Identification of a Family of Insulin-Like Growth Factor II Secreted by Cultured Rat Epithelial-Like Cell Line 18,54-SF: Application of a Monoclonal Antibody

Tanaka, Hideyuki; Asami, Osamu; Hayano, Tomohiko; Sasaki, Ikuharu; Yoshitake, Yoshino; Nishikawa, Katsuzo

doi:10.1210/endo-124-2-870

Cited by 46 publications

(13 citation statements)

References 30 publications

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“…Although insufficient amounts of material were available for fur-ther characterization, we have found that all of these forms dilute in parallel in the IGF-II radioimmunoassay. Several similar peptides have been detected in the serum, tissue or cell culture medium (12, [34][35][36][37]. Our results are consistent with those of Gowan et al who showed that an unusual, intermediate molecular weight form of IGF-II isolated from human serum Cohn fraction IV associated with serum binding proteins with the same affinity as that exhibited by IGF-II itself (36).…”

Section: Subjectssupporting

confidence: 89%

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

Shapiro¹,

Bell²,

Polonsky³

et al. 1990

J. Clin. Invest.

117

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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: Subjectssupporting

confidence: 89%

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

Shapiro¹,

Bell²,

Polonsky³

et al. 1990

J. Clin. Invest.

117

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“…For the assay, Amano monoclonal antibody generated against rat IGF-II (10 ,ug ml-') was used at a final dilution of 1:14 285 (Amano Enzymes USA, Troy, VA, USA). This antibody cross-reacts 100% with human and rat IGF-II and 10% with human IGF-I (Tanaka et al, 1989).…”

Section: Radioimmunoassays Of Gh Igf-i and Igf-iimentioning

confidence: 98%

Inhibition of in vivo proliferation of androgen-independent prostate cancers by an antagonist of growth hormone-releasing hormone

Jungwirth

Schally²,

Pinski³

et al. 1997

Br J Cancer

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Summary Tumour-inhibitory effects of a new antagonist of growth hormone-releasing hormone (GH-RH), MZ-4-71, were evaluated in nude mice bearing androgen-independent human prostate cancer cell lines DU-145 and PC-3 and in Copenhagen rats implanted with Dunning R-3327 AT-1 prostatic adenocarcinoma. After 6 weeks of therapy, the tumour volume in nude mice with DU-1 45 prostate cancers treated with 40 ,ug day-' MZ-4-71 was significantly decreased to 37 ± 13 mm3 (P < 0.01) compared with controls that measured 194 ± 35 mm3. A similar inhibition of tumour growth was obtained in nude mice bearing PC-3 cancers, in which the treatment with MZ-4-71 for 4 weeks diminished the tumour volume to 1 19 ± 35 mm3 compared with 397 ± 115 mm3 for control animals. Therapy with MZ-4-71 also significantly decreased weights of PC-3 and DU-145 tumours and increased tumour doubling time. Serum levels of GH and IGF-I were significantly decreased in animals treated with GH-RH antagonist. In PC-3 tumour tissue, the levels of IGF-I and IGF-II were reduced to non-detectable values after therapy with MZ-4-71. The growth of Dunning R-3327 AT-1 tumours in rats was also significantly inhibited after 3 weeks of treatment with 100 gg of MZ-4-71 day-' i.p. as shown by a reduction in tumour volume and weight (both P-values < 0.05). Specific high-affinity binding sites for IGF-I were found on the membranes of DU-145, PC-3 and Dunning R-3327 AT-1 tumours. Our results indicate that GH-RH antagonist MZ-4-71 suppresses growth of PC-3, DU-145 and Dunning AT-I androgen-independent prostate cancers, through diminution of GH release and the resulting decrease in the secretion of hepatic IGF-I, or through mechanisms involving a lowering of tumour IGF-I levels and possibly an inhibition of tumour IGF-I and IGF-Il production. GH-RH antagonists could be considered for further development for the therapy of prostate cancer, especially after the relapse.

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“…Recombinant human IGF2 was used as standard and as tracer. An equilibrium assay was established using monoclonal anti-rat IGF2 antibody at 2.5 ng/tube (Tanaka et al 1989). The antibody shows 100% cross-reactivity with human IGF2 and < 10% reactivity with human IGF1 {Amano Enzymes USA Co., Troy, VA1.…”

Section: Igf2 Radioimmunoassaymentioning

confidence: 99%

Loss of the imprinted IGF2/cation-independent mannose 6-phosphate receptor results in fetal overgrowth and perinatal lethality.

Lau¹,

Stewart²,

Liu³

et al. 1994

Genes Dev.

554

325

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Murine embryos that inherit a nonfunctional insulin-like growth factor-If/cation-independent mannose 6-phosphate receptor (Igf2r) gene from their fathers are viable and develop normally into adults. However, the majority of mice inheriting the same mutated allele from their mothers die around birth, as a consequence of major cardiac abnormalities. These mice do not express IGF2R in their tissues, are 25-30% larger than their normal siblings, have elevated levels of circulating IGF2 and IGF-binding proteins, and exhibit a slight kink in their tails. These results show that lgf2r is paternally imprinted and reveal that the receptor is crucial for regulating normal fetal growth, circulating levels of IGF2, and heart development.

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Identification of a Family of Insulin-Like Growth Factor II Secreted by Cultured Rat Epithelial-Like Cell Line 18,54-SF: Application of a Monoclonal Antibody

Cited by 46 publications

References 30 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.

Inhibition of in vivo proliferation of androgen-independent prostate cancers by an antagonist of growth hormone-releasing hormone

Loss of the imprinted IGF2/cation-independent mannose 6-phosphate receptor results in fetal overgrowth and perinatal lethality.

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