Journal of Histochemistry and Cytochemistry (J HISTOCHEM CYTOCHEM)

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: 2.40

Impact Factor Rankings

2015 Impact Factor Available summer 2015
2013 / 2014 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 2.53
Cited half-life 0.00
Immediacy index 0.56
Eigenfactor 0.01
Article influence 0.80
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
    ​ yellow

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: MLL (mixed-lineage-leukemia gene) rearrangements are typical for acute leukemia and are associated with an aggressive course of disease, with a worse outcome than comparable case, and thus require intensified treatment. Here we describe a 69-year-old female with adult B-cell precursor acute lymphoblastic leukemia (BCPALL) with hyperleukocytosis and immunopheotype CD10- and CD19+ with cryptic MLL-rearrangements. G-banding showed at the time of diagnosis a normal karyotype 46,XX. Molecular cytogenetics using multitude multicolor banding (mMCB) revealed a complex rearrangement of both chromosomes 11. However, a locus specific probe additionally identified that the MLL gene at 11q23.3 was disrupted and the 5′ region was inserted into the chromosomal subband 4q21; thus the aberration involved 3 chromosomes and 5 break events. Unfortunately, the patient died six months after initial diagnosis from serious infections and severe complications. Overall the present findings confirm that by far not all MLL aberrations are seen by routine chromosome banding techniques and that fluorescence in situ hybridization (FISH) should be regarded as standard tool to access MLL rearrangements in patients with BCP-ALL.
    Journal of Histochemistry and Cytochemistry 02/2015;
  • Journal of Histochemistry and Cytochemistry 01/2015; DOI:10.1369/0022155415573323
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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; 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: Inosine-5-monophosphate dehydrogenase catalyzes the critical step in the de novo synthesis of guanosine nucleotides: the oxidation of inosine monophosphate to xanthosine monophosphate. This reaction can be inhibited by specific inhibitors, such as ribavirin or mycophenolic acid, which are widely used in clinical treatment when required to inhibit the proliferation of viruses or cells. However, it was recently found that such an inhibition affects the cells, leading to a redistribution of IMPDH2 and the appearance of IMPDH2 inclusions in the cytoplasm. According to their shape, these inclusions have been termed Rods and Rings (R&R). In this work, we focused on the subcellular localization of IMPDH2 protein and the ultrastructure of R&R inclusions. Using microscopy and western blot analysis, we show the presence of nuclear IMPDH2 in human cells. We also show that the nuclear pool has an ability to form Rod structures after inhibition by ribavirin. Concerning the ultrastructure, we observed that R&R inclusions in cellulo correspond to the accumulation of fibrous material that is not surrounded by a biological membrane. The individual fibers are composed of regularly repeating subunits with a length of approximately 11 nm. Together, our findings describe the localization of IMPDH2 inside the nucleus of human cells as well as the ultrastructure of R&R inclusions.
    Journal of Histochemistry and Cytochemistry 06/2014; DOI:10.1369/0022155414543853
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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;
  • Journal of Histochemistry and Cytochemistry 01/2012; 60:346-358.
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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
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    ABSTRACT: The pituitary gland dynamically changes its hormone output under various pathophysiological conditions. One of the pathways implicated in the regulatory mechanism of this gland is a dopaminergic system that operates the phosphoinositide (PI) cycle to transmit downstream signal through second messengers. We have previously shown that diacylglycerol kinase β (DGKβ) is coexpressed with dopamine D1 and D2 receptors in medium spiny neurons of the striatum, suggesting a plausible implication of DGKβ in dopaminergic transmission. However, it remains elusive whether DGKβ is involved in the dopaminergic system in the pituitary gland. The aim of this study is to investigate the expression and localization of DGK in the pituitary gland, together with the molecular components involved in the PI signaling cascade, including dopamine receptors, phospholipase C (PLC), and a major downstream molecule, protein kinase C (PKC). Here we show that DGKβ and the dopamine D2 receptor are coexpressed in the intermediate lobe and localize to the plasma membrane side by side. In addition, we reveal that PLCβ4 and PKCα are the subtypes expressed in the intermediate lobe among those families. These findings will substantiate and further extend our understanding of the molecular-anatomical pathway of PI signaling and the functional roles of DGK in the pituitary intermediate lobe. (J Histochem Cytochem 58:119-129, 2010).
    Journal of Histochemistry and Cytochemistry 10/2009; 58(2):119-29. DOI:10.1369/jhc.2009.954347