Purification and characterization of three molecular forms of insulin-like growth factor II from human Cohn paste IV

Straczek, J.; Heulin, M. G.; Chenut, A.M.; Lasbennes, A; Geschier, C.; Belleville, F.; Nabet, P

doi:10.1016/s0378-4347(00)83775-5

Cited by 8 publications

(3 citation statements)

References 30 publications

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“…One major difference is that the kangaroo protein has a three amino acid insert of Leu-Pro-Gly at position 30 (numbering based on human sequence). Comparison with other known IGF-II sequences revealed that kIGF-II is similar to a minor IGF-II variant, [Ser 29 ]-hIGF-II, previously described in human serum (Hampton et al 1989, Straczek et al 1990) and placental tissue (De Ceuninck et al 1995b). This variant also contains an insertion of Leu-Pro-Gly at position 30 along with a substitution of Arg for Ser at position 29.…”

Section: Discussionmentioning

confidence: 53%

“…While the majority of IGF-II exists as the mature form of 7·5 kDa, high molecular weight (MW) isoforms of IGF-II have been detected in human serum (Zumstein et al 1985, Gowan et al 1987, cerebrospinal fluid (Haselbacher & Humbel 1982) and malignant tissue extracts (Daughaday et al 1988, Daughaday & Kapadia 1989. Variant forms of IGF-II have also been identified in human serum (Hampton et al 1989, Straczek et al 1990, Van den Brande et al 1990) and placental tissue (De Ceuninck et al 1995b).…”

Section: Introductionmentioning

confidence: 99%

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Kangaroo IGF-II is structurally and functionally similar to the human [Ser29]-IGF-II variant

Yandell¹,

Francis²,

Wheldrake³

et al. 1999

Journal of Endocrinology

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Kangaroo IGF-II has been purified from western grey kangaroo (Macropus fuliginosus) serum and characterised in a number of in vitro assays. In addition, the complete cDNA sequence of mature IGF-II has been obtained by reverse-transcription polymerase chain reaction. Comparison of the kangaroo IGF-II cDNA sequence with known IGF-II sequences from other species revealed that it is very similar to the human variant, [Ser 29 ]-hIGF-II. Both the variant and kangaroo IGF-II contain an insert of nine nucleotides that encode the amino acids Leu-Pro-Gly at the junction of the B and C domains of the mature protein.The deduced kangaroo IGF-II protein sequence also contains three other amino acid changes that are not observed in human IGF-II. These amino acid differences share similarities with the changes described in many of the IGF-IIs reported for non-mammalian species. Characterisation of human IGF-II, kangaroo IGF-II, chicken IGF-II and [Ser 29 ]-hIGF-II in a number of in vitro assays revealed that all four proteins are functionally very similar. No significant differences were observed in the ability of the IGF-IIs to bind to the bovine IGF-II/cationindependent mannose 6-phosphate receptor or to stimulate protein synthesis in rat L6 myoblasts. However, differences were observed in their abilities to bind to IGF-binding proteins (IGFBPs) present in human serum. Kangaroo, chicken and [Ser 29 ]-hIGF-II had lower apparent affinities for human IGFBPs than did human IGF-II. Thus, it appears that the major circulating form of IGF-II in the kangaroo and a minor form of IGF-II found in human serum are structurally and functionally very similar. This suggests that the splice site that generates both the variant and major form of human IGF-II must have evolved after the divergence of marsupials from placental mammals.

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Section: Discussionmentioning

confidence: 53%

Section: Introductionmentioning

confidence: 99%

Kangaroo IGF-II is structurally and functionally similar to the human [Ser29]-IGF-II variant

Yandell¹,

Francis²,

Wheldrake³

et al. 1999

Journal of Endocrinology

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“…Lipids are required for long-term multiplication because only a short-term stimulatory effect was observed with delipidated Cf-IV-1. This fraction is enriched in alpha globulins (6, 13a), lipoproteins (6, 13a), and growth factors (3,25,28); a combination of these compounds is probably required a Each value represents a percentage of the control and is the mean of three independent experiments performed in triplicate ± the standard deviation. Cf-IV-1 was used at 0.5 mg/ml of medium.…”

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confidence: 99%

Serum Cohn fraction IV-1 supports the growth of Giardia lamblia in vitro

et al. 1994

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Bovine serum Cohn fractions were substituted for whole bovine serum in TYI-S-33 medium. Only fraction IV-1 supported attachment, cysteine uptake, and growth of Giardia lamblia. Among the mammalian sources tested, only goat and horse fractions showed activities comparable to that of the bovine fraction. Agglutinating immunoglobulins were identified as deleterious agents in human, rat, rabbit, and dog fractions. Giardia lamblia is an intestinal protozoan that infects humans and other mammals (1, 27). Trophozoites grow efficiently in vitro in complex media containing serum and a high concentration of L-cysteine (1, 9, 10, 13, 15, 20, 27, 29). It is not known what factors in serum are important to Giardia trophozoites or how these serum components compare to those present in the small intestine. Several groups have attempted to grow Giardia trophozoites in serum-free media (2, 10, 29). Bifulco and Schaefer (2) replaced serum in TYI-S-33 medium with the serum substitute Ultoser G. Although the exact composition of Ultoser G is unknown, it does contain serum constituents. Gillin and Reiner (11) reported that bovine Cohn fraction III (Cf-TTT) from Sigma (Cf-ITT from suppliers other than Sigma were not active) contains a factor that is required by trophozoites for attachment and short-term survival in different media. However, these media fail to support longterm growth of Giardia trophozoites. In the present work, factors in serum important for growth, attachment, and uptake of L-cysteine were studied by supplementing Keister's modified TYI-S-33 medium (15) with different serum components at concentrations equivalent to 10% serum (16). Table 1 shows that among the various bovine serum Cfs (6, 13a), only Cf-IV-1 supported attachment, growth, and cysteine uptake of the isolate WB-derived clone 1267 (21, 24) of G. lamblia. Cf-II plus-TTT (enriched in beta and gamma globulins), Cf-Ill (enriched in alpha, beta, and gamma globulins), Cf-IV-4 (enriched in alpha and beta globulins), and Cf-V (rich in albumin) supported attachment to glass but had little effect on growth. Cf-I (fibrinogen), Cf-TI (gamma globulins), insulin, transferrin, and fibronectin supported neither growth nor attachment. Gillin and Reiner (11) observed no effect when they used a crude bovine Cf-IV preparation (no source given) or ,B-lipoproteins (bovine serum Cf-IV-4) obtained from ICN Nutritional Biochemicals. Although we found that Cf-IV-4 (Sigma) has no effect on trophozoites, bovine Cf-IV-1 (Sigma) can replace serum in TYI-S-33 medium for serial cultivation of Giardia trophozoites (subcultures were done every 72 to 96 h 39 times). The beneficial effect of bovine Cf-IV-1 on the attachment of Tnchomonas vaginalis to plastic surfaces has also been reported (12). In previous work, we demonstrated that L-cysteine is essential for the growth of Giardia trophozoites in vitro and that

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Purification from human plasma of a tetrapeptide that potentiates insulin‐like growth factor‐I activity in chick embryo cartilage

et al. 1995

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Human plasma has been shown to contain a low molecular weight factor that potentiates human IGF-I stimulation of glycosaminoglycan synthesis in chick embryo cartilage. The peptide was purified and characterized by Edman degradation and electrospray mass spectrometry. The primary structure determined was: Trp-Gly-His-Glu. A homologous synthetic peptide similarly promoted matrix biosynthesis in cartilage exposed to

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Purification and characterization of three molecular forms of insulin-like growth factor II from human Cohn paste IV

Cited by 8 publications

References 30 publications

Kangaroo IGF-II is structurally and functionally similar to the human [Ser29]-IGF-II variant

Kangaroo IGF-II is structurally and functionally similar to the human [Ser29]-IGF-II variant

Serum Cohn fraction IV-1 supports the growth of Giardia lamblia in vitro

Purification from human plasma of a tetrapeptide that potentiates insulin‐like growth factor‐I activity in chick embryo cartilage

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