Journal of Histochemistry and Cytochemistry Impact Factor & Information

Publisher: Histochemical Society, Histochemical Society

Journal description

Journal of Histochemistry & Cytochemistry (JHC) has been a pre-eminent cell biology journal for over 50 years. Published monthly, JHC offers primary research articles, timely reviews, editorials, and perspectives on the structure and function of cells, tissues, and organs, as well as mechanisms of development, differentiation, and disease. JHC also publishes new developments in microscopy and imaging, especially where imaging techniques complement current genetic, molecular and biochemical investigations of cell and tissue function. JHC offers generous space for articles and recognizing the value of images that reveal molecular, cellular and tissue organization, offers free color to all authors.

Current impact factor: 1.96

Impact Factor Rankings

2015 Impact Factor Available summer 2016
2014 Impact Factor 1.959
2013 Impact Factor 2.403
2012 Impact Factor 2.255
2011 Impact Factor 2.725
2010 Impact Factor 2.381
2009 Impact Factor 2.372
2008 Impact Factor 2.823
2006 Impact Factor 2.449
2005 Impact Factor 2.208
2004 Impact Factor 2.513
2003 Impact Factor 2.408
2002 Impact Factor 2.283
2001 Impact Factor 2.718
2000 Impact Factor 2.61
1999 Impact Factor 2.675
1998 Impact Factor 2.536
1997 Impact Factor 2.776

Impact factor over time

Impact factor

Additional details

5-year impact 2.59
Cited half-life >10.0
Immediacy index 0.32
Eigenfactor 0.01
Article influence 0.81
Website Journal of Histochemistry and Cytochemistry website
Other titles The journal of histochemistry and cytochemistry, Journal of histochemistry & cytochemistry
ISSN 0022-1554
OCLC 1800247
Material type Periodical, Internet resource
Document type Journal / Magazine / Newspaper, Internet Resource

Publisher details

Histochemical Society

  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author cannot archive a post-print version
  • Restrictions
    • 12 months embargo
  • Conditions
    • On any repository or website
    • Post-print on non-commercial site
    • Publisher's version/PDF cannot be used
  • Classification

