Publication:
Signaling mechanisms in red blood cells: a view through the protein phosphorylation and deformability

dc.contributor.departmentKUTTAM (Koç University Research Center for Translational Medicine)
dc.contributor.departmentGraduate School of Health Sciences
dc.contributor.departmentSchool of Medicine
dc.contributor.kuauthorÇilek, Neslihan
dc.contributor.kuauthorGöksel, Evrim
dc.contributor.kuauthorUğurel, Elif
dc.contributor.kuauthorYalçın, Özlem
dc.contributor.schoolcollegeinstituteGRADUATE SCHOOL OF HEALTH SCIENCES
dc.contributor.schoolcollegeinstituteResearch Center
dc.contributor.schoolcollegeinstituteSCHOOL OF MEDICINE
dc.date.accessioned2024-12-29T09:38:17Z
dc.date.issued2024
dc.description.abstractIntracellular signaling mechanisms in red blood cells (RBCs) involve various protein kinases and phosphatases and enable rapid adaptive responses to hypoxia, metabolic requirements, oxidative stress, or shear stress by regulating the physiological properties of the cell. Protein phosphorylation is a ubiquitous mechanism for intracellular signal transduction, volume regulation, and cytoskeletal organization in RBCs. Spectrin-based cytoskeleton connects integral membrane proteins, band 3 and glycophorin C to junctional proteins, ankyrin and Protein 4.1. Phosphorylation leads to a conformational change in the protein structure, weakening the interactions between proteins in the cytoskeletal network that confers a more flexible nature for the RBC membrane. The structural organization of the membrane and the cytoskeleton determines RBC deformability that allows cells to change their ability to deform under shear stress to pass through narrow capillaries. The shear stress sensing mechanisms and oxygenation-deoxygenation transitions regulate cell volume and mechanical properties of the membrane through the activation of ion transporters and specific phosphorylation events mediated by signal transduction. In this review, we summarize the roles of Protein kinase C, cAMP-Protein kinase A, cGMP-nitric oxide, RhoGTPase, and MAP/ERK pathways in the modulation of RBC deformability in both healthy and disease states. We emphasize that targeting signaling elements may be a therapeutic strategy for the treatment of hemoglobinopathies or channelopathies. We expect the present review will provide additional insights into RBC responses to shear stress and hypoxia via signaling mechanisms and shed light on the current and novel treatment options for pathophysiological conditions.
dc.description.indexedbyWOS
dc.description.indexedbyScopus
dc.description.indexedbyPubMed
dc.description.issue3
dc.description.publisherscopeInternational
dc.description.sponsoredbyTubitakEuN/A
dc.description.sponsorshipThe authors gratefully acknowledge the use of the services and facilities of the Koç University Research Center for Translational Medicine (KUTTAM) funded by the Presidency of Turkey, Presidency of Strategy and Budget.
dc.description.volume239
dc.identifier.doi10.1002/jcp.30958
dc.identifier.eissn1097-4652
dc.identifier.issn0021-9541
dc.identifier.quartileQ1
dc.identifier.scopus2-s2.0-85147507123
dc.identifier.urihttps://doi.org/10.1002/jcp.30958
dc.identifier.urihttps://hdl.handle.net/20.500.14288/22645
dc.identifier.wos928820000001
dc.keywordsDeformability
dc.keywordsMechanism
dc.keywordsProtein phosphorylation
dc.keywordsRed blood cell
dc.keywordsShear stress
dc.keywordsSignaling
dc.language.isoeng
dc.publisherJohn Wiley and Sons Inc
dc.relation.ispartofJournal of Cellular Physiology
dc.subjectCell biology
dc.subjectPhysiology
dc.titleSignaling mechanisms in red blood cells: a view through the protein phosphorylation and deformability
dc.typeReview
dspace.entity.typePublication
local.contributor.kuauthorÇilek, Neslihan
local.contributor.kuauthorUğurel, Elif
local.contributor.kuauthorGöksel, Evrim
local.contributor.kuauthorYalçın, Özlem
local.publication.orgunit1GRADUATE SCHOOL OF HEALTH SCIENCES
local.publication.orgunit1SCHOOL OF MEDICINE
local.publication.orgunit1Research Center
local.publication.orgunit2KUTTAM (Koç University Research Center for Translational Medicine)
local.publication.orgunit2School of Medicine
local.publication.orgunit2Graduate School of Health Sciences
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