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  2. Identification and characterization of non-small cell lung cancer associated sialoglycoproteins

Identification and characterization of non-small cell lung cancer associated sialoglycoproteins

  • J Proteomics. 2021 Sep 30:248:104336. doi: 10.1016/j.jprot.2021.104336.
Munmun Kumari 1 Praveen Singh 1 Navneet Singh 2 Amanjit Bal 3 Radhika Srinivasan 4 Sujata Ghosh 5
Affiliations

Affiliations

  • 1 Department of Experimental Medicine and Biotechnology, Postgraduate Institute of Medical Education and Research, Chandigarh, India.
  • 2 Department of Pulmonary Medicine, Postgraduate Institute of Medical Education and Research, Chandigarh, India.
  • 3 Department of Histopathology, Postgraduate Institute of Medical Education and Research, Chandigarh, India.
  • 4 Department of Cytology & Gynecological Pathology, Postgraduate Institute of Medical Education and Research, Chandigarh, India.
  • 5 Department of Experimental Medicine and Biotechnology, Postgraduate Institute of Medical Education and Research, Chandigarh, India. Electronic address: [email protected].
Abstract

Aberrantly sialylated cellular glycoconjugates were found to be involved in different processes during tumorigenesis. Such alteration was also noted in case of lung Cancer, an important cause of cancer-related death throughout the world. Thus, study on lung Cancer associated sialoglycoproteins is of paramount relevance to have a deeper insight into the mechanism of the disease pathogenesis. In the present study, sialic acid specific lectin (Maackia amurensis agglutinin and Sambcus nigra agglutinin)-based affinity chromatography followed by 2D-PAGE and MALDI-TOF/TOF mass spectrometric analysis were done to explore the disease-associated serum proteins of squamous cell carcinoma and adenocarcinoma [the major two subtypes of NSCLC (non-small cell lung carcinoma)] patients. Among seven identified proteins, α1-antitrypsin and haptoglobin-β were preferred for further studies. These two proteins were characterized as the disease associated serum-sialoglycoproteins of NSCLC-patients by western immunoblotting using each lectin specific inhibitor. The presence of these sialoglycoproteins was found on NSCLC cell lines (NCI-H520 & A549) by confocal microscopy. Both these proteins were also present in tissue samples of NSCLC origin and involved in proliferation, invasion and migration of NSCLC cells. Our findings suggest that α1-antitrypsin and haptoglobin-β may be the disease-associated sialoglycoproteins in NSCLC, which seem to be involved in disease progression. SIGNIFICANCE: Our contribution regarding the identification of the NSCLC associated sialoglycoproteins may provide a new vision towards the development of clinically useful newer strategies for the treatment of this disease.

Keywords

Haptoglobin-β; Lung cancer; Maackia amurensis leukoagglutinin; Sambcus nigra agglutinin; Sialoglycoproteins; α-1-antitrypsin.

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