We are analyzing https://link.springer.com/article/10.1007/s002770100352.

Title:
Protein kinase C isoforms in human erythrocytes | Annals of Hematology
Description:
Erythrocytes are the most abundant cells in blood and carry out the vital function of oxygen transport. These cells lack nuclei and do not synthesise new proteins. Their cellular responses are modulated entirely by post-translational modifications in existing proteins. Phosphorylation mediated by protein kinase C (PKC) plays a significant role in red cell physiology. To date PKC α and ζ are the only isoforms reported to be expressed in erythrocytes. Upon activation they influence cytoskeletal integrity and erythrocyte functions. In this study we report for the first time the presence of PKC ι and PKC µ in addition to PKC α and ζ in human erythrocytes. All isoforms were present only in the cytosolic fraction. PKC α was the only isoform that translocated to the membrane upon stimulation with phorbol myristate acetate (PMA). It could thus mediate several of the reported PMA-regulated membrane modifications. Investigations on alterations in PMA-mediated phosphorylation of erythrocyte skeletal components in disorders such as chronic myeloid leukaemia can now focus on PKC α, which is the only isoform in erythrocytes, which translocates to the membrane on stimulation of the cells.
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Keywords {🔍}

article, erythrocytes, pkc, privacy, cookies, content, publish, research, search, protein, kinase, isoforms, human, zingde, access, data, information, log, journal, govekar, cells, proteins, phosphorylation, erythrocyte, membrane, discover, author, springer, function, optional, analysis, personal, parties, policy, find, track, annals, hematology, published, july, cite, explore, blood, modifications, red, cell, reported, isoform, stimulation, institution,

Topics {✒️}

month download article/chapter pma-mediated phosphorylation privacy choices/manage cookies cancer research institute full article pdf post-translational modifications red cell physiology related subjects european economic area scope submit manuscript phosphorylation mediated influence cytoskeletal integrity phorbol myristate acetate erythrocyte skeletal components chronic myeloid leukaemia molecular biology division tata memorial centre conditions privacy policy accepting optional cookies cells lack nuclei article annals journal finder publish date pkc α human erythrocytes author correspondence article log protein kinase ages article 01 privacy policy personal data existing proteins books a article cite article govekar optional cookies manage preferences hematology aims erythrocyte functions check access lamprey erythrocytes instant access subscription content similar content isoforms reported data protection essential cookies cookies skip institution subscribe journal publish pkc α

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         description: Erythrocytes are the most abundant cells in blood and carry out the vital function of oxygen transport. These cells lack nuclei and do not synthesise new proteins. Their cellular responses are modulated entirely by post-translational modifications in existing proteins. Phosphorylation mediated by protein kinase C (PKC) plays a significant role in red cell physiology. To date PKC α and ζ are the only isoforms reported to be expressed in erythrocytes. Upon activation they influence cytoskeletal integrity and erythrocyte functions. In this study we report for the first time the presence of PKC ι and PKC µ in addition to PKC α and ζ in human erythrocytes. All isoforms were present only in the cytosolic fraction. PKC α was the only isoform that translocated to the membrane upon stimulation with phorbol myristate acetate (PMA). It could thus mediate several of the reported PMA-regulated membrane modifications. Investigations on alterations in PMA-mediated phosphorylation of erythrocyte skeletal components in disorders such as chronic myeloid leukaemia can now focus on PKC α, which is the only isoform in erythrocytes, which translocates to the membrane on stimulation of the cells.
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      headline:Protein kinase C isoforms in human erythrocytes
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