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ACTA HISTOCHEMICA ET CYTOCHEMICA
- Vol.49(2016)
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Predecessor

Proceedings of the Japanese Histochemical Association

ACTA HISTOCHEMICA ET CYTOCHEMICA Vol. 49(2016) No. 4

REGULAR ARTICLE

Visualization of Neutrophil Extracellular Traps and Fibrin Meshwork in Human Fibrinopurulent Inflammatory Lesions: I. Light Microscopic Study

Kazuya Shiogama, Takanori Onouchi, Yasuyoshi Mizutani, Kouhei Sakurai, Ken-ichi Inada, Yutaka Tsutsumi

Released: August 30, 2016

[Advance Publication] Released: July 30, 2016

p.109-116

Neutrophil extracellular traps (NETs) are extracellular fibrillary structures composed of degraded chromatin and granules of neutrophil origin. In fibrinopurulent inflammation such as pneumonia and abscess, deposition of fibrillar eosinophilic material is a common histopathological finding under hematoxylin-eosin staining. Expectedly, not only fibrin fibrils but also NETs consist of the fibrillar material. The aim of the present study is to analyze immunohistochemically how NETs are involved in the inflammatory process. Archival formalin-fixed, paraffin-embedded sections accompanying marked neutrophilic infiltration were the target of analysis. Neutrophil-associated substances (citrullinated histone H3, lactoferrin, myeloperoxidase and neutrophil elastase) were evaluated as NETs markers, while fibrinogen gamma chain was employed as a fibrin marker. Light microscopically, the fibrils were categorized into three types: thin, thick and clustered thick. Lactoferrin represented a good and stable NETs marker. Thin fibrils belonged to NETs. Thick fibrils are composed of either mixed NETs and fibrin or fibrin alone. Clustered thick fibrils were solely composed of fibrin. Neutrophils were entrapped within the fibrilllar meshwork of the thin and thick types. Apoptotic cells immunoreactive to cleaved caspase 3 and cleaved actin were dispersed in the NETs. In conclusion, NETs and fibrin meshwork were consistently recognizable by immunostaining for lactoferrin and fibrinogen gamma chain.

Visualization of Neutrophil Extracellular Traps and Fibrin Meshwork in Human Fibrinopurulent Inflammatory Lesions: II. Ultrastructural Study

Takanori Onouchi, Kazuya Shiogama, Takahiro Matsui, Yasuyoshi Mizutani, Kouhei Sakurai, Ken-ichi Inada, Yutaka Tsutsumi

Released: August 30, 2016

[Advance Publication] Released: July 30, 2016

p.117-123

Neutrophil extracellular traps (NETs) represent an extracellular, spider’s web-like structure resulting from cell death of neutrophils. NETs play an important role in innate immunity against microbial infection, but their roles in human pathological processes remain largely unknown. NETs and fibrin meshwork both showing fibrillar structures are observed at the site of fibrinopurulent inflammation, as described in our sister paper [Acta Histochem. Cytochem. 49; 109–116, 2016]. In the present study, immunoelectron microscopic study was performed for visualizing NETs and fibrin fibrils (thick fibrils in our tongue) in formalin-fixed, paraffin-embedded sections of autopsied lung tissue of legionnaire’s pneumonia. Lactoferrin and fibrinogen gamma chain were utilized as markers of NETs and fibrin, respectively. Analysis of immuno-scanning electron microscopy indicated that NETs constructed thin fibrils and granular materials were attached onto the NETs fibrils. The smooth-surfaced fibrin fibrils were much thicker than the NETs fibrils. Pre-embedding immunoelectron microscopy demonstrated that lactoferrin immunoreactivities were visible as dots on the fibrils, whereas fibrinogen gamma chain immunoreactivities were homogeneously observed throughout the fibrils. Usefulness of immunoelectron microscopic analysis of NETs and fibrin fibrils should be emphasized.

p62 Regulates the Proliferation of Molecular Apocrine Breast Cancer Cells

Fumi Nozaki, Yukari Hirotani, Yoko Nakanishi, Hiromi Yamaguchi, Haruna Nishimaki, Hiroko Noda, Xiaoyan Tang, Hisae Yamamoto, Atsuko Suzuki, Toshimi Seki, Shinobu Masuda

Released: August 30, 2016

[Advance Publication] Released: August 03, 2016

p.125-130

p62, also called sequestosome 1 (SQSTM1), is a multifunctional signaling molecule that affects cell proliferation. Recently, we found accumulation of p62 in apocrine carcinoma of the breast, however, the biological role of p62 expression in apocrine carcinoma still remains unclear. To investigate whether p62 might contribute to tumor cell proliferation in apocrine carcinomas, we used the MDA-MB-453 (androgen receptor-positive, HER2-type) and MFM223 (androgen receptor-positive, triple-negative type) breast cancer cell lines as models of molecular apocrine carcinoma. Both MDA-MB-453 and MFM223 showed strong and d high p62 protein expression than MCF7 cells (androgen receptor-negative, luminal A type). Knockdown of p62 resulted in significant reduction of the cell proliferative activity in both MDA-MB-453 (P<0.01) and MFM223 (P<0.05). In conclusion, p62 could contribute to cell proliferation and represent a therapeutic target in apocrine carcinoma.

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Volume And Issue List
ACTA HISTOCHEMICA ET CYTOCHEMICA

Predecessor

ACTA HISTOCHEMICA ET CYTOCHEMICA Vol. 49(2016) No. 4

REGULAR ARTICLE

Visualization of Neutrophil Extracellular Traps and Fibrin Meshwork in Human Fibrinopurulent Inflammatory Lesions: I. Light Microscopic Study

Visualization of Neutrophil Extracellular Traps and Fibrin Meshwork in Human Fibrinopurulent Inflammatory Lesions: II. Ultrastructural Study

p62 Regulates the Proliferation of Molecular Apocrine Breast Cancer Cells

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Volume And Issue List ACTA HISTOCHEMICA ET CYTOCHEMICA

Predecessor

ACTA HISTOCHEMICA ET CYTOCHEMICA Vol. 49(2016) No. 4

REGULAR ARTICLE

Visualization of Neutrophil Extracellular Traps and Fibrin Meshwork in Human Fibrinopurulent Inflammatory Lesions: I. Light Microscopic Study

Visualization of Neutrophil Extracellular Traps and Fibrin Meshwork in Human Fibrinopurulent Inflammatory Lesions: II. Ultrastructural Study

p62 Regulates the Proliferation of Molecular Apocrine Breast Cancer Cells

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Announcement From J-STAGE

Journal Tools

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Volume And Issue List
ACTA HISTOCHEMICA ET CYTOCHEMICA