Katarzyna Ratajczak-Wielgomas

Dr. Katarzyna Ratajczak-Wielgomas

Division of Histology and Embryology, Department of Human Morphology and Embryology, Wroclaw Medical University, Wroclaw, Poland
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Research Focus & Metrics

Academic Career Length

21Years (2006-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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30 August 2022 in Cancers
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Journal Article
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AWAdrian Wąsik
Adrian Wąsik
KRKatarzyna Ratajczak-Wielgomas
Katarzyna Ratajczak-Wielgomas
ABArkadiusz Badziński
Arkadiusz Badziński
Piotr DziegielPiotr Dziegiel
Piotr Dziegiel
MPMarzenna Podhorska-Okolow
Marzenna Podhorska-Okolow
Periostin (POSTN) is a protein that is part of the extracellular matrix (ECM) and which significantly affects the control of intracellular signaling pathways (PI3K-AKT, FAK) through binding integrin receptors (αvβ3, αvβ5, α6β4). In addition, increased POSTN expression enhances the expression of VEGF family growth factors and promotes Erk phosphorylation. As a result, this glycoprotein controls the Erk/VEGF pathway. Therefore, it plays a crucial role in the formation of new blood and lymphatic vessels, which may be significant in the process of metastasis. Moreover, POSTN is involved in the proliferation, progression, migration and epithelial-mesenchymal transition (EMT) of tumor cells. Its increased expression has been detected in many cancers, including breast cancer, ovarian cancer, non-small cell lung carcinoma and glioblastoma. Many studies have shown that this protein may be an independent prognostic and predictive factor in many cancers, which may influence the choice of optimal therapy.

29 July 2015 in Folia Histochemica et Cytobiologica
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Journal Article
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KRKatarzyna Ratajczak-Wielgomas
Katarzyna Ratajczak-Wielgomas
Piotr DziegielPiotr Dziegiel
Piotr Dziegiel
Periostin, also called osteoblast-specific factor 2 (OSF-2), is a multifunctional glycoprotein that belongs to the group of matricellular proteins. Due to its characteristic molecular structure containing integrin-binding domains, periostin is capable of binding to multiple integrin receptors (αvβ3, αvβ5, α6β4), thus affecting the regulation of the intracellular signaling pathways associated with protein kinases PI3K/AKT and focal adhesion kinase (FAK). This protein thus plays a role in the adhesion process, in the migration of many cells, and importantly, epithelial-mesenchymal transition of cancer cells. Periostin also participates in the processes of angiogenesis and lymphangiogenesis, metastases of cancer cells, and remodeling of the extracellular matrix. Increased expression of periostin has been observed in various tumor types, including breast, NSCLC, colorectal, pancreatic, prostate, and ovarian cancers, as well as tumors of the head and neck, and glioblastomas. Many groups have recently reported on periostin's key role in tumor progression, which suggests that periostin can be considered a potential therapeutic target.

15 September 2016 in Oncology Reports
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KRKatarzyna Ratajczak-Wielgomas
Katarzyna Ratajczak-Wielgomas
JGJedrzej Grzegrzolka
Jedrzej Grzegrzolka
APAleksandra Piotrowska
Aleksandra Piotrowska
AGAgnieszka Gomulkiewicz
Agnieszka Gomulkiewicz
WWWojciech Witkiewicz
Wojciech Witkiewicz
Piotr DziegielPiotr Dziegiel
Piotr Dziegiel
Spandidos Publications is a scientific publisher with a long-standing international reputation for excellent standards and high quality science publications

19 March 2010 in Wound Repair and Regeneration
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KSKatarzyna Skórkowska-Telichowska
Katarzyna Skórkowska-Telichowska
MZMagdalena Zuk
Magdalena Zuk
AKAnna Kulma
Anna Kulma
ABAda Bugajska-Prusak
Ada Bugajska-Prusak
KRKatarzyna Ratajczak-Wielgomas
Katarzyna Ratajczak-Wielgomas
JSJan Szopa
Jan Szopa

11 October 2019 in Cancers
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KNKatarzyna Nowinska
Katarzyna Nowinska
KJKarolina Jabłońska
Karolina Jabłońska
KPKonrad Pawełczyk
Konrad Pawełczyk
APAleksandra Piotrowska
Aleksandra Piotrowska
APAleksandra Partyńska
Aleksandra Partyńska
Piotr DziegielPiotr Dziegiel
Piotr Dziegiel
Background: Recent in vitro studies have indicated that irisin inhibits proliferation, migration and epithelial-mesenchymal transition. Irisin expression has not been studied in tumour tissues of non-small cell lung cancer (NSCLC) patients yet. The aim of the study was to determine the irisin expression in NSCLCs in comparison to the clinicopathological factors and expression of TTF-1, p63 and Ki-67. Material and methods: Tissue microarrays with 729 NSCLC and 140 non-malignant lung tissue (NMLT) were used to perform immunohistochemical reactions. Laser Capture Microdissection (LCM) was used to collect cancer and stromal cells from NSCLCs. FNDC5 expression was tested for LCM samples, 75 NSCLCs and 25 NMLTs with the RT-PCR technique. Western-blot, immunofluorescence reaction and RT-PCR assays were performed on lung cancer cell lines. Results: Irisin expression was observed in NSCLC cancer cells and stromal fibroblasts. In cancer cells, irisin expression was decreased in higher grades (G) of malignancy, tumour size (T) and according to lymph node metastasis. In stromal cells, irisin expression was increased in higher G and advanced T. A shorter overall survival was observed in patients with higher irisin expression in NSCLC stromal cells. Conclusions: Irisin expression in stromal fibroblasts may influence cancer cell proliferation and may be a prognostic factor for survival in NSCLC.

Verified
Journal Article
Open access
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KRKatarzyna Ratajczak-Wielgomas
Katarzyna Ratajczak-Wielgomas
AKAlicja Kmiecik
Alicja Kmiecik
JGJedrzej Grzegrzolka
Jedrzej Grzegrzolka
APAleksandra Piotrowska
Aleksandra Piotrowska
AGAgnieszka Gomulkiewicz
Agnieszka Gomulkiewicz
Piotr DziegielPiotr Dziegiel
Piotr Dziegiel
Background: The microenvironment of solid tumours is significant in cancer development and progression. The aim of this study was to determine periostin (POSTN) expression by cancer-associated fibroblasts (CAFs) in non-small-cell lung cancer (NSCLC), as well as to assess associations with clinicopathological factors and prognosis. Materials and Methods: Immunohistochemical analysis of POSTN expression was performed on NSCLC (N = 700) and non-malignant lung tissue (NMLT) (N = 110) using tissue microarrays. Laser capture microdissection (LCM) for isolation of stromal and cancer cells of NSCLC was employed, and subsequently, POSTN mRNA expression was detected by real-time PCR. Immunofluorescence reaction and colocalisation analysis were performed by confocal microscopy. Results: Expression of POSTN in CAFs was significantly higher in NSCLC and in the adenocarcinoma (AC) and squamous cell carcinoma (SCC) subtypes compared to NMLT. POSTN expression in CAFs increased with clinical cancer stage, grades (G) of malignancy, and lymph node involvement in NSCLC. Higher POSTN expression in CAFs was an independent prognostic factor for overall survival (OS). LCM confirmed significantly higher POSTN mRNA expression in the stromal cells (CAFs) compared to the lung cancer cells. Conclusions: POSTN produced by CAFs might be crucial for NSCLC progression and can be an independent negative prognostic factor in NSCLC.