Immunoglobulin biosynthesis by the MOPC 173 mouse myeloma tumor and a variant spleen clone

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

The IgG2a producing MOPC 173 tumor synthesizes heavy (H) and light (L) chains and assembles them into H2L2 utilizing heavy chain dimers (H2) and H2L as the major precursors. Although the tumor cells secrete only H2L2, they synthesize excess L chains which appear to be degraded and are not secreted. A L chain producing variant arising spontaneously from the MOPC 173 tumor also failed to secrete any L chains. MOPC 173 tumor cells were cloned in the spleens of normal BALB/c mice and 1 of 23 spleen clones appeared to differ from the parent tumor in demonstrating a transient block in the assembly of H2L2 at the H2 level, leading to delayed formation and secretion of H2L2, appreciable amounts of non covalently bonded H2L, an abnormal intracellular immunoglobulin species, H4, and production of equimolar amounts of H and L chains. The patterns of immunoglobulin synthesis and assembly demonstrable in the above studies were also observed when tumor cells were studied in situ. Tryptic peptide mapping of the H and L chains produced by the MOPC 173 tumor and the variant spleen clone failed to demonstrate any differences in the H chains, but there were definite chemical differences in the L chains. These studies indicate that variant myeloma cells producing structurally altered immunoglobulins may continually be arising in myeloma tumors.

Original languageEnglish (US)
Pages (from-to)65-74
Number of pages10
JournalJournal of Immunology
Volume116
Issue number1
StatePublished - 1976
Externally publishedYes

Fingerprint

Immunoglobulins
Spleen
Clone Cells
Neoplasms
Peptide Mapping
myeloma protein MOPC 173
Light

ASJC Scopus subject areas

  • Immunology

Cite this

Immunoglobulin biosynthesis by the MOPC 173 mouse myeloma tumor and a variant spleen clone. / Baumal, R.; Scharff, Matthew D.

In: Journal of Immunology, Vol. 116, No. 1, 1976, p. 65-74.

Research output: Contribution to journalArticle

@article{d1bd5522d91a4caf8723ff80ca051487,
title = "Immunoglobulin biosynthesis by the MOPC 173 mouse myeloma tumor and a variant spleen clone",
abstract = "The IgG2a producing MOPC 173 tumor synthesizes heavy (H) and light (L) chains and assembles them into H2L2 utilizing heavy chain dimers (H2) and H2L as the major precursors. Although the tumor cells secrete only H2L2, they synthesize excess L chains which appear to be degraded and are not secreted. A L chain producing variant arising spontaneously from the MOPC 173 tumor also failed to secrete any L chains. MOPC 173 tumor cells were cloned in the spleens of normal BALB/c mice and 1 of 23 spleen clones appeared to differ from the parent tumor in demonstrating a transient block in the assembly of H2L2 at the H2 level, leading to delayed formation and secretion of H2L2, appreciable amounts of non covalently bonded H2L, an abnormal intracellular immunoglobulin species, H4, and production of equimolar amounts of H and L chains. The patterns of immunoglobulin synthesis and assembly demonstrable in the above studies were also observed when tumor cells were studied in situ. Tryptic peptide mapping of the H and L chains produced by the MOPC 173 tumor and the variant spleen clone failed to demonstrate any differences in the H chains, but there were definite chemical differences in the L chains. These studies indicate that variant myeloma cells producing structurally altered immunoglobulins may continually be arising in myeloma tumors.",
author = "R. Baumal and Scharff, {Matthew D.}",
year = "1976",
language = "English (US)",
volume = "116",
pages = "65--74",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "1",

}

TY - JOUR

T1 - Immunoglobulin biosynthesis by the MOPC 173 mouse myeloma tumor and a variant spleen clone

AU - Baumal, R.

AU - Scharff, Matthew D.

PY - 1976

Y1 - 1976

N2 - The IgG2a producing MOPC 173 tumor synthesizes heavy (H) and light (L) chains and assembles them into H2L2 utilizing heavy chain dimers (H2) and H2L as the major precursors. Although the tumor cells secrete only H2L2, they synthesize excess L chains which appear to be degraded and are not secreted. A L chain producing variant arising spontaneously from the MOPC 173 tumor also failed to secrete any L chains. MOPC 173 tumor cells were cloned in the spleens of normal BALB/c mice and 1 of 23 spleen clones appeared to differ from the parent tumor in demonstrating a transient block in the assembly of H2L2 at the H2 level, leading to delayed formation and secretion of H2L2, appreciable amounts of non covalently bonded H2L, an abnormal intracellular immunoglobulin species, H4, and production of equimolar amounts of H and L chains. The patterns of immunoglobulin synthesis and assembly demonstrable in the above studies were also observed when tumor cells were studied in situ. Tryptic peptide mapping of the H and L chains produced by the MOPC 173 tumor and the variant spleen clone failed to demonstrate any differences in the H chains, but there were definite chemical differences in the L chains. These studies indicate that variant myeloma cells producing structurally altered immunoglobulins may continually be arising in myeloma tumors.

AB - The IgG2a producing MOPC 173 tumor synthesizes heavy (H) and light (L) chains and assembles them into H2L2 utilizing heavy chain dimers (H2) and H2L as the major precursors. Although the tumor cells secrete only H2L2, they synthesize excess L chains which appear to be degraded and are not secreted. A L chain producing variant arising spontaneously from the MOPC 173 tumor also failed to secrete any L chains. MOPC 173 tumor cells were cloned in the spleens of normal BALB/c mice and 1 of 23 spleen clones appeared to differ from the parent tumor in demonstrating a transient block in the assembly of H2L2 at the H2 level, leading to delayed formation and secretion of H2L2, appreciable amounts of non covalently bonded H2L, an abnormal intracellular immunoglobulin species, H4, and production of equimolar amounts of H and L chains. The patterns of immunoglobulin synthesis and assembly demonstrable in the above studies were also observed when tumor cells were studied in situ. Tryptic peptide mapping of the H and L chains produced by the MOPC 173 tumor and the variant spleen clone failed to demonstrate any differences in the H chains, but there were definite chemical differences in the L chains. These studies indicate that variant myeloma cells producing structurally altered immunoglobulins may continually be arising in myeloma tumors.

UR - http://www.scopus.com/inward/record.url?scp=0017257748&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017257748&partnerID=8YFLogxK

M3 - Article

VL - 116

SP - 65

EP - 74

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 1

ER -