Identification and characterization of the lamprey Flotillin-1 gene with a role in cell adhesion. Issue 71 (December 2017)
- Record Type:
- Journal Article
- Title:
- Identification and characterization of the lamprey Flotillin-1 gene with a role in cell adhesion. Issue 71 (December 2017)
- Main Title:
- Identification and characterization of the lamprey Flotillin-1 gene with a role in cell adhesion
- Authors:
- Xu, Rong
Song, Xiaoping
Su, Peng
Pang, Yue
Li, Qingwei - Abstract:
- Abstract: Flotillin-1 is a kind of localize into specific cholesterol rich microdomains in cellular membranes and highly conserved lipid rafts marker protein widely distributed in animals and plants. It provides a platform for the reaction of many proteins in signal transduction, as scaffolding plays an important role in transmembrane signaling and cell adhesion. Here, Flotillin-1 protein from lamprey was identified and characterized (designated as L-Flotillin-1). After a partial cDNA sequence of L-Flotillin-1 was identified in a lamprey supraneural body cDNA library, the full-length cDNA was obtained using 3'- and 5'-rapid amplification of cDNA ends (RACE). L-Flotillin-1 encodes 424 amino acids and contains a prohibitin domain and a flotillin repetitive area. The L-Flotillin-1 protein was primarily distributed in kidney, supraneural body, gill, heart, liver and intestine via real-time PCR and immunohistochemistry assays. Immunofluorescence and western blot results showed that L-Flotillin-1 was considered to be used as a marker protein of lamprey lipid rafts and exosomes. Furthermore, overexpression of pEGFP-N1-L-Flotillin-1 induced the up-regulation of vascular cell adhesion molecule-1 (VCAM-1) and intercellular cell adhesion molecule-1 (ICAM-1) mRNA levels. These results indicated that the L-Flotillin-1 gene encodes Flotillin-1 protein that was used as a conserved marker protein and may play an important role in cell adhesion, providing clues for understanding theAbstract: Flotillin-1 is a kind of localize into specific cholesterol rich microdomains in cellular membranes and highly conserved lipid rafts marker protein widely distributed in animals and plants. It provides a platform for the reaction of many proteins in signal transduction, as scaffolding plays an important role in transmembrane signaling and cell adhesion. Here, Flotillin-1 protein from lamprey was identified and characterized (designated as L-Flotillin-1). After a partial cDNA sequence of L-Flotillin-1 was identified in a lamprey supraneural body cDNA library, the full-length cDNA was obtained using 3'- and 5'-rapid amplification of cDNA ends (RACE). L-Flotillin-1 encodes 424 amino acids and contains a prohibitin domain and a flotillin repetitive area. The L-Flotillin-1 protein was primarily distributed in kidney, supraneural body, gill, heart, liver and intestine via real-time PCR and immunohistochemistry assays. Immunofluorescence and western blot results showed that L-Flotillin-1 was considered to be used as a marker protein of lamprey lipid rafts and exosomes. Furthermore, overexpression of pEGFP-N1-L-Flotillin-1 induced the up-regulation of vascular cell adhesion molecule-1 (VCAM-1) and intercellular cell adhesion molecule-1 (ICAM-1) mRNA levels. These results indicated that the L-Flotillin-1 gene encodes Flotillin-1 protein that was used as a conserved marker protein and may play an important role in cell adhesion, providing clues for understanding the universal functions of Flotillin-1 proteins in other species and suggesting that these proteins could serve as pattern recognition molecules in immunotherapy. We revealed that Flotillin-1 protein of lamprey overexpression in human cells plays a prevalent role in cell migration and provide new thought of treatment to diseases. Highlights: Flotillin-1 gene was identified from lamprey supraneural body cDNA library. With continuous LPS stimulation, the level of Flotillin-1 protein expression was significant increase in intestinal tissue. The overexpression of pEGFP-N1-L-Flotillin-1 induced the up-regulation of VCAM-1 and ICAM-1 mRNA levels in Hela and HepG-2 cells. … (more)
- Is Part Of:
- Fish & shellfish immunology. Issue 71(2017)
- Journal:
- Fish & shellfish immunology
- Issue:
- Issue 71(2017)
- Issue Display:
- Volume 71, Issue 71 (2017)
- Year:
- 2017
- Volume:
- 71
- Issue:
- 71
- Issue Sort Value:
- 2017-0071-0071-0000
- Page Start:
- 286
- Page End:
- 294
- Publication Date:
- 2017-12
- Subjects:
- Flotillin-1 -- Lipid rafts -- Lamprey -- Cell adhesion
Fishes -- Immunology -- Periodicals
Shellfish -- Immunology -- Periodicals
Poissons -- Immunologie -- Périodiques
Crustacés -- Immunologie -- Périodiques
571.9617 - Journal URLs:
- http://www.sciencedirect.com/science/journal/10504648 ↗
http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=1050-4648;screen=info;ECOIP ↗
http://www.sciencedirect.com/science/journal/latest/10504648 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.fsi.2017.06.061 ↗
- Languages:
- English
- ISSNs:
- 1050-4648
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3934.880000
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- 5460.xml