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

dc.contributor.departmentN/A
dc.contributor.kuauthorÇilek, Neslihan
dc.contributor.kuauthorUğurel, Elif
dc.contributor.kuauthorGöksel, Evrim
dc.contributor.kuauthorYalçın, Özlem
dc.contributor.kuprofilePhD Student
dc.contributor.kuprofileResearcher
dc.contributor.kuprofilePhD Student
dc.contributor.kuprofileFaculty Member
dc.contributor.researchcenterKoç University Research Center for Translational Medicine (KUTTAM) / Koç Üniversitesi Translasyonel Tıp Araştırma Merkezi (KUTTAM)
dc.contributor.schoolcollegeinstituteGraduate School of Sciences and Engineering
dc.contributor.schoolcollegeinstituteSchool of Medicine
dc.contributor.schoolcollegeinstituteGraduate School of Health Sciences
dc.contributor.schoolcollegeinstituteSchool of Medicine
dc.contributor.yokidN/A
dc.contributor.yokidN/A
dc.contributor.yokidN/A
dc.contributor.yokid218440
dc.date.accessioned2024-11-09T22:48:54Z
dc.date.issued2023
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.openaccessNO
dc.description.publisherscopeInternational
dc.description.sponsorshipKoç University
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.urihttp://dx.doi.org/10.1002/jcp.30958
dc.identifier.urihttps://hdl.handle.net/20.500.14288/6419
dc.identifier.wos928820000001
dc.keywordsDeformability
dc.keywordsMechanism
dc.keywordsProtein phosphorylation
dc.keywordsRed blood cell
dc.keywordsShear stress
dc.keywordsSignaling
dc.languageEnglish
dc.publisherWiley
dc.sourceJournal 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.authorid0000-0002-5369-5411
local.contributor.authorid0000-0001-7789-0337
local.contributor.authorid0000-0003-4759-155X
local.contributor.authorid0000-0001-5547-6653
local.contributor.kuauthorÇilek, Neslihan
local.contributor.kuauthorUğurel, Elif
local.contributor.kuauthorGöksel, Evrim
local.contributor.kuauthorYalçın, Özlem

Files