Dissociation kinetics of 125I-nerve growth factor from cell surface receptors. Acceleration by unlabeled ligand and its relationship to negative cooperativity.

Tait, Jonathan F.; Weinman, Steven A.; Bradshaw, R A

doi:10.1016/s0021-9258(19)68559-5

Cited by 49 publications

(3 citation statements)

References 28 publications

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“…The addition of either aNGF, 7NGF, or unlabeled 0NGF has basically the same effect on the kinetics of 125I-0NGF dissociation (Table II) or on the cold chase stable bound ,25I-/3NGF (Table III). This observation has relevance to the discussion of positive cooperativity with PC 12 cells and to the discussion of negative cooperativity and unstirred layer effects with NGF receptors, done primarily with neurons (Frazier et al, 1974;Sutter et al, 1979;Olender & Stach, 1980;Riopelle et al, 1980;Tail et al, 1981). The enhanced rate of dissociation seen with a chase experiment compared to dilution (Yankner & Shooter, 1979;Neet et al, 1984) cannot be due to negative cooperativity in the PC 12 system since addition of aNGF or 7NGF would not fill empty 5NGF receptors to enhance dissociation, as proposed by the negative cooperativity model.…”

Section: Discussionmentioning

confidence: 82%

Inhibition of .beta. nerve growth factor binding to PC12 cells by .alpha. nerve growth factor and .gamma. nerve growth factor

Woodruff¹,

Neet²

1986

Biochemistry

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Pheochromocytoma (PC12) cells have been found to differ from dorsal root ganglionic cells with respect to the modulation of the beta nerve growth factor (beta NGF) binding properties elicited by alpha NGF and gamma NGF. In contrast to our previous results with intact dorsal root ganglionic cells in which only high-affinity binding was blocked, alpha NGF and gamma NGF were found to block competitively all steady-state binding of iodinated beta NGF to PC12 cells at both 37 and 0.5 degrees C. The EC50 that was found for the alpha NGF displacement was 9-10 microM, and the gamma NGF effect had an EC50 of 200 nM, in the predicted range based upon the apparent Kd for dissociation of the alpha beta or the beta gamma complex in solution. The concurrence of the binding EC50 and the Kd for each complex indicates that the formation of alpha beta or beta gamma complexes in solution competes with the process of PC12 receptor binding with 125I-beta NGF. Experiments were carried out examining the dissociation kinetics following the addition of excess unlabeled beta NGF or alpha NGF at both 37 and 0.5 degrees C. Three dissociation components were observed with alpha NGF, in contrast to the two normally found with beta NGF. Lowering the chase temperature to 0.5 degrees C changed the relative contributions made by each component without dramatically changing any of the rate constants. The "slow" receptor was further examined by the dependence on 125I-beta NGF concentration of the slowest component with a chase of either excess alpha NGF or excess gamma NGF at 0.5 degrees C.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Discussionmentioning

confidence: 82%

Inhibition of .beta. nerve growth factor binding to PC12 cells by .alpha. nerve growth factor and .gamma. nerve growth factor

Woodruff¹,

Neet²

1986

Biochemistry

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“…IGF-II Cross-Linking. Human recombinant IGF-II (2 × 10 7 cpm/µg) was iodinated by the lactoperoxidase method as described by Tait et al (23). Purified Dom 7-11 (0.8 nM) was incubated with [ 125 I]IGF-II (10 nM) in cross-linking buffer [0.1 M HEPES (pH 8.0) and 0.1 M NaCl] in the presence or absence of a 100-fold molar excess of unlabeled IGF-II, IGF-I, or insulin for 2 h at room temperature.…”

