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

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...

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Veröffentlicht in:The Journal of biological chemistry 1994-04, Vol.269 (16), p.12310-12319
Hauptverfasser: CHE-LEUNG LAW, SIDORENKO, S. P, CHANDRAN, K. A, DRAVES, K. E, CHAN, A. C, WEISS, A, EDELHOFF, S, DISTECHE, C. M, CLARK, E. A
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container_end_page 12319
container_issue 16
container_start_page 12310
container_title The Journal of biological chemistry
container_volume 269
creator CHE-LEUNG LAW
SIDORENKO, S. P
CHANDRAN, K. A
DRAVES, K. E
CHAN, A. C
WEISS, A
EDELHOFF, S
DISTECHE, C. M
CLARK, E. A
description 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.
doi_str_mv 10.1016/S0021-9258(17)32717-5
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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. 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Psychology ; genes ; Humans ; immunoglobulin M ; Intracellular Signaling Peptides and Proteins ; lymphocytes B ; man ; Mice ; Molecular Sequence Data ; nucleotide sequence ; Phosphorylation ; prediction ; protein-tyrosine kinase ; Protein-Tyrosine Kinases - biosynthesis ; Protein-Tyrosine Kinases - genetics ; Protein-Tyrosine Kinases - isolation &amp; purification ; Receptors, Antigen, B-Cell - isolation &amp; purification ; Receptors, Antigen, B-Cell - metabolism ; Restriction Mapping ; RNA, Messenger - analysis ; RNA, Messenger - biosynthesis ; Sequence Homology, Amino Acid ; Spleen - enzymology ; Swine ; Syk Kinase ; T-Lymphocytes - immunology ; Transfection ; Transferases</subject><ispartof>The Journal of biological chemistry, 1994-04, Vol.269 (16), p.12310-12319</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-47d4b8a644cd39e2abf707ce94854816e247edad717bcdd1aa54a7f4009c46033</citedby><cites>FETCH-LOGICAL-c440t-47d4b8a644cd39e2abf707ce94854816e247edad717bcdd1aa54a7f4009c46033</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=4153701$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8163536$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>CHE-LEUNG LAW</creatorcontrib><creatorcontrib>SIDORENKO, S. P</creatorcontrib><creatorcontrib>CHANDRAN, K. A</creatorcontrib><creatorcontrib>DRAVES, K. E</creatorcontrib><creatorcontrib>CHAN, A. C</creatorcontrib><creatorcontrib>WEISS, A</creatorcontrib><creatorcontrib>EDELHOFF, S</creatorcontrib><creatorcontrib>DISTECHE, C. M</creatorcontrib><creatorcontrib>CLARK, E. A</creatorcontrib><title>Molecular cloning of human Syk. A B cell protein-tyrosine kinase associated with the surface immunoglobulin M-B cell receptor complex</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>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. 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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.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8163536</pmid><doi>10.1016/S0021-9258(17)32717-5</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record>
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subjects Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
association
B-Lymphocytes - enzymology
B-Lymphocytes - immunology
Base Sequence
Biological and medical sciences
cDNA
Cell Line
cell surface
Chromosome Mapping
Chromosomes, Human, Pair 9
Cloning, Molecular - methods
Conserved Sequence
DNA, Complementary - analysis
Enzyme Precursors - biosynthesis
Enzyme Precursors - genetics
Enzyme Precursors - isolation & purification
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
genes
Humans
immunoglobulin M
Intracellular Signaling Peptides and Proteins
lymphocytes B
man
Mice
Molecular Sequence Data
nucleotide sequence
Phosphorylation
prediction
protein-tyrosine kinase
Protein-Tyrosine Kinases - biosynthesis
Protein-Tyrosine Kinases - genetics
Protein-Tyrosine Kinases - isolation & purification
Receptors, Antigen, B-Cell - isolation & purification
Receptors, Antigen, B-Cell - metabolism
Restriction Mapping
RNA, Messenger - analysis
RNA, Messenger - biosynthesis
Sequence Homology, Amino Acid
Spleen - enzymology
Swine
Syk Kinase
T-Lymphocytes - immunology
Transfection
Transferases
title Molecular cloning of human Syk. A B cell protein-tyrosine kinase associated with the surface immunoglobulin M-B cell receptor complex
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