PMID- 2999161
OWN - NLM
STAT- MEDLINE
DCOM- 19860103
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 1540-8140 (Electronic)
IS  - 0021-9525 (Linking)
VI  - 101
IP  - 6
DP  - 1985 Dec
TI  - Cell anchorage determines whether mammary tumor virus glycoproteins are processed 
      for plasma membranes or secretion.
PG  - 2274-83
AB  - The subcellular localization of mouse mammary tumor virus (MMTV) glycoproteins 
      was analyzed in infected and cloned rat hepatocarcinoma cells cultured with the 
      MMTV transcriptional inducer dexamethasone. When reacted with protein A-coated 
      erythrocytes in the presence of antisera specific for viral glycoproteins or with 
      fluorescent antisera, only some of the cells acquired surface label. This 
      diversity was dependent on cell anchorage to the substratum. In general, the more 
      rounded, less adherent cells contained the MMTV glycoproteins on their surfaces, 
      whereas the flatter, more adherent cells did not. After a change in adherence, a 
      delay preceded complete remodeling of the plasma membranes. Fluorescent antibody 
      studies of fixed cells and analyses of viral glycoprotein synthesis and shedding 
      using L-[35S]methionine indicated that the different expression of MMTV 
      glycoproteins in round versus flat cells is caused by a switch in 
      posttranslational processing. In round cells, the MMTV-encoded precursor 
      glycoprotein is proteolytically cleaved and then transported to plasma membranes 
      as a complex of two subunits, the smaller being the membrane anchor. In flat 
      adherent cells, the smaller subunit is rapidly degraded in an intracellular 
      organelle and the larger is then secreted into the medium. As indicated by 
      labeling of cells with 125I, the concentrations of several host-encoded plasma 
      membrane components are also influenced by cell anchorage. We propose that this 
      switch in cell surfaces and in secretions dependent upon cell-substratum 
      attachments may be a common control mechanism important for embryogenesis, wound 
      healing, and cancer.
FAU - Kabat, D
AU  - Kabat D
FAU - Gliniak, B
AU  - Gliniak B
FAU - Rohrschneider, L
AU  - Rohrschneider L
FAU - Polonoff, E
AU  - Polonoff E
LA  - eng
GR  - CA 20551/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Glycoproteins)
RN  - 0 (Iodoproteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Viral Proteins)
RN  - 7S5I7G3JQL (Dexamethasone)
SB  - IM
MH  - Animals
MH  - Biological Transport
MH  - *Cell Adhesion
MH  - Cell Compartmentation
MH  - Cell Membrane/*metabolism
MH  - Cells, Cultured
MH  - Dexamethasone/pharmacology
MH  - Fluorescent Antibody Technique
MH  - Glycoproteins/*metabolism
MH  - Iodoproteins/analysis
MH  - Mammary Tumor Virus, Mouse/*metabolism
MH  - Membrane Proteins/*metabolism
MH  - Mice
MH  - Molecular Weight
MH  - Protein Processing, Post-Translational
MH  - Rats
MH  - Viral Proteins/*metabolism
PMC - PMC2114026
EDAT- 1985/12/01 00:00
MHDA- 1985/12/01 00:01
PMCR- 1986/06/01
CRDT- 1985/12/01 00:00
PHST- 1985/12/01 00:00 [pubmed]
PHST- 1985/12/01 00:01 [medline]
PHST- 1985/12/01 00:00 [entrez]
PHST- 1986/06/01 00:00 [pmc-release]
AID - 86059678 [pii]
AID - 10.1083/jcb.101.6.2274 [doi]
PST - ppublish
SO  - J Cell Biol. 1985 Dec;101(6):2274-83. doi: 10.1083/jcb.101.6.2274.