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Loss of Kindlin-1 drives a more aggressive phenotype in cutaneous squamous cell carcinoma

ABSTRACT: Loss of Kindlin-1 drives a more aggressive phenotype in cutaneous squamous cell carcinoma

PROVIDER: PRJNA992569 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25195454.fastq.gz	Fastqsanger.gz
	SRR25195455.fastq.gz	Fastqsanger.gz
	SRR25195456.fastq.gz	Fastqsanger.gz
	SRR25195457.fastq.gz	Fastqsanger.gz
	SRR25195458.fastq.gz	Fastqsanger.gz

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Loss of Kindlin-1 drives a more aggressive phenotype in cutaneous squamous cell carcinoma

Project description:Kindler syndrome (KS) is a rare genodermatosis resulting from loss-of-function mutations in FERMT1, the gene that encodes Kindlin-1. KS patients have a high propensity to develop aggressive and metastatic cutaneous squamous cell carcinoma (SCC). In this study, we show that loss of Kindlin-1 in a mouse model of cutaneous SCC leads to increased migration, invasion and degradation of collagen. Loss of Kindlin-1 increased tumor growth in vivo and in 3D spheroids, which was associated with the development of a hypoxic tumor environment and increased glycolysis. One of the most highly upregulated genes in Kindlin-1-depleted tumors was Mmp13, and the increased expression of MMP13 was responsible for driving the increased migration and invasion of the Kindlin-1-depleted SCC cells. These results provide evidence that Kindlin-1 loss in SCC can promote migration and invasion through the upregulation of MMP13, and offer novel insights into how Kindlin-1 loss leads to the development of a hypoxic environment that is permissive for tumor growth.

2023-07-14 | GSE236883 | GEO

Expression data of cDNA from the ACHN control and Kindlin-2-depleting cells

Project description:Kindlin-2, an integrin-interacting FERM-domain-containing protein, has been known to play critical roles for tumor progression. However, the role of Kindlin-2 in renal cell carcinoma (RCC) progression has not been reported. We aim to investigate the role of Kindlin-2 in the progression of RCC and the underlying mechanisms. To uncover the related pathway in which Kindlin-2 is involved to promote clear cell renal cell carcinoma progression, ACHN control and Kindlin-2-depleting cells were analyzed by Affymetrix GeneChip human Gene 1.0 ST Arrays. ACHN cells were transfected with control short hairpin RNA (shRNA) or Kindlin-2 shRNA. ACHN control and Kindlin-2-depleting cells cDNAs were hybridized to Affymetrix GeneChip Human Gene 1.0 ST arrays. Data were analyzed by Expression Console 1.4.1.

2015-12-16 | E-GEOD-76020 | biostudies-arrayexpress

Kindlin-2 modulates PTH1R to regulate bone mass and PTH actions in bone

Project description:To investigation the role of PTH and Kindlin-2 in bone development, we performed single-cell RNA-sequencing. From Con-veh, Con-PTH, cKO-veh, cKO-PTH, we profiled more than 20k single cells, including multi-potent mesenchymal stromal cells (MSC), osteoprogenitors, osteoblasts, chondrocytes, fibroblasts, endothelial cells, smooth muscle cells, skeletal muscle cells, pericytes, and schwann cells. We found proportion of part of these cells were significant altered by PTH or Kindlin-2 loss, especially for MSC, osteoblast, chondrocyte, and fibroblast. Transcriptomic analysis revealed gene expression was dramatically regulated by PTH or Kindlin-2 loss.

2020-10-01 | GSE150291 | GEO

Expression data of cDNA from the ACHN control and Kindlin-2-depleting cells

2015-12-16 | GSE76020 | GEO

Mechanism of Kindlin-2 regulating invasion and metastasis of human Hepatocellular carcinoma

Project description:To explore the mechanism of Kindlin-2 regulating invasion and metastasis of human Hepatocellular carcinoma, we performed gene expression microarray analysis on Kindlin-2 knockdown LM3 cells and the control cells to compare the gene expression levels between the two groups.

