Antibodies to distal carboxyl terminal epitopes in the v-fms-coded glycoprotein do not cross-react with the c-fms gene product.
Antibodies to distal carboxyl terminal epitopes in the v-fms-coded glycoprotein do not cross-react with the c-fms gene product.
复制标题
针对 v-fms 编码糖蛋白中远端羧基末端表位的抗体不会与 c-fms 基因产物发生交叉反应。
DOI:
10.1016/0042-6822(86)90145-5
复制
发表时间:
1986
期刊:
影响因子:
3.7
通讯作者:
Sherr,CJ
中科院分区:
文献类型:
--
作者:
Furman,WL;Rettenmier,CW;Chen,JH;Roussel,MF;Quinn,CO;Sherr,CJ
The product of the v-fmsoncogene is an integral transmembrane glycoprotein that is closely related to the cell surface receptor for the macrophage colony stimulating factor, CSF-1. A fragment of the v-fmsgene encoding a major portion of the extracellular amino terminal domain, the membrane-spanning segment, and the entire carboxyl terminal tyrosine kinase domain of the glycoprotein was molecularly cloned into an inducible prokaryotic expression plasmid. Polypeptide products consisting only of v-fms-coded amino acids were produced in bacteria and were used to prepare immune reagents that precipitated the v-fms-coded glycoproteins expressed in transformed cells. Whereas rabbit antisera to recombinant polypeptides detected antigenic determinants of the c-fmsproto-oncogene product, seven mouse monoclonal antibodies to these same antigens reacted only with v-fms-specific epitopes. Proteolytic mapping experiments and studies with a mutant v-fms-coded glycoprotein lacking the 37 carboxyl terminal amino acids of the wild-type product showed that the monoclonal antibodies were restricted in their reactivity to epitopes at the extreme carboxyl terminus of the glycoprotein. The v-fmsand c-fmsgene products must differ significantly in this region.