Section: Methodsmentioning

confidence: 99%

Recognition of Dictyostelium discoideum Lysosomal Enzymes Is Conferred by the Amino-Terminal Carbohydrate Binding Site of the Insulin-like Growth Factor II/Mannose 6-Phosphate Receptor

et al. 2000

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The insulin-like growth factor-II/mannose 6-phosphate receptor (IGF-II/MPR) is a type I glycoprotein that mediates both the intracellular sorting of lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) residues to the lysosome and the bioavailability of IGF-II. The extracytoplasmic region of the IGF-II/MPR contains 15 repeating domains; the two carbohydrate recognition domains (CRDs) have been localized to domains 1-3 and 7-9, and the high-affinity IGF-II binding site maps to domain 11. To characterize the carbohydrate binding properties of the IGF-II/MPR, regions of the receptor encompassing the individual CRDs were produced in a baculovirus expression system. Characterization of the recombinant proteins revealed that the pH optimum for carbohydrate binding is significantly more acidic for the carboxyl-terminal CRD than for the amino-terminal CRD (i.e., pH 6.4-6.5 vs 6.9). Equilibrium binding studies demonstrated that the two CRDs exhibit a similar affinity for Man-6-P. Furthermore, substitution of the conserved arginine residue in domain 3 (R435) or in domain 9 (R1334) with alanine resulted in a similar >1000-fold decrease in the affinity for the lysosomal enzyme, beta-glucuronidase. In contrast, the two CRDs differ dramatically in their ability to recognize the distinctive modifications (i.e., mannose 6-sulfate and Man-6-P methyl ester) found on Dictyostelium discoideum lysosomal enzymes: the amino-terminal CRD binds mannose 6-sulfate and Man-6-P methyl ester with a 14-55-fold higher affinity than the carboxyl-terminal CRD. Taken together, these results demonstrate that the IGF-II/MPR contains two functionally distinct CRDs.

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“…30/~g ~-glucuronidase was iodinated with 1 mCi of 125I-Na using soluble lactoperoxidase as described (30). The iodination reaction was applied to a 1.0 x 110 cm Sephadex G-150 column that was previously equilibrated with 0.05 M NaPO4, pH 7.6, 0.15 M NaCI, and 1 mg/ml BSA.…”

Section: Purification and Lodination Of ~-Glucuronidasementioning

confidence: 99%

The cytoplasmic tail of the mannose 6-phosphate/insulin-like growth factor-II receptor has two signals for lysosomal enzyme sorting in the Golgi.

Johnson

Kornfeld

1992

The Journal of Cell Biology

220

115

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Abstract. The mannose 6-phosphate/insulin-like growth factor-II (Man-6-P/IGF-II) receptor is known to cycle between the Golgi, endosomes, and the plasma membrane. In the Golgi the receptor binds newly synthesized lysosomal enzymes and transports them directly to an endosomal (prelysosomal) compartment without traversing the plasma membrane. Deletion of the carboxyl-terminal Leu-Leu-His-Val residues of the 163 amino acid cytoplasmic tail of the bovine Man-6-P/IGF-II receptor partially impaired this function, resulting in the diversion of a portion of the receptor-ligand complexes to the cell surface, where they were endocytosed. The same phenotype was observed when 134 residues of the cytoplasmic tail were deleted from the carboxyl terminus. Disruption of the Tyr24-Lys-Tyr-Ser-Lys-Va129 plasma membrane internalization signal alone had little effect on Golgi sorting, but when combined with either deletion resulted in a complete loss of this function. The mutant receptors retained the ability to recycle to the Golgi and bind cathepsin D. These results indicate that the cytoplasmic tail of the Man-6-P/IGF-II receptor contains two signals that contribute to Golgi sorting, presumably by interacting with the Golgi clathrin-coated pit adaptor proteins. The Leu-Leu-containing sequence represents a novel motif for mediating interaction with Golgi adaptor proteins.

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Dissociation kinetics of 125I-nerve growth factor from cell surface receptors. Acceleration by unlabeled ligand and its relationship to negative cooperativity.

Cited by 49 publications

References 28 publications

Inhibition of .beta. nerve growth factor binding to PC12 cells by .alpha. nerve growth factor and .gamma. nerve growth factor

Inhibition of .beta. nerve growth factor binding to PC12 cells by .alpha. nerve growth factor and .gamma. nerve growth factor

Recognition of Dictyostelium discoideum Lysosomal Enzymes Is Conferred by the Amino-Terminal Carbohydrate Binding Site of the Insulin-like Growth Factor II/Mannose 6-Phosphate Receptor

The cytoplasmic tail of the mannose 6-phosphate/insulin-like growth factor-II receptor has two signals for lysosomal enzyme sorting in the Golgi.

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