2017-04-19 | GSE97951 | GEO

Comparative gene expression profiling of group-housed, less aggressive vs. single-housed, more aggressive male flies

Project description:Social experience influences multiple behaviors of many animal species, including aggression. Social isolation often increases aggressiveness. To investigater the molecular basis of social influences on aggressiveness, we performed comparative gene expression profiling on heads from 6-day-old, single-housed, more aggressive and group-housed, less aggressive male flies. Keywords: social experience

2008-02-08 | GSE6994 | GEO

Gene expression profile at single cell level of mammary gland from Kindlin-2 genetically modified mouse model

Project description:During gestation, alveolar cells are derived from luminal progenitors in the mammary gland. However, the mechanism underlying luminal progenitor commitment to alveolar cells remains largely unknown. By using five genetically modified mouse lines and single cell RNA sequencing, we identified a Kindlin-2 - Stat3 - Dll1 signaling cascade in myoepithelial cells which controls the inactivation of Notch signaling in luminal cells that consequently drives luminal progenitor commitment to alveolar cells. We found that loss of Kindlin-2 in myoepithelial cells impairs mammary morphogenesis and alveologenesis, and lactation. Single-cell profiling reveals that Kindlin-2 loss significantly decreases the proportion of alveolar cells.

2023-03-07 | GSE222028 | GEO

Low kindlin-3 levels in osteoclasts of kindlin-3 hypomorphic mice result in osteopetrosis due to leaky sealing zones

Project description:Osteoclasts form special integrin-mediated adhesion structures called sealing zones that enable them to adhere to and resorb bone. Sealing zones consist mainly of densely packed podosomes tightly inter-connected by actin fibers. Their formation requires the presence of the hematopoietic integrin regulator kindlin-3. In the current study, we investigated osteoclasts and their adhesion structures in kindlin-3 hypomorphic mice expressing only 5-10% of kindlin-3. Low kindlin-3 expression reduces integrin activity, results in impaired osteoclast adhesion and signaling, and delays cell spreading. Despite these defects, in vitro generated kindlin-3-hypomorphic osteoclasts arrange their podosomes into adhesion patches and belts, which show abnormal podosome and actin organization. Remarkably, kindlin-3-hypomorphic osteoclasts form sealing zones when cultured on calcified matrix in vitro and on bone surface in vivo. However, functional assays as well as immunohistochemical staining and electron micrographs of bone sections showed that they fail to properly seal the resorption lacunae, which is required for secreted proteases to be able to digest bone matrix. This results in mild osteopetrosis. Our study reveals a new, hitherto understudied function of kindlin-3 as an essential organizer of integrin-mediated adhesion structures, such as sealing zones.

2021-11-25 | PXD026711 | Pride

Mass spectrometry-based analysis of kindlin phosphorylation, ubiquitination and interactome

Project description:Kindlin is an essential activator of integrins and thus indispensable in cell to extracellular matrix (ECM) adhesion. Kindlin abundance and functions are tightly regulated by multiple mechanisms including post-translational modifications (PTMs). Despite the critical roles of kindlin during embryonic development and pathogenesis, the knowledge of kindlin’s PTMs and interactome is far from complete. Here we analyze the phosphorylation, ubiquitination and interacting partners of kindlin in flat, firmly adherent interphase cells and round, weakly attached mitotic cells by immunoprecipitation-based mass spectrometry (IP-MS). The analysis generated potential phosphorylation and ubiquitination sites as well as interactors of kindlin and paved the way to investigate PTMs and binding partners of kindlin.

2022-02-22 | PXD031829 | Pride

Mass spectrometry proteomics detecting interaction proteins of Kindlin-2

Project description:We aim to find out the Kindlin-2 interaction proteins. We transfected plasmids Flag or Flag-Kindlin-2 to HKC cell lines and then used Flag-M2 beads to do the coimmunoprecipitation experiments and followed by NuPAGE Tris-Acetate Mini Gels detection and stained by Coomassie brilliant blue. Compared the two groups,and then we will find the proteins interact with Kindlin-2.

2019-12-16 | PXD016008 | Pride

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