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Molecular cloning of human Syk. A B cell protein-tyrosine kinase associated with the surface immunoglobulin M-B cell receptor complex.

Law, C.L., Sidorenko, S.P., Chandran, K.A., Draves, K.E., Chan, A.C., Weiss, A., Edelhoff, S., Disteche, C.M., Clark, E.A.·1994·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(17)32717-5
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Abstract

B cell antigen receptors are multicomponent complexes consisting of the surface immunoglobulin and accessory molecules with associating protein-tyrosine kinases. A spleen tyrosine kinase, Syk, in porcine B cells and a 72-kDa protein-tyrosine kinase, PTK72, in murine B cells associate with the B cell antigen receptor. Herein, we report the isolation of a full-length cDNA encoding the human homologue of Syk. This cDNA predicted a polypeptide consisting of two NH2-terminal SH2 domains and a COOH-terminal tyrosine kinase domain. Syk is highly conserved between human and swine and is homologous to the T cell-associated protein-tyrosine kinase ZAP-70. Both Syk mRNA and protein were detected in cells derived from multiple hematopoietic lineages. Within the B cell compartment, Syk was expressed from pro-B cells to plasma cells. In vitro kinase assays conducted on the human Syk protein isolated from B cells revealed the presence of autophosphorylation activity on Syk tyrosine residues. Tyrosine phosphorylation of Syk associating with the B cell receptor complex in human was augmented rapidly after surface immunoglobulin cross-linking. The human SYK locus was mapped to chromosome 9 at band q22.

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Cited by

Metadata

Authors
Law, C. L., Sidorenko, S. P., Chandran, K. A., Draves, K. E., Chan, A. C., Weiss, A., Edelhoff, S., Disteche, C. M., & Clark, E. A.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1994-04
Volume
269
Issue
16
Pages
12310-12319
ISSN
0021-9258
DOI
10.1016/s0021-9258(17)32717-5
Cited by
103
References
1
Language
en
Licence

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