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: Fas-mediated induction of apoptosis is a major factor in the selection of lymphocytes and downregulation of immunological processes. In the present study, we have assessed endothelial Fas-ligand (FasL) expression in normal human ileum, appendix, and colon, and compared the expression levels with that in inflammatory bowel disease and in acute appendicitis. In a normal appendix, endothelial FasL levels were constant in almost half of the mucosal vessels; but, in the normal ileum and colon, endothelial FasL was practically restricted to areas in close proximity to lymphatic follicles, and was expressed mainly in the submucosal aspect of the follicles in the vessels with high endothelium. In samples from subjects with either Crohn’s disease or ulcerative colitis, the extent of endothelial FasL expression was elevated in the submucosa and associated with an elevated number of lymphoid follicles. In inflammatory bowel disease, ulcers and areas with a high density of mononuclear cells expressing FasL also showed an elevated density of blood vessels with endothelial FasL expression. Although the function of endothelial FasL remains unclear, such a specific expression pattern suggests that endothelial FasL expression has a role in the regulation of lymphocyte access to the peripheral lymphoid tissues, including the intestinal mucosa.
    Journal of Histochemistry and Cytochemistry 09/2015; DOI:10.1369/0022155415608917
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    ABSTRACT: Primary normal human bronchial/tracheal epithelial (NHBE) cells, derived from the distal-most aspect of the trachea at the bifurcation, have been used for a number of studies in respiratory disease research. Differences between the source tissue and the differentiated primary cells may impact infection studies based on this model. Therefore, we examined how well-differentiated NHBE cells compared with their source tissue, the human distal trachea, as well as the ramifications of these differences on influenza A viral pathogenesis research using this model. We employed a histological analysis including morphological measurements, electron microscopy, multi-label immunofluorescence confocal microscopy, lectin histochemistry, and microarray expression analysis to compare differentiated NHBEs to human distal tracheal epithelium. Pseudostratified epithelial height, cell type variety and distribution varied significantly. Electron microscopy confirmed differences in cellular attachment and paracellular junctions. Influenza receptor lectin histochemistry revealed that α2,3 sialic acids were rarely present on the apical aspect of the differentiated NHBE cells, but were present in low numbers in the distal trachea. We bound fluorochrome bioconjugated virus to respiratory tissue and NHBE cells and infected NHBE cells with human influenza A viruses. Both indicated that the pattern of infection progression in these cells correlated with autopsy studies of fatal cases from the 2009 pandemic.
    Journal of Histochemistry and Cytochemistry 01/2015; 63(5). DOI:10.1369/0022155415570968
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    ABSTRACT: To determine whether vascular endothelial growth factor-C (VEGF-C) and its receptor (VEGFR-3) are involved in the glial reaction elicited by transplanted mesenchymal stem cells (MSCs), we examined the cellular localization of VEGF-C and VEGFR-3 proteins in the striatum of adult normal rats that received bone marrow-derived human MSCs. The MSC grafts were infiltrated with activated microglia/macrophages and astrocytes over a 2-week period post-transplantation, which appeared to parallel the loss of transplanted MSCs. VEGF-C/VEGFR-3 was expressed in activated microglia/macrophages recruited to the graft site, where the induction of VEGF-C protein was rather late compared with that of its receptor. VEGF-C protein was absent or very weak on day 3, whereas VEGFR-3 immunoreactivity was evident within the first three days. Furthermore, within three days, VEGF-C could be detected in the brain macrophages localized immediately adjacent to the needle track. At the same time, almost all the brain macrophages in both regions expressed VEGFR-3. Reactive astrocytes at the graft site expressed VEGFR-3, but not VEGF-C. These data demonstrated the characteristic time- and cell-dependent expression patterns for VEGF-C and VEGFR-3 within the engrafted brain tissue, suggesting that they may contribute to neuroinflammation in MSC transplantation, possibly through the recruitment and/or activation of microglia/macrophages and astrogliosis. © The Author(s) 2014.
    Journal of Histochemistry and Cytochemistry 12/2014; DOI:10.1369/0022155414564218
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    ABSTRACT: The removal of excess cytoplasm from elongated spermatids by Sertoli cells is the last essential step in spermatogenesis. It must require the cell-to-cell recognition between Sertoli cell and elongating spermatid through protein-protein interaction. CEACAM2-L, an adhesion molecule of the immunoglobulin superfamily (IgSF), is present at the plasma membrane covering the excess cytoplasm of elongated spermatids, which might be involved in the cell-to-cell recognition. In this study, we investigated the interaction between CEACAM2-L and Poliovirus receptor (PVR) that is one of IgSFs expressed in Sertoli cells. Immunohistochemical analysis showed that CEACAM2-L expressed on elongated spermatids was in close contact with PVR-positive cell processes of Sertoli cells. Immunoprecipitation experiments both in vivo and in vitro demonstrated direct heterophilic interaction between CEACAM2-L and PVR. N-terminal Ig domain of CEACAM2-L was critical for the interaction with PVR. In addition, we found that CEACAM2-L formed heterophilic trans-tetramers with PVR in transfected COS7 cells. From these data, we proposed that Sertoli cells recognize the excess cytoplasm of elongated spermatids through the PVR-CEACAM2-L interaction in mouse testis. Keywords: CEACAM2, PVR, Sertoli cells, phagocytosis, spermatids, spermatogenesis
    Journal of Histochemistry and Cytochemistry 06/2014;
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    ABSTRACT: Human hepatocellular carcinoma (HCC) is the fifth most common cancer in the world. Currently, surgical resection is the only effective treatment for HCC if the tumor is resectable. Small molecule, biologics and siRNA anti-cancer drugs have been explored for the treatment of HCC. Selective targeting to tumor tissue rather than normal liver in HCC patients is still a challenge. Galactosamine-mediated targeting delivery of anti-cancer drugs in the liver has been tested because its receptor, asialoglycoprotein receptor 1 (ASGPR1), is expressed in the liver and not in other human tissues. We examined ASGPR1 expression levels by immunohistochemistry in HCC with different grades. Guidance for a targeting delivery strategy for anti-cancer drugs to HCC is suggested in this report.
    Journal of Histochemistry and Cytochemistry 11/2013; 61(12):901-909. DOI:10.1369/0022155413503662
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    ABSTRACT: Reticular cells and follicular dendritic cells (FDCs) build up a framework that underlies the compartmentalization of spleens and lymph nodes. Subpopulations of reticular cells express the smooth-muscle isoform of actin, indicative of a specialized contractile apparatus. We have investigated the distribution of the actin-binding protein caldesmon in spleen and lymph nodes of mice and rats. Caldesmon modulates contraction and regulates cell motility. Alternative splicing of transcripts from a single gene results in high-molecular-mass isoforms (h-caldesmon) that are predominately expressed by smooth-muscle cells (SMCs), and low-molecular-mass isoforms (l-caldesmon) that are thought to be widely distributed in non-muscle tissues, but the distribution of caldesmon in spleen and lymph nodes has not been reported. We have performed Western blot analysis and immunohistochemistry using four different antibodies against caldesmon, among these a newly developed polyclonal antibody directed against recombinant mouse caldesmon. Western blot analysis showed the preponderance of l-caldesmon in spleen and lymph nodes. Our results from immunohistochemistry demonstrate caldesmon in SMCs, as expected, but also in reticular cells and FDCs, and suggest that the isoform highly expressed by reticular cells is l-caldesmon. In spleen of SCID mice, caldesmon was expressed by reticular cells in the absence of lymphocytes. (J Histochem Cytochem 58:183-193, 2010).
    Journal of Histochemistry and Cytochemistry 11/2009; 58(2):183-93. DOI:10.1369/jhc.2009.954651