Assignment of the human kinectin gene (KTN1), encoding a kinesin-binding protein, to chromosome 14 band q22.1 by in situ hybridization

1997 ◽  
Vol 79 (3-4) ◽  
pp. 196-197
Author(s):  
P.N. Rao ◽  
H. Yu ◽  
R. Hodge ◽  
M.J. Pettenati ◽  
M.P. Sheetz
Keyword(s):  
In Situ Hybridization ◽  
Binding Protein ◽  
Chromosome 14

scholarly journals In situ detection of vitamin D-induced calcium-binding protein (9-kDa CaBP) messenger RNA in rat duodenum.

1986 ◽  
Vol 34 (2) ◽  
pp. 277-280 ◽  
Author(s):  
M Warembourg ◽  
O Tranchant ◽  
C Perret ◽  
C Desplan ◽  
M Thomasset
Keyword(s):  
Vitamin D ◽  
In Situ Hybridization ◽  
Calcium Binding ◽  
Binding Protein ◽  
Cdna Probe ◽  
Calcium Binding Protein ◽  
Pbr322 Dna ◽  
Rat Duodenum ◽  
Columnar Cells

We have previously described the molecular cloning of a cDNA fragment synthesized from rat duodenal mRNA coding for a 9000-dalton vitamin D-induced calcium-binding protein (9-kDa CaBP) (3). We now report the use of this cloned cDNA to study the cytological distribution of 9-kDa CaBP mRNA in rat duodenum by in situ hybridization. Tissue sections, fixed in ethanol:acetic acid, were hybridized to the 3H-cDNA probe and processed for autoradiography. The specificity of the CaBP mRNA-DNA hybrid formation was checked using 3H-labeled plasmid pBR322 DNA as a control probe. 9k-Da CaBP mRNA, visualized by silver grains, was found only in the absorptive epithelial cells, and the concentration was greater in the cells at the villous tips than in those of the crypts. The 9k-Da CaBP mRNA was observed mainly in the cytoplasm of the columnar cells and less frequently in the nucleus. Labeling was not seen in the brush border and goblet cells. The submucosa, with Brunner's glands and muscularis, also showed no specific 9-kDa CaBP mRNA concentration. This demonstration of 9-kDa CaBP gene activity in the columnar cells of the rat duodenum illustrates the usefulness of in situ hybridization for characterization of specific cells involved in the expression of 1,25(OH)2 D3 activity.

scholarly journals In situ hybridization histochemistry of Spot 35 protein, a calcium-binding protein, in the rat brain

1991 ◽  
Vol 15 (3) ◽  
pp. 207-216 ◽  
Author(s):  
Hiroshi Usui ◽  
Takashi Katagiri ◽  
Yasuji Yoshida ◽  
Akiko Nishiyama ◽  
Tomio Ichikawa ◽  
...  
Keyword(s):  
In Situ Hybridization ◽  
Rat Brain ◽  
Calcium Binding ◽  
Binding Protein ◽  
Protein A ◽  
Calcium Binding Protein ◽  
Hybridization Histochemistry ◽  
In Situ Hybridization Histochemistry

Mapping of rat prostatic binding protein genes C1, C2, and C3 to rat chromosome 5 by in situ hybridization

1988 ◽  
Vol 48 (2) ◽  
pp. 121-123 ◽  
Author(s):  
J. Zhang ◽  
L. Dirckx ◽  
P. Marynen ◽  
W. Rombauts ◽  
B. Delaey ◽  
...  
Keyword(s):  
In Situ Hybridization ◽  
Binding Protein ◽  
Chromosome 5

scholarly journals Significance of p53-Binding Protein 1 Nuclear Foci in Cervical Squamous Intraepithelial Lesions: Association With High-Risk Human Papillomavirus Infection and P16INK4a Expression

2020 ◽  
Vol 27 (1) ◽  
pp. 107327481990117
Author(s):  
Sayaka Kawashita ◽  
Katsuya Matsuda ◽  
Hisayoshi Kondo ◽  
Yuriko Kitajima ◽  
Yuri Hasegawa ◽  
...  
Keyword(s):  
In Situ Hybridization ◽  
Human Papillomavirus ◽  
High Risk ◽  
Binding Protein ◽  
Histological Grade ◽  
Neoplastic Progression ◽  
Cervical Lesions ◽  
Nuclear Foci ◽  
The Impact

As p53-binding protein 1 (53BP1) localizes to the sites of DNA double-strand breaks and rapidly forms nuclear foci (NF), and its presence may be an indicator of endogenous genomic instability (GIN). We previously showed that 53BP1 NF in cervical cells increase with neoplastic progression, indicating the significance of 53BP1 expression for the estimation of malignant potential during cervical carcinogenesis. This study aimed to further elucidate the impact of 53BP1 expression as a biomarker for cervical squamous intraepithelial lesion (SIL). A total of 81 tissue samples, including 17 of normal cervical epithelium, 22 of cervical intraepithelial neoplasia (CIN) 1, 21 of CIN2, and 21 of CIN3, from patients positive for high-risk human papillomavirus (HR-HPV) were used for double-label immunofluorescence of 53BP1 and Ki-67/p16INK4a expression and HR-HPV in situ hybridization. We analyzed associations between 53BP1 expression type with parameters such as CIN grade, HR-HPV infection status, p16INK4a expression, and CIN prognosis. Expression type of 53BP1 was significantly associated with histological grade of CIN and HR-HPV in situ hybridization signal pattern ( P < .0001). There was a significant correlation between 53BP1 and p16INK4a expression levels ( r = .73, P < .0001). However, there was no association between 53BP1 expression type and CIN prognosis. We propose that 53BP1 expression type is a valuable biomarker for SIL, which can help estimate the grade and GIN of cervical lesions reflecting replication stress caused by the integration of HR-HPV to the host genome.

scholarly journals Detection of interphotoreceptor retinoid binding protein (IRBP) mRNA in human and cone-dominant squirrel retinas by in situ hybridization.

1991 ◽  
Vol 39 (2) ◽  
pp. 171-176 ◽  
Author(s):  
K Porrello ◽  
S P Bhat ◽  
D Bok
Keyword(s):  
In Situ Hybridization ◽  
Ground Squirrel ◽  
Binding Protein ◽  
Pigment Epithelium ◽  
Specific Cell ◽  
Human Retina ◽  
Cell Type ◽  
Rods And Cones ◽  
Interphotoreceptor Retinoid Binding Protein

Interphotoreceptor retinoid binding protein (IRBP) is a soluble glycolipoprotein located between the neurosensory retina and pigment epithelium, which may serve to transport vitamin A derivatives between these tissues. The specific cell type responsible for IRBP synthesis has not been well established. To address this issue, we have examined the expression of IRBP mRNA in human and cone-dominant ground squirrel retinas by in situ hybridization. Optimal labeling and histological resolution were achieved with 35S- and 3H-labeled anti-sense riboprobes made from a human IRBP cDNA clone, and semi-thin wax-embedded retinal sections. In human retina, label was localized over the inner segments of both rod and cone photoreceptors. Quantitative analysis demonstrated a fourfold higher density of label over rod inner segments. In ground squirrel retina, labeling was found almost exclusively over the inner segments of cones. The results indicate that in human retina both rods and cones express IRBP mRNA, albeit at different levels. In cone-dominant species such as the ground squirrel, cones are the principal cell type responsible for IRBP mRNA synthesis.

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