Emerging roles of the cellular prion protein (PrPC) and 37/67 kDa laminin receptor (RPSA) interaction in cancer biology.
| Title: | Emerging roles of the cellular prion protein (PrPC) and 37/67 kDa laminin receptor (RPSA) interaction in cancer biology. |
|---|---|
| Authors: | Limone, Adriana1 (AUTHOR), Maggisano, Valentina2 (AUTHOR), Sarnataro, Daniela1 (AUTHOR) sarnatar@unina.it, Bulotta, Stefania2 (AUTHOR) |
| Source: | Cellular & Molecular Life Sciences. Aug2023, Vol. 80 Issue 8, p1-18. 18p. |
| Abstract: | The cellular prion protein (PrPC) is well-known for its involvement, under its pathogenic protease-resistant form (PrPSc), in a group of neurodegenerative diseases, known as prion diseases. PrPC is expressed in nervous system, as well as in other peripheral organs, and has been found overexpressed in several types of solid tumors. Notwithstanding, studies in recent years have disclosed an emerging role for PrPC in various cancer associated processes. PrPC has high binding affinity for 37/67 kDa laminin receptor (RPSA), a molecule that acts as a key player in tumorigenesis, affecting cell growth, adhesion, migration, invasion and cell death processes. Recently, we have characterized at cellular level, small molecules able to antagonize the direct PrPC binding to RPSA and their intracellular trafficking. These findings are very crucial considering that the main function of RPSA is to modulate key events in the metastasis cascade. Elucidation of the role played by PrPC/RPSA interaction in regulating tumor development, progression and response to treatment, represents a very promising challenge to gain pathogenetic information and discover novel specific biomarkers and/or therapeutic targets to be exploited in clinical settings. This review attempts to convey a detailed description of the complexity surrounding these multifaceted proteins from the perspective of cancer hallmarks, but with a specific focus on the role of their interaction in the control of proliferation, migration and invasion, genome instability and mutation, as well as resistance to cell death controlled by autophagic pathway. [ABSTRACT FROM AUTHOR] |
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| Items | – Name: Title Label: Title Group: Ti Data: Emerging roles of the cellular prion protein (PrP<superscript>C</superscript>) and 37/67 kDa laminin receptor (RPSA) interaction in cancer biology. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Limone%2C+Adriana%22">Limone, Adriana</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Maggisano%2C+Valentina%22">Maggisano, Valentina</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Sarnataro%2C+Daniela%22">Sarnataro, Daniela</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> sarnatar@unina.it</i><br /><searchLink fieldCode="AR" term="%22Bulotta%2C+Stefania%22">Bulotta, Stefania</searchLink><relatesTo>2</relatesTo> (AUTHOR) – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Cellular+%26+Molecular+Life+Sciences%22">Cellular & Molecular Life Sciences</searchLink>. Aug2023, Vol. 80 Issue 8, p1-18. 18p. – Name: Abstract Label: Abstract Group: Ab Data: The cellular prion protein (PrPC) is well-known for its involvement, under its pathogenic protease-resistant form (PrPSc), in a group of neurodegenerative diseases, known as prion diseases. PrPC is expressed in nervous system, as well as in other peripheral organs, and has been found overexpressed in several types of solid tumors. Notwithstanding, studies in recent years have disclosed an emerging role for PrPC in various cancer associated processes. PrPC has high binding affinity for 37/67 kDa laminin receptor (RPSA), a molecule that acts as a key player in tumorigenesis, affecting cell growth, adhesion, migration, invasion and cell death processes. Recently, we have characterized at cellular level, small molecules able to antagonize the direct PrPC binding to RPSA and their intracellular trafficking. These findings are very crucial considering that the main function of RPSA is to modulate key events in the metastasis cascade. Elucidation of the role played by PrPC/RPSA interaction in regulating tumor development, progression and response to treatment, represents a very promising challenge to gain pathogenetic information and discover novel specific biomarkers and/or therapeutic targets to be exploited in clinical settings. This review attempts to convey a detailed description of the complexity surrounding these multifaceted proteins from the perspective of cancer hallmarks, but with a specific focus on the role of their interaction in the control of proliferation, migration and invasion, genome instability and mutation, as well as resistance to cell death controlled by autophagic pathway. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Cellular & Molecular Life Sciences is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1007/s00018-023-04844-2 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 18 StartPage: 1 Titles: – TitleFull: Emerging roles of the cellular prion protein (PrPC) and 37/67 kDa laminin receptor (RPSA) interaction in cancer biology. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Limone, Adriana – PersonEntity: Name: NameFull: Maggisano, Valentina – PersonEntity: Name: NameFull: Sarnataro, Daniela – PersonEntity: Name: NameFull: Bulotta, Stefania IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 08 Text: Aug2023 Type: published Y: 2023 Identifiers: – Type: issn-print Value: 1420682X Numbering: – Type: volume Value: 80 – Type: issue Value: 8 Titles: – TitleFull: Cellular & Molecular Life Sciences Type: main |
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