Biotin-Containing Intranuclear Inclusions in Endometrial Glands During Gestation and Puerperium

Yokoyama, Shigeo; Kashima, Kenji; Inoue, Souichi; Daa, Tsutomu; Nakayama, Iwao; Moriuchi, Akira

doi:10.1093/ajcp/99.1.13

Cited by 73 publications

(30 citation statements)

References 7 publications

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“…With respect to intracellular distribution, biotin is restricted predominantly to the mitochondria and cytosol. Aberrant nuclear accumulation of biotin was demonstrated in the present as well as in several recent studies [20][21][22][23][24][25][26][27] . Furthermore, two mitochondrial biotin-binding enzymes (PAC and PCC) were also found in the intranuclear inclusions of morules, and always coexisted with biotin.…”

Section: Discussionsupporting

confidence: 81%

Immunohistochemical Analysis of Morules in Colonic Neoplasms: Morules Are Morphologically and Qualitatively Different from Squamous Metaplasia

Ueo¹,

Kashima²,

Daa³

et al. 2005

Pathobiology

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Morules develop in several neoplasms and have been considered as a type of squamous metaplasia despite the absence of keratinization and intercellular bridges. The objective of this study was to clarify the pathological significance of morules and to distinguish morules from squamous metaplasia in colonic neoplasms. Ten cases of morule-associated colonic neoplasms (4 adenocarcinomas, 1 adenoma with carcinoma in situ, and 5 adenomas), and 3 cases of squamous metaplasia in colonic adenocarcinoma were examined morphologically and immunohistochemically. Morules were well-defined structures composed of small, oval to short-spindled cells with bland nuclei, and frequently associated with intranuclear inclusions that were positive for biotin and biotin-binding enzymes (pyruvic acid carboxylase and propionyl CoA carboxylase). On immunohistochemical examination, morules characteristically showed nuclear overexpression of β-catenin, cyclin D1 and p63, low Ki-67 labeling index (<1%), cytoplasmic overexpression of CD10, and no expression of cytokeratin 20. These molecules were useful for the differentiation of morules. Furthermore, p63 and 34βE12 positivities in morules suggested that they have a basal/stem cell phenotype. Thus, morules were morphologically and qualitatively different from squamous metaplasia. We consider that morules in colonic neoplasms are cell clusters with a basal/stem cell phenotype, and have less proliferative and less invasive potential than other cancer cells.

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Section: Discussionsupporting

confidence: 81%

Immunohistochemical Analysis of Morules in Colonic Neoplasms: Morules Are Morphologically and Qualitatively Different from Squamous Metaplasia

Ueo¹,

Kashima²,

Daa³

et al. 2005

Pathobiology

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“…56,187,239,257,275 EABA is typically in the cytoplasm but has been reported in the nucleus. 250,257,342,428 Commercially available EABA blocking reagents (pure avidin and biotin solutions) are expensive, so many laboratories use ''homemade'' solutions with egg white as a source of avidin and 5% powdered milk as a source of biotin. 12,84,175,239,285,418 Non-Avidin-Biotin Methods Peroxidase-Antiperoxidase (PAP) Method.…”

Section: Detection Systems: the Sensitivity Issuementioning

confidence: 99%

When Tissue Antigens and Antibodies Get Along

2013

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Once focused mainly on the characterization of neoplasms, immunohistochemistry (IHC) today is used in the investigation of a broad range of disease processes with applications in diagnosis, prognostication, therapeutic decisions to tailor treatment to an individual patient, and investigations into the pathogenesis of disease. This review addresses the technical aspects of immunohistochemistry (and, to a lesser extent, immunocytochemistry) with attention to the antigen-antibody reaction, optimal fixation techniques, tissue processing considerations, antigen retrieval methods, detection systems, selection and use of an autostainer, standardization and validation of IHC tests, preparation of proper tissue and reagent controls, tissue microarrays and other high-throughput systems, quality assurance/quality control measures, interpretation of the IHC reaction, and reporting of results. It is now more important than ever, with these sophisticated applications, to standardize the entire IHC process from tissue collection through interpretation and reporting to minimize variability among laboratories and to facilitate quantification and interlaboratory comparison of IHC results.

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“…4 In mammals, biotin reutilization occurs through the action of biotinidase, an enzyme which hydrolyzes biotin from biotinyl-lysine (biocytin) or short peptides containing biotin which are the products of normal proteolytic digestion of holocarboxylases. 8 In recent years, biotin has been described in the nucleus of cells, 9 including in tumor material [10][11][12] .…”

Section: Introductionmentioning

confidence: 99%

Nonenzymatic biotinylation of histone H2A

et al. 2009

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Holocarboxylase synthetase (HCS, eukaryotic enzyme) and BirA (prokaryotic) are biotin protein ligases that catalyze the ATP-dependent attachment of biotin to apocarboxylases via the reactive intermediate, bio-5 0 -AMP. In this study, we examined the in vitro mechanism of biotin attachment to histone H2A in the presence of HCS and BirA. The experiment derives from our observations that HCS is found in the nucleus of cells in addition to the cytoplasm, and it has the ability to attach biotin to histones in vitro (Narang et al., Hum Mol Genet 2004; 13:15-23). Using recombinant HCS or BirA, the rate of biotin attachment was considerably slower with histone H2A than with the biotin binding domain of an apocarboxylase. However, on incubation of recombinant H2A with chemically synthesized bio-5 0 -AMP, H2A was observed to be rapidly labeled with biotin in the absence of enzyme. Nonenzymatic biotinylation of a truncated apocarboxylase (BCCP87) has been previously reported (Streaker and Beckett, Protein Sci 2006; 15:1928-1935), though at a much slower rate than we observe for H2A. The specific attachment sites of nonenzymatically biotinylated recombinant H2A at different time points were identified using mass spectrometry, and were found to consist of a similar pattern of biotin attachment as seen in the presence of HCS, with preference for lysines in the highly basic N-terminal region of the histone. None of the lysine sites within H2A resembles the biotin attachment consensus sequence seen in carboxylases, suggesting a novel mechanism for histone biotinylation.

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Biotin-Containing Intranuclear Inclusions in Endometrial Glands During Gestation and Puerperium

Cited by 73 publications

References 7 publications

Immunohistochemical Analysis of Morules in Colonic Neoplasms: Morules Are Morphologically and Qualitatively Different from Squamous Metaplasia

Immunohistochemical Analysis of Morules in Colonic Neoplasms: Morules Are Morphologically and Qualitatively Different from Squamous Metaplasia

When Tissue Antigens and Antibodies Get Along

Nonenzymatic biotinylation of histone H2A

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