Multiple soluble vertebrate galactoside-binding lectins

Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anchorage and cell transformation

“…Notably, Ras and galectin-1 were also released by DTT from Ras-immunoreactive complexes with Mr values higher than 34 ± 43 kDa (Figure 2c), such as those already observed in the early puri®cation steps (Figure 1a). These results are consistent with the possible existence of higher orders of H-Ras(12V)-galectin-1 complexes, including galectin-1 dimers (Barondes et al, 1994;Cho and Cummings, 1995;Wells and Mallucci, 1991) with Ras and Ras dimers (Inouye et al, 2000) with galectin-1. Consistent with the above noted observations, we found cross-linked galectin-1-H-Ras(12V) in membranes of cells treated with 100 mM lactose (Figure 2d), known to prevent binding of galectin-1 to glycosylated proteins (Wells and Mallucci, 1991).…”

Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anchorage and cell transformation

“…Notably, Ras and galectin-1 were also released by DTT from Ras-immunoreactive complexes with Mr values higher than 34 ± 43 kDa (Figure 2c), such as those already observed in the early puri®cation steps (Figure 1a). These results are consistent with the possible existence of higher orders of H-Ras(12V)-galectin-1 complexes, including galectin-1 dimers (Barondes et al, 1994;Cho and Cummings, 1995;Wells and Mallucci, 1991) with Ras and Ras dimers (Inouye et al, 2000) with galectin-1. Consistent with the above noted observations, we found cross-linked galectin-1-H-Ras(12V) in membranes of cells treated with 100 mM lactose (Figure 2d), known to prevent binding of galectin-1 to glycosylated proteins (Wells and Mallucci, 1991).…”

Fungal Galectins, Sequence and Specificity of Two Isolectins from Coprinus cinereus

“…The carbohydrate-binding specificity of recombinant Cgl-II is very similar to the specificities reported for other galectins (1). As with all other galectins, only galactoside, and especially lactoside, sugars competed for the lectin binding site.…”

Dimeric Galectin-8 Induces Phosphatidylserine Exposure in Leukocytes through Polylactosamine Recognition by the C-terminal Domain

“…However, unlike Gal-1, Gal-2, and Gal-3, which form homo-oligomeric structures required for cellular signaling (6), the oligomeric structure of Gal-8 and the contributions of each CRD required for cell signaling toward leukocytes are not well understood. Gal-8 is currently thought to exist as a monomer with each CRD joined by a common linker region, providing functional bivalency (32)(33)(34). However, the two separate CRDs of Gal-8 share little sequence similarity (34), consistent with preliminary findings that each domain likely recognizes distinct ligands (29,35).…”

Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anchorage and cell transformation

“…Notably, Ras and galectin-1 were also released by DTT from Ras-immunoreactive complexes with Mr values higher than 34 ± 43 kDa (Figure 2c), such as those already observed in the early puri®cation steps (Figure 1a). These results are consistent with the possible existence of higher orders of H-Ras(12V)-galectin-1 complexes, including galectin-1 dimers (Barondes et al, 1994;Cho and Cummings, 1995;Wells and Mallucci, 1991) with Ras and Ras dimers (Inouye et al, 2000) with galectin-1. Consistent with the above noted observations, we found cross-linked galectin-1-H-Ras(12V) in membranes of cells treated with 100 mM lactose (Figure 2d), known to prevent binding of galectin-1 to glycosylated proteins (Wells and Mallucci, 1991).…”

Fungal Galectins, Sequence and Specificity of Two Isolectins from Coprinus cinereus

“…The carbohydrate-binding specificity of recombinant Cgl-II is very similar to the specificities reported for other galectins (1). As with all other galectins, only galactoside, and especially lactoside, sugars competed for the lectin binding site.…”

Dimeric Galectin-8 Induces Phosphatidylserine Exposure in Leukocytes through Polylactosamine Recognition by the C-terminal Domain

“…However, unlike Gal-1, Gal-2, and Gal-3, which form homo-oligomeric structures required for cellular signaling (6), the oligomeric structure of Gal-8 and the contributions of each CRD required for cell signaling toward leukocytes are not well understood. Gal-8 is currently thought to exist as a monomer with each CRD joined by a common linker region, providing functional bivalency (32)(33)(34). However, the two separate CRDs of Gal-8 share little sequence similarity (34), consistent with preliminary findings that each domain likely recognizes distinct ligands (29,35).…”

Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anchorage and cell transformation

“…Notably, Ras and galectin-1 were also released by DTT from Ras-immunoreactive complexes with Mr values higher than 34 ± 43 kDa (Figure 2c), such as those already observed in the early puri®cation steps (Figure 1a). These results are consistent with the possible existence of higher orders of H-Ras(12V)-galectin-1 complexes, including galectin-1 dimers (Barondes et al, 1994;Cho and Cummings, 1995;Wells and Mallucci, 1991) with Ras and Ras dimers (Inouye et al, 2000) with galectin-1. Consistent with the above noted observations, we found cross-linked galectin-1-H-Ras(12V) in membranes of cells treated with 100 mM lactose (Figure 2d), known to prevent binding of galectin-1 to glycosylated proteins (Wells and Mallucci, 1991).…”

Fungal Galectins, Sequence and Specificity of Two Isolectins from Coprinus cinereus

“…The carbohydrate-binding specificity of recombinant Cgl-II is very similar to the specificities reported for other galectins (1). As with all other galectins, only galactoside, and especially lactoside, sugars competed for the lectin binding site.…”

Dimeric Galectin-8 Induces Phosphatidylserine Exposure in Leukocytes through Polylactosamine Recognition by the C-terminal Domain

“…However, unlike Gal-1, Gal-2, and Gal-3, which form homo-oligomeric structures required for cellular signaling (6), the oligomeric structure of Gal-8 and the contributions of each CRD required for cell signaling toward leukocytes are not well understood. Gal-8 is currently thought to exist as a monomer with each CRD joined by a common linker region, providing functional bivalency (32)(33)(34). However, the two separate CRDs of Gal-8 share little sequence similarity (34), consistent with preliminary findings that each domain likely recognizes distinct ligands (29,35).…”