Isolation of protein kinase C subspecies from a preparation of human T lymphocytes
- 18 July 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 234 (2) , 387-391
- https://doi.org/10.1016/0014-5793(88)80122-4
Abstract
Using a preparation of purified human T lymphocytes, we were able to resolve a partially purified protein kinase C (PKC) enzyme fraction into two distinct subspecies, of approximately equal activity. Biochemical and immunocytochemical analysis revealed that these fractions closely resembled the type II(β) and type III(α) PKC subspecies previously identified and characterised from brain tissue. These results provide valuable information for further studies on the role of individual PKC subspecies in T lymphocyte proliferation.Keywords
This publication has 23 references indexed in Scilit:
- Identification of three additional members of rat protein kinase C family: gd‐, ϵ‐ and ξ‐subspeciesFEBS Letters, 1987
- Immunochemical identification of protein kinase C isozymes as products of discrete genesBiochemical and Biophysical Research Communications, 1987
- The common structure and activities of four subspecies of rat brain protein kinase C familyFEBS Letters, 1987
- Primary structures of human protein kinase C βI and βII differ only in their C‐terminal sequencesFEBS Letters, 1987
- Alternative Splicing Increases the Diversity of the Human Protein Kinase C FamilyDNA, 1987
- Differential expression of multiple protein kinase C subspecies in rat central nervous tissueBiochemical and Biophysical Research Communications, 1987
- Identification of the structures of multiple subspecies of protein kinase C expressed in rat brainFEBS Letters, 1987
- Three distinct forms of rat brain protein kinase C: Differential response to unsaturated fatty acidsBiochemical and Biophysical Research Communications, 1987
- Highly Purified Human T-Lymphocytes do not Respond to Mitogens-Including Calcium Ionophore and Phorbol EsterImmunological Investigations, 1987
- Early steps of lymphocyte activation bypassed by synergy between calcium ionophores and phorbol esterNature, 1985