Ki67/KIT double immunohistochemical staining in cutaneous mast cell tumors from Boxer dogs

Fonseca-Alves, Carlos Eduardo; Bento, Daniel Diola; Torres-Neto, Rafael; Werner, Juliana; Kitchell, Barbara E.; Amorim, Renée Laufer

doi:10.1016/j.rvsc.2015.08.007

Cited by 22 publications

(28 citation statements)

References 26 publications

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“…Pattern III immunostaining was not observed in the present study. The vast majority of low grade neoplasms presented immunostaining pattern II, corroborating with the literature (Webster et al 2007, Fonseca-Alves et al 2015, Flores et al 2016, Sledge et al 2016. This information is important considering that it has been observed that MCTs that lose membrane expression and acquire cytoplasmic expression for KIT antigen, present a more aggressive biological behavior (Kiupel et al 2004).…”

Section: Discussionsupporting

confidence: 83%

“…Alves & Roman (2005) reported decreased positive immunostaining to proliferating cell nuclear antigen (PCNA) in tonsil samples, using the biotinylated system, in cases with formalin fixation longer than 24 hours. Other authors have found values of 43% (Fonseca- Alves et al 2015) and 23% (Kandefer-Gola et al 2015) failure in immunostaining for Ki67 protein in MCTs, and did not explain the reasons for such failures. According to Munakata & Hendricks (1993), the best results for Ki67 antigen were observed in tonsil samples after 4 hours of formalin fixation, with weak immunostaining in samples after 48 hours of fixation.…”

Section: Discussionmentioning

confidence: 86%

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Use of different fixation times and application of two immunohistochemical methods for detection of KIT and Ki67 proteins in canine cutaneous mast cell tumors

et al. 2019

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Due to the high prevalence of mast cell tumors (MCTs) in the diagnostic routine, several factors, especially prognostic, have been sought to determine the biological behavior of these neoplasms. Immunohistochemistry (IHC) is one of the main tools utilized to biologically differentiate more aggressive tumors from less aggressive ones. However, some immunostainings are influenced by formalin fixation, interfering with the results. This is both a retrospective and prospective study of MCTs diagnosed in laboratory routine. A total of 25 samples, without knowledge about fixation time, were analyzed in the retrospective study, whereas 12 samples, with known fixation times, were assessed in the prospective study. Two histologic grading systems (Patnaik and Kiupel), special staining of toluidine blue, and IHC for KIT and Ki67 proteins were applied in both studies. Additionally, two amplification systems (biotinylated and non-biotinylated) for Ki67 protein and counting of the argyrophilic nucleolar organizing regions (AgNOR method) were tested in the prospective study. In the retrospective study, greater agreement between the evaluating pathologists was observed when the Kiupel system was used. IHC staining for KIT protein was effective in both studies, regardless of fixation time. IHC staining for Ki67 protein was highly sensitive to formaldehyde, and staining failure was observed in 56% of the cases in the retrospective study. In the prospective study, samples fixed for longer than 24 hours showed a reduction in the number of stained cells (altering the determination of the cell growth fraction) or showed absence of IHC staining in both amplification systems. The use of the AgNOR method to evaluate the rate of cell proliferation may be an alternative when the fixation time of the neoplasm is unknown or longer than 24 hours.

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Section: Discussionsupporting

confidence: 83%

Section: Discussionmentioning

confidence: 86%

Use of different fixation times and application of two immunohistochemical methods for detection of KIT and Ki67 proteins in canine cutaneous mast cell tumors

et al. 2019

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“…The P130 and P107 proteins have considerable sequence homology compared with Rb [45–47], and are regulated by G1 cyclin-dependent kinases [48]. Ki67 is a proliferation indicator [49] that determines the risk of distant tumor recurrence [50]. …”

Section: Discussionmentioning

confidence: 99%

Aurora kinase A revives dormant laryngeal squamous cell carcinoma cells via FAK/PI3K/Akt pathway activation

Yang

He²,

Chen³

et al. 2016

Oncotarget

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Revival of dormant tumor cells may be an important tumor metastasis mechanism. We hypothesized that aurora kinase A (AURKA), a cell cycle control kinase, promotes the transition of laryngeal squamous cell carcinoma (LSCC) cells from G0 phase to active division. We therefore investigated whether AURKA could revive dormant tumor cells to promote metastasis. Western blotting revealed that AURKA expression was persistently low in dormant laryngeal cancer Hep2 (D-Hep2) cells and high in non-dormant (T-Hep2) cells. Decreasing AURKA expression in T-Hep2 cells induced dormancy and reduced FAK/PI3K/Akt pathway activity. Increasing AURKA expression in D-Hep2 cells increased FAK/PI3K/Akt pathway activity and enhanced cellular proliferation, migration, invasion and metastasis. In addition, FAK/PI3K/Akt pathway inhibition caused dormancy-like behavior and reduced cellular mobility, migration and invasion. We conclude that AURKA may revive dormant tumor cells via FAK/PI3K/Akt pathway activation, thereby promoting migration and invasion in laryngeal cancer. AURKA/FAK/PI3K/Akt inhibitors may thus represent potential targets for clinical LSCC treatment.

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“…Outro marcador molecular muito utilizado nestes tumores é o gene c-Kit, que codifica a proteína do receptor de tirosina quinase KIT (YARDEN et al, 1987 WEBSTER et al, 2006;TAKEUCHI et al, 2013), e ambas foram correlacionadas com o pior prognóstico da doença. Mutações do tipo duplicação interna em tandem (DIT) no éxon 11 do gene c-Kit podem estar presentes entre 20 a 30% dos MCTs em cães (WEBSTER et al, 2006;LETARD et al, 2008 KIUPEL et al, 2004;MORINI;WEBSTER et al, 2007;MAGLENNON et al, 2008;GIANTIN et al, 2012a;BERLATO et al, 2015;COSTA CASAGRANDE et al, 2015;FONSECA-ALVES et al, 2015 GINN et al, 2000;JAFFE et al, 2000;PALTRINIERI, 2004;SCASE et al, 2006;PATRUNO et al, 2009;GIANTIN et al, 2012b;PRADA et al, 2012;STREFEZZI et al, 2012;VASCELLARI et al, 2013 (BRODEY, 1970;FINNIE;BOSTOCK, 1979;BOSTOCK, 1986;ROTHWELL et al, 1987;LONDON;SEGUIN, 2003) e com prevalência de 0,27% na população canina (SHOOP et al, 2015 (BOSTOCK, 1986;ROTHWELL et al, 1987;KIUPEL et al, 2005;WHITE et al, 2011;DOBSON, 2013;SHOOP et al, 2015).…”

Section: Introdução Geralunclassified

<b>Valor prognóstico de marcadores imunohistoquímicos em mastocitomas cutâneos caninos</b>

Freytag¹

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Ki67/KIT double immunohistochemical staining in cutaneous mast cell tumors from Boxer dogs

Cited by 22 publications

References 26 publications

Use of different fixation times and application of two immunohistochemical methods for detection of KIT and Ki67 proteins in canine cutaneous mast cell tumors

Use of different fixation times and application of two immunohistochemical methods for detection of KIT and Ki67 proteins in canine cutaneous mast cell tumors

Aurora kinase A revives dormant laryngeal squamous cell carcinoma cells via FAK/PI3K/Akt pathway activation

<b>Valor prognóstico de marcadores imunohistoquímicos em mastocitomas cutâneos caninos</b>

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