Corrigendum

Shoelson, S.; Haneda, M.; Blix, P.; Nanjo, A.; Sanke, T.; Inouye, K.; Steiner, D.; Rubenstein, A.; Tager, H.

doi:10.1038/304754b0

Cited by 2 publications

(2 citation statements)

References 7 publications

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“…IGF-II immunoreactivity as well as optical absorbance at 275 nm was measured in each fraction. Fraction numbers 56, 64, and 70 from the resulting elution profile of higher molecular weight IGF-II material and fraction number 78 from the lower molecular weight profile were lyophilized and then further analyzed by reverse-phase HPLC in a gradient of 20-40% acetonitrile in triethylammonium phosphate buffer over 60 min as previously described (26). l-ml fractions were collected and IGF-I1 immunoreactivity was determined in each fraction.…”

Section: Subjectsmentioning

confidence: 99%

Tumor hypoglycemia: relationship to high molecular weight insulin-like growth factor-II.

Shapiro¹,

Bell²,

Polonsky³

et al. 1990

J. Clin. Invest.

119

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The mechanism of tumor-associated hypoglycemia was examined in 11 patients with hepatocellular carcinoma, 6 of whom presented with severe hypoglycemia and 5 in whom plasma glucose was persistently normal. Serum insulin levels in the hypoglycemic patients were low. Although total serum insulinlike growth factor II (IGF-II) levels in both groups of tumor patients were lower than normal, tumor tissue from hypoglycemic patients contained levels of IGF-II mRNA that were 10-20-fold higher than those present in normal liver.IGF-II immunoreactivity consisted in all cases of a mixture of both higher molecular weight forms and material having the character of IGF-II itself. The former comprised a greater proportion of total IGF-II, in patients with hypoglycemia. Studies to characterize the interactions of IGF-II with serum proteins showed that (a) the radiolabeled peptide bound to an -40,000-D protein in sera from both hypoglycemic patients and normal subjects, (b) sera from hypoglycemic patients and normal subjects had similar capacity to bind the radiolabeled peptide, and (c) the apparent affinities of serum binding proteins for IGF-II were the same for both hypoglycemic patients and normal subjects. Whereas, acid extracted, tumor-derived IGF-II immunoreactive peptides with low or intermediate molecular weights bound to serum proteins in a manner indistinguishable from that of IGF-II itself, the highest molecular weight IGF-II immunoreactive peptide exhibited negligible ability to compete for radiolabeled ligand binding to serum proteins. The low affinity of serum binding proteins for this component suggests that high molecular weight IGF-II immunoreactivity might circulate free and be available for interaction with cell-surface receptors. (J. Clin. Invest. 1990.

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Section: Subjectsmentioning

confidence: 99%

Tumor hypoglycemia: relationship to high molecular weight insulin-like growth factor-II.

Shapiro¹,

Bell²,

Polonsky³

et al. 1990

J. Clin. Invest.

119

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“…Recently, another mechanism underlying impaired insulin action, has emerged from the work of Tager et al [3], who found that insulin isolated from the pancreas of a diabetic patient with elevated levels of circulating insulin showed decreased activity in hormone binding to cell-membrane insulin receptors, because of the presence of an abnormal variant of insulin, which contained a leucine for pheny-lalanine substitution at position 24 or 25 of the insulin B-chain. Subsequent to this work, three chemically distinct mutant insulins have been identified in patients with NIDDM, each involving a substitution of either B24 of B25 phenylalanine [4]. Out of these, two have been unambiguously characterized -B25(Phe -j Leu) and B24(Phe -+ Ser).…”

Section: Introductionmentioning

confidence: 97%

Conformational basis of the receptor-binding potency of normal and mutant insulin molecules with relevance to the pathophysiology of noninsulin dependent diabetes mellitus (NIDDM)

Rao

Bajaj

1988

Int. J. Quantum Chem.

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Residues 23-26 (Gly-, Phe-, Phe-, Tyr) of the B-chain of insulin constitute a critical area of the receptorbinding region of the molecule. Three chemically distinct mutant insulins have recently been identified in patients with NIDDM, each involving substitution of either B24 of 825 phenylalanine. Two of the mutations have been unambiguously characterized: a B25 phenylalanine-to-leucine substitution [B25(Phe + Leu)], and the other, a B24 phenylalanine-to-serine [B24 (Phe -+ Ser)]. We have calculated the preferred conformations of normal and mutant insulins using a global optimization method developed by us earlier. The mutant insulins exhibit significant alterations in conformation and in the average distances between amino acid side-chains as compared to normal insulin. Therefore, the decreased binding affinity of mutant insulin could be either due to an alteration in the nature of the substituted residue (hydrophilic in place of hydrophobic) or to the alteration in one or more critical side-chain distances in the case of a hydrophobic to hydrophobic substitution.

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Corrigendum

Abstract: T1ble :Z Elastic properties of defined length DNA helices Sample poly( dO) · poly(dC) poly(dA-dC) · poly(dT -dG) Chicken DNA poly(dA) · poly(dT) poly(dG) · poly(dC) poly(dA -dC) ·poly( dT -dG) Chicken DNA poly(dA) · poly(dT) poly(dG) · poly(dC)

Cited by 2 publications

References 7 publications

Tumor hypoglycemia: relationship to high molecular weight insulin-like growth factor-II.

Tumor hypoglycemia: relationship to high molecular weight insulin-like growth factor-II.

Conformational basis of the receptor-binding potency of normal and mutant insulin molecules with relevance to the pathophysiology of noninsulin dependent diabetes mellitus (NIDDM)

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