ArticleThe Biochemical journal1995
Identification of a novel form of the alpha 3 integrin subunit: covalent association with transferrin receptor.
Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Biotin-transfer from a trifunctional crosslinker for identification of cell surface receptors of soluble protein ligands.Scientific reports · 2017Article
- Maintaining human fetal pancreatic stellate cell function and proliferation require β1 integrin and collagen I matrix interactions.Oncotarget · 2015Article
- Expression and function of alphabeta1 integrins in pancretic beta (INS-1) cells.Journal of cell communication and signaling · 2008Article
- Candidate genes, pathways and mechanisms for alcoholism: an expanded convergent functional genomics approach.The pharmacogenomics journal · 2007Article
- Evidence for a role of tumor-derived laminin-511 in the metastatic progression of breast cancer.The American journal of pathology · 2007Article
- Physiological and pathological roles of alpha3beta1 integrin.The Journal of membrane biology · 2004Review
- Integrin alpha 3 beta 1 participates in the phagocytosis of extracellular matrix molecules by human breast cancer cells.Molecular biology of the cell · 1996Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The alpha 3 beta 1 integrin is a cell-surface receptor for laminin, entactin, collagen, fibronectin and epiligrin. On some prostatic-carcinoma cell lines that express the alpha 3 beta 1 heterodimer we have identified a novel form of the alpha 3 subunit. Whereas the prototypic alpha 3 subunit has a molecular mass of approximately 155 kDa, we have isolated a approximately 225 kDa protein (p225) which is recognized by monoclonal antibodies to the alpha 3 subunit. Protein sequence analysis revealed that p225 consists of two polypeptides, namely integrin alpha 3 heavy chain (approximately 130 kDa) disulphide-bonded to a monomer of the transferrin receptor (approximately 95 kDa) instead of the typical alpha 3 light chain (approximately 25 kDa). The p225 seems to be directly associated with beta 1 subunit, since it was immunoprecipitable with anti-(beta 1 subunit) antibodies. The association of transferrin receptor and integrin alpha 3 was apparently not the result of spurious disulphide-bond formation occurring during the protein purification, as iodoacetamide and GSH did not block the formation of the complex. The transferrin receptor is normally a homodimer that is involved in the internalization of iron-bound transferrin into cells and can be expressed at relatively high levels in the cell lines which we have studied. The p225 is not found on all cell types examined to date and therefore it may represent a unique complex between the integrin alpha 3 subunit and the transferrin receptor, a covalent association which may play a role in the adherence and/or proliferation of some types of tumour cells.
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