Cold-Insoluble Globulin and Its Interaction with Fibrinogen

2015 ◽  
pp. 145-150
Author(s):  
Nils Olav Solum ◽  
Ole Fyrand ◽  
Peter Kierulf
Keyword(s):  
Cold Insoluble Globulin

scholarly journals The structure and stability of human plasma cold-insoluble globulin.

1979 ◽  
Vol 254 (5) ◽  
pp. 1501-1505 ◽  
Author(s):  
S.S. Alexander ◽  
G. Colonna ◽  
H. Edelhoch
Keyword(s):  
Human Plasma ◽  
Structure And Stability ◽  
Cold Insoluble Globulin

scholarly journals Receptors for cold-insoluble globulin (plasma fibronectin) on human monocytes.

1981 ◽  
Vol 153 (1) ◽  
pp. 42-60 ◽  
Author(s):  
M P Bevilacqua ◽  
D Amrani ◽  
M W Mosesson ◽  
C Bianco
Keyword(s):  
Cell Attachment ◽  
Divalent Cations ◽  
Binding Activity ◽  
Membrane Receptors ◽  
Human Monocytes ◽  
Plasma Fibronectin ◽  
Blood Monocytes ◽  
Cold Insoluble Globulin ◽  
Particle Ingestion ◽  
Coated Surfaces

This investigation focused on the role played by cold-insoluble globulin (CIg, plasma fibronectin) in monocyte function. Surface-bound CIg mediated a concentration-dependent of human blood monocytes to gelatin-coated surfaces. CIg also mediated the binding of gelatin-coated particles such as latex beads or tanned erythrocytes to surface-bound human monocytes. However, CIg did not mediate particle ingestion. Subfractionated CIg that was highly enriched in monomeric forms (zone II CIg, mol wt 190,000-235,000) was less effective than were fractions enriched in dimeric forms (zone I CIg, mol wt 450,000) in promoting monocyte attachment. Binding of CIg to a gelatin or plastic surface occurred in the absence of divalent cations, but monocyte attachment to CIg-coated surfaces required divalent cations, Mg++ being much more effective than Ca++. Cation-dependent cell attachment was reversible in that bound cells could be released by treatment with EDTA. Serum-mediated binding of monocytes to gelatin-coated plastic dishes was a result of its content of CIg because the binding activity was abolished by removal of CIg from serum, and could be restored by readdition of purified CIg. Treatment of monocytes with trypsin abolished subsequent cell attachment to CIg-gelatin surfaces or particles. Expression of certain other known monocyte membrane receptors (Fc and C3b) was markedly enhanced as a result of CIg-monocyte interaction. These several observations indicate that monocytes bear membrane receptors (termed receptor cold-insoluble globulin) for surface-bound CIg.

scholarly journals Amniotic fluid fibronectin. Characterization and synthesis by cells in culture.

1978 ◽  
Vol 78 (3) ◽  
pp. 701-715 ◽  
Author(s):  
E Crouch ◽  
G Balian ◽  
K Holbrook ◽  
D Duksin ◽  
P Bornstein
Keyword(s):  
Amniotic Fluid ◽  
Matrix Protein ◽  
Sodium Dodecyl ◽  
Basement Membranes ◽  
The Body ◽  
Connective Tissues ◽  
Human Amniotic Fluid ◽  
Cold Insoluble Globulin ◽  
Kinetics Of

A glycoprotein immunologically related to plasma cold-insoluble globulin (CIG) and fetal skin fibroblast fibronectin has been purified from second-trimester human amniotic fluid. This protein (amniotic fluid fibronectin) migrated more slowly than CIG on sodium dodecyl sulfate gel electrophoresis and showed greater polydispersity which could result, at least in part, from heterogeneity in glycosylation. Cloned human amniotic fluid epithelioid and fibroblastic cells synthesized and secreted a protein with similar properties into the culture medium. Fibronectin was shown to be associated with the pericellular and extracellular matrix of cultured amniotic fluid cells by immunofluorescence, lactoperoxidase-catalyzed iodination, and labeling with ferritin-conjugated antibodies. The kinetics of secretion of the protein were consistent with its role as a matrix protein. We anticipate that amniotic fluid fibronectin will prove to be the same protein which elsewhere in the body is incorporated into connective tissues and basement membranes. Amniotic fluid could, therefore, serve as a convenient source of in vivo synthesized fibronectin for biological and structural studies.

scholarly journals Interaction of soluble fibroblast surface antigen with fribrinogen and fibrin.

1975 ◽  
Vol 141 (2) ◽  
pp. 497-501 ◽  
Author(s):  
E Ruoslahti ◽  
A Vaheri
Keyword(s):  
Human Plasma ◽  
Low Temperatures ◽  
Serum Proteins ◽  
Biological Significance ◽  
Cell Type ◽  
Fold Enrichment ◽  
Glycoprotein Antigen ◽  
A Cell ◽  
Cell Type Specific ◽  
Cold Insoluble Globulin

A cell-type specific glycoprotein antigen (SFA) from fibroblast surface appears in human plasma and serum. The amount of SFA in serum was reduced if the blood coagulation clot was removed at a low temperature. SFA could be bound to Sepharose-conjugated fibrinogen and to fibrin powder at 0 degrees C and was subsequently released when the temperature was elevated to plus 37 degrees C. This procedure resulted in a 10-fold enrichment of SFA relative to other serum proteins. SFA was found to be concentrated in the cryoprecipitate fraction of human plasma and was copurified with the cold insoluble globulin (CIG) with procedures published for the purification of the latter component. SFA/CIG is not soluble at low temperatures as such and its appearance in the cryoprecipitate fraction of plasma is likely to be due to its affinity to cryofibrinogen evident from these experiments. The biological significance of the interaction of fibroblast surface SFA moleculres with fibrin(ogen) is not known.

Structural Studies of the Sugar Chains of Cold-Insoluble Globulin Isolated from Human Plasma1

1980 ◽  
Vol 88 (6) ◽  
pp. 1587-1594 ◽  
Author(s):  
Seiichi TAKASATA ◽  
Katsuko YAMASHITA ◽  
Koji SUZUKI ◽  
AKIRA KOBATA
Keyword(s):  
Structural Studies ◽  
Cold Insoluble Globulin ◽  
Sugar Chains

Similarity of antigelatin factor and cold insoluble globulin

1978 ◽  
Vol 533 (1) ◽  
pp. 227-237 ◽  
Author(s):  
Waltraud Dessau ◽  
Franz Jilek ◽  
Bernhard C. Adelmann ◽  
Helmut Hörmann
Keyword(s):  
Cold Insoluble Globulin

scholarly journals Isolation and characterization of Chinese hamster ovary cell variants defective in adhesion to fibronectin-coated collagen.

1980 ◽  
Vol 87 (3) ◽  
pp. 755-763 ◽  
Author(s):  
P A Harper ◽  
R L Juliano
Keyword(s):  
Chinese Hamster Ovary ◽  
Cho Cells ◽  
Divalent Cations ◽  
Chinese Hamster ◽  
Ovary Cell ◽  
Human Diploid Fibroblasts ◽  
Isolation And Characterization ◽  
A Cell ◽  
Cold Insoluble Globulin

Variant clones of Chinese hamster ovary (CHO) cells were selected for reduced adhesion to serum-coated tissue culture plates. These clones also displayed reduced adhesion to substrata composed of collagen layers coated with bovine serum or with fibronectin (cold-insoluble globulin). Wild-type (WT) and adhesion variant (ADv) cells grew at comparable rates in suspension culture, but the adhesion variants could not be grown in monolayer culture because of their inability to attach to the substratum. The adhesion deficit in these cells was not corrected by raising the concentration of divalent cations or of serum to levels 10-fold greater than those normally utilized in cell culture. However, both WT and ADv clones could adhere, spread, and attain a normal CHO morphology on substrata coated with concanavalin A or poly-L-lysine. In addition, the adhesion variants could attach to substrata coated with "footpad" material (substratum-attached material) derived from monolayers of human diploid fibroblasts or WT CHO cells. These observations suggest that the variant clones may have a cell surface defect that prevents them from utilizing exogeneous fibronectin as an adhesion-promoting ligand; however the variants seem to have normal cytoskeletal and metabolic capacities that allow them to attach and spread on substrata coated with alternative ligands. These variants should be extremely useful in studying the molecular basis of cell adhesion.

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