Antibody-Suppressible and Nonsuppressible Insulin-Like Activities in Human Serum and Their Physiologic Significance. An Insulin Assay With Adipose Tissue of Increased Precision and Specificity*

Froesch, E. R.; Bürgi, H; Ramseier, Erich; Bally, Peter R.; Labhart, A.

doi:10.1172/jci104866

Cited by 386 publications

(130 citation statements)

References 37 publications

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“…The connecting peptides of proinsulins differ much more widely than the corresponding A and B chains, both in length and in amino acid composition. It appears that either changes are selectively neutral in evolution (18) or, alternatively, the functional requirements for the connecting peptides differ widely (1,6,19).…”

Section: Resultsmentioning

confidence: 99%

Insulin-like growth factor: a model for tertiary structure accounting for immunoreactivity and receptor binding.

Blundell¹,

Bedarkar²,

Rinderknecht³

et al. 1978

Proc. Natl. Acad. Sci. U.S.A.

260

137

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A model for the three-dimensional structure of insulin-like growth factor (IGF) is proposed based on the close sequence homology of IGF with insulin, the tertiary structure of which is known. The IGF molecule is postulated to have an insulin-like main chain conformation for residues equivalent to B6-B27 and A1-A21 and a hydrophobic core nearly identical to that of insulin. A short connecting peptide of twelve residues and an extension at the COOH-terminus are easily accommodated on the molecular surface. MATERIALS AND METHODS The model was built in several stages. The proposed structure was first constructed using Lapquip model parts at a scale of 1 cm = 1 A. This was examined for unfavorable intramolecular contracts and readjusted before the coordinates of each atom were read off using a mechanical device. The approximate coordinates were then regularized using the "modelfit" computer program of Isaacs et al (12), and bond lengths and angles and other intramolecular distances were calculated using an IBM 360/65 computer. The model was then displayed on a computer graphics system (Digital Equipment Corp. graphics with a PDPll computer) using programs written by D. Richardson, P. Pauling, and C. Chothia, and adjustments were made using the interactive facilities of the graphics system to optimize the intramolecular distances. Finally, the model was regeometricized using "modelfit" and stereo pairs of the model were generated in hard copy. RESULTS AND DISCUSSIONThree-dimensional model for IGF I Table 1 shows the sequences of human IGF I, IGF II, and porcine insulin aligned so that the maximum homology is obtained. The numbering for the insulin A and B chains is indicated, as is the numbering for the IGF I polypeptide. The sequence of the IGF connecting peptide of 12 residues is also included, but because this shows no homology with the proinsulin connecting peptide, the latter is omitted. IGF I has an extension of eight residues at the COOH terminus of the A chain. Table 2 gives the differences in numbers of amino acids between the 51 amino acids of porcine insulin and the equivalent residues of other insulins, the protein hormone relaxin (13)(14)(15), which also appears to be homologous with insulin, and IGF.The sequence comparison shows a close homology for residues 5-25 of IGF (B6-B26 of insulin) and 42-61 (A1-A20). The arrangement of cystines is identical in IGF and insulin, and glycines 7 (B8), 19 (B20), and 22 (B23), which have dihedral angles that are disallowed for residues with side chains, are conserved, so that the polypeptide backbone can assume the same three-dimensional structure as insulin. We began by building the sequence 5-26 and 42-61 into an insulin-like structure. This conformation is shown schematically in Fig. 1. Residues 8-18 (B9-B19) and [43][44][45][46][47][48] (A2-A7) are right-handed a-helices and residues 54-60 (A13-A19) formed a less organized right-handed helix. Cys 47 and 52 (A6 and All) and Cys 61 and 18 (A20 and B19) have their disulfides placed in the core, while the Cys ...

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Section: Resultsmentioning

confidence: 99%

Insulin-like growth factor: a model for tertiary structure accounting for immunoreactivity and receptor binding.

Blundell¹,

Bedarkar²,

Rinderknecht³

et al. 1978

Proc. Natl. Acad. Sci. U.S.A.

260

137

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“…This finding led researchers to conclude that insulin acts in a coordinated manner with serum components. Growth factors were discovered one after another during this era: nerve growth factor,67 epidermal growth factor,68, 69 insulin‐like growth factor,70, 71, 72, 73 fibroblast growth factor (FGF),74, 75 platelet‐derived growth factor,76, 77, 78 and transforming growth factor (TGF) 79, 80. The addition of these growth factors to a culture medium increased cellular proliferation.…”

Section: History Of Cell Culture Mediamentioning

confidence: 99%

Animal‐cell culture media: History, characteristics, and current issues

Yao

Asayama

2017

Reprod Medicine & Biology

396

278

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BackgroundCell culture technology has spread prolifically within a century, a variety of culture media has been designed. This review goes through the history, characteristics and current issues of animal‐cell culture media.MethodsA literature search was performed on PubMed and Google Scholar between 1880 and May 2016 using appropriate keywords.ResultsAt the dawn of cell culture technology, the major components of media were naturally derived products such as serum. The field then gradually shifted to the use of chemical‐based synthetic media because naturally derived ingredients have their disadvantages such as large batch‐to‐batch variation. Today, industrially important cells can be cultured in synthetic media. Nevertheless, the combinations and concentrations of the components in these media remain to be optimized. In addition, serum‐containing media are still in general use in the field of basic research. In the fields of assisted reproductive technologies and regenerative medicine, some of the medium components are naturally derived in nearly all instances.ConclusionsFurther improvements of culture media are desirable, which will certainly contribute to a reduction in the experimental variation, enhance productivity among biopharmaceuticals, improve treatment outcomes of assisted reproductive technologies, and facilitate implementation and popularization of regenerative medicine.

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“…Embora estudo prévio tenha identificado a relação entre os níveis séricos de IGF-1 e o porte em várias raças de cães (Eigenmann, Amador, Patterson 1988) e tenham sido relacionados ao crescimento em humanos (Froesch et al 1963, Daughaday et al 1972) o fato que deve ser lembrado é que, são os valores teciduais e não os séricos de IGF-1 que determinam o crescimento do corpo (Yakar et al 1999).…”

Section: Avaliação Do Fator De Crescimento Semelhante à Insulina Tipounclassified

Relação da expressão de fatores de crescimento celular (IGF-1) e (SCF) com fatores prognósticos e o alvo da rapamicina em mamíferos (m-TOR) em mastocitomas cutâneos caninos

et al. 2013

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Pesq. Vet. Bras. 33(4):549-556, abril 2013 549 RESUMO.-O mastocitoma cutâneo (MTC) é a neoplasia maligna mais comum na pele dos cães e seu comportamento biológico é muito variável. Dentre os fatores prognósticos estudados nos MTCs, a classificação histopatológica, o ín-dice proliferativo e o padrão de expressão doc-KIT são os que apresentam uma associação mais relevante com o provável prognóstico deste tumor. O objetivo deste trabalho foi avaliar a expressão proteica de fator de crescimento semelhante à insulina tipo 1 (IGF-1), fator de célula tronco (SCF) e sua relação com o receptor tirosina quinase (c-KIT), alvo da rapamicina em mamíferos (m-TOR), grau histológico, índice proliferativo pelo KI-67e o número de figuras de mitose (IM) com dados clínicos de cães com MTCs .

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Antibody-Suppressible and Nonsuppressible Insulin-Like Activities in Human Serum and Their Physiologic Significance. An Insulin Assay With Adipose Tissue of Increased Precision and Specificity*

Cited by 386 publications

References 37 publications

Insulin-like growth factor: a model for tertiary structure accounting for immunoreactivity and receptor binding.

Insulin-like growth factor: a model for tertiary structure accounting for immunoreactivity and receptor binding.

Animal‐cell culture media: History, characteristics, and current issues

Relação da expressão de fatores de crescimento celular (IGF-1) e (SCF) com fatores prognósticos e o alvo da rapamicina em mamíferos (m-TOR) em mastocitomas cutâneos caninos

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