TY - JOUR
T1 - Mouse myeloma mutants blocked in the assembly, glycosylation and secretion of immunoglobulin
AU - Weitzman, S.
AU - Scharff, M. D.
N1 - Funding Information:
We thank Lucille Frank and Theresa Kelly for their expert technical assistance, and Dr Jean-Louis Preud'homme whoso preliminary observations led to these experiments. This work was supported by grants from the National Institutes of Health (NIHAI05231, NIHAI10702), the National Science Foundation (BMS75-13609), and the American Cancer Society.
PY - 1976/4/5
Y1 - 1976/4/5
N2 - Two stable mutant cell lines derived from the MPC-11 mouse myeloma synthesize immunoglobulin with abnormal heavy chains and normal light chains. The mutant heavy chains have molecular weights of 38,000 to 42,000 (M3.11) and 50,000 (ICR 11.19) as compared to 55,000 of the wild type. The mutants demonstrate a variety of blocks in the assembly, glycosylation and secretion of immunoglobulin. (1) The wild type assembles and secretes 90% of its immunoglobulin primarily as H2L2 while M3.11 is partially blocked in the assembly of H2L2, and secretes approximately one half of its immunoglobulin as HL. ICR 11.19, with a more complete block in interchain disulfide bond formation, assembles less than 10% of its immunoglobulin into H2L2, has a block in secretion and degrades most of its immunoglobulin. (2) M3.11 uses only one of the two wild type pathways of assembly. Reduction of isolated H2L2 with 2-mercapthoethanol suggests an altered stability of the inter-H chain disulfide bonds in M3.11 as compared to the wild type immunoglobulin. (3) While the parent glycosylates all of its heavy chains, M3.11 does not attach any carbohydrate to 30 to 50% of its heavy chains. These non-glycosylated heavy chains are, nonetheless, assembled and secreted with similar kinetics to the glycosylated heavy chain.
AB - Two stable mutant cell lines derived from the MPC-11 mouse myeloma synthesize immunoglobulin with abnormal heavy chains and normal light chains. The mutant heavy chains have molecular weights of 38,000 to 42,000 (M3.11) and 50,000 (ICR 11.19) as compared to 55,000 of the wild type. The mutants demonstrate a variety of blocks in the assembly, glycosylation and secretion of immunoglobulin. (1) The wild type assembles and secretes 90% of its immunoglobulin primarily as H2L2 while M3.11 is partially blocked in the assembly of H2L2, and secretes approximately one half of its immunoglobulin as HL. ICR 11.19, with a more complete block in interchain disulfide bond formation, assembles less than 10% of its immunoglobulin into H2L2, has a block in secretion and degrades most of its immunoglobulin. (2) M3.11 uses only one of the two wild type pathways of assembly. Reduction of isolated H2L2 with 2-mercapthoethanol suggests an altered stability of the inter-H chain disulfide bonds in M3.11 as compared to the wild type immunoglobulin. (3) While the parent glycosylates all of its heavy chains, M3.11 does not attach any carbohydrate to 30 to 50% of its heavy chains. These non-glycosylated heavy chains are, nonetheless, assembled and secreted with similar kinetics to the glycosylated heavy chain.
UR - http://www.scopus.com/inward/record.url?scp=0017283463&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0017283463&partnerID=8YFLogxK
U2 - 10.1016/S0022-2836(76)80051-4
DO - 10.1016/S0022-2836(76)80051-4
M3 - Article
C2 - 818392
AN - SCOPUS:0017283463
SN - 0022-2836
VL - 102
SP - 237
EP - 252
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 2
ER -