, De Peralta-Venturina MN, et al. P504S immunohistochemical detection in 405 prostatic specimens including 376 18-gauge needle biopsies. Am J Surg Pathol 2002; 26: 1588-96.
[21]  Jiang Z, Woda BA, Rock KL, et al. P504S: a new molecular marker for the detection of prostate carcinoma. Am J Surg Pathol 2001; 25:1397-404.
[22]  Amin MB, Schultz DS, Zarbo RJ. Analysis of cribriform morphology in prostatic neoplasia using antibody to high–molecular weight cytokeratins. Arch Pathol Lab Med 1994; 118:260-4.
[23]  Rubin MA, Zhou M, Dhanasekaran SM, et al. α-Methylacyl coenzyme A racemase as a tissue biomarker for prostate cancer. JAMA 2002; 287:1662-70.
[24]  Sung MT, Jiang Z, Montironi R, MacLennan GT, Mazzucchelli R, Cheng L. alpha-Methyl acyl-CoA racemase (P504S)/34ßE12/p63 triple cocktail stain in prostatic adenocarcinoma after hormonal therapy. Human Pathol 2007;38:332-41.