POLYMORPHISM OF PROTEIN AND POLYPEPTIDE HORMONES<sup>1</sup>

Franchimont, P; Gaspard, Ulysse; Reuter, A.; Heynen, G

doi:10.1111/j.1365-2265.1972.tb00402.x

Cited by 130 publications

(56 citation statements)

References 25 publications

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“…Although our studies provide no direct evidence for such a precursor hypothesis, there is ample precedent for neoplasms producing precursor forms of polypeptides (4). Immunoactive alplhalike forms of apparently higher molecular weight ill gel chromatography-have been noted in l)lacental extracts, pregnancy Serum, and urine (41,42), but these…”

Section: Purification Of Ectopic Alpha Subunitsmentioning

confidence: 99%

Differences between purified ectopic and normal alpha subnits of human glycoprotein hormones.

Weintraub¹,

Krauth²,

Rosen³

et al. 1975

J. Clin. Invest.

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A B S T R A C T "Ectopic" proteins, not distinguished immunologically from the common alpha subunit of the human glycoprotein hormones, were purified approximately 10,000-fold from a gastric carcinoid tumor (A.L.-a) and from tissue culture medium of bronchogenic carcinoma cell lines (ChaGo-a). The purified A.L.-a was homogeneous by sodium dodecyl sulfate (SDS) gel electrophoresis while the purified ChaGo-a showed multiple components, some of which represented aggregated species. In SDS gel electrophoresis. the apparent molecular wreights of A.L.-a (15,000) and dithioerythritol-reduced ChaGo-a (13,000) were significantly lower than those of the alpha subunits of human chorionic goniadotropin (hCG-a), luteinizing hormone, follicle-stinmtulatinig hormone, or thyroid-stimulating hormone (22,000-23,000). Binding experiments with ['S]-SDS suggested that these apparent differences in molecular wveight resulted, at least in part, from diminished binding of the SDS by the normal compared to the ectopic alpha subunits. In gel chromatography. the apparent molecular weights of A.L.-a (27,000) and ChaGo-a (30.000) were slightly higher than those of normal alpha subunits (23,000-24,000). Both A.L.-a and CliaGo-a were not distinguished from hCG-a in ionexchacnge chromatography. The composition of A.L.-a wvas similar to that of hCG-a in 13 amino acids but showed decreased phenylalanine and increased valine; glu1cosamine was identified in both A.L.-a and h1CG-a.Under conditions in which hCG-a combined with the hCG beta subunit (hCG-P) to produce 95%te of the expected gonadotropin-biniding-activity in a rat testis radioreceptor-assay, A.L.-a incuibation wvith hCG-P resullted in only 2c% of the expected activity, and ChaGo-a incubation with hCG-9 produced nlo detectable activity.

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Section: Purification Of Ectopic Alpha Subunitsmentioning

confidence: 99%

Differences between purified ectopic and normal alpha subnits of human glycoprotein hormones.

Weintraub¹,

Krauth²,

Rosen³

et al. 1975

J. Clin. Invest.

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“…Fragments of this type have been observed in the urine of pregnant women (5,6,8,9), in crude commercial preparations of hCG from pregnancy (16), and in the urine of several patients with trophoblastic neoplasms (1) and nontrophoblastic tumors (1,8,11). We have observed that this type of fragment also appears in the urine after infusion of highly purified hCG/B subunit into normal subjects (17) and, therefore, it is a product of the metabolism of hCGI3.…”

Section: Introductionmentioning

confidence: 63%

“…Parenthetically, the specimens shown in Fig. 7 contained the form of free alpha subunit that has been reported to be excreted in pregnancy (5,6,8,9), and the 13,000-apparent molecular weight hCG# core fragment that cross-reacts in RIA using antiserum to the hCG,B subunit (data not shown).…”

Section: Resultsmentioning

confidence: 90%

“…Some of these forms of the hormone appear to be subunits of hCG (1)(2)(3)(4)(5)(6)(7), and some appear to be fragments, as they exhibit molecular sizes smaller than those of the hCG subunits (1,5,6,(8)(9)(10)(11). When obtained from different sources, hCG itself has been found to have variable biological, physicochemical, and immunological properties; this microheterogeneity seems to be related, in part, to variations in its carbohydrate composition (10,(12)(13)(14)(15).…”

Section: Introductionmentioning

confidence: 99%

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Characterization of a carboxyterminal peptide fragment of the human choriogonadotropin beta-subunit excreted in the urine of a woman with choriocarcinoma.

Amr¹,

Wehmann²,

Birken³

et al. 1983

J. Clin. Invest.

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A B S T R A C T We have observed low-molecular weight carboxyterminal fragments of the human choriogonadotropin (hCG) a-subunit in the urines of several women with choriocarcinoma, and we have characterized one fragment in detail. Its apparent molecular weight by gel chromatography on Sephadex G-100 was 14,200. The fragment was not adsorbed to concanavalin A-Sepharose, indicating that it lacked the asparagine-linked carbohydrate groups of intact hCG#. It was active in radioimmunoassays (RIA) using antisera either to the hCG# carboxyterminal peptide (CTP) or to the desialylated hCG# CTP (hCG# as-CTP), indicating the presence of not only the hCG# carboxyterminus but also desialylated O-serine-linked carbohydrate side chains on the fragment. It lacked luteinizing hormone/choriogonadotropin radioreceptor activity and hCG# conformational immunoreactivity (SB6 RIA). On Sephadex G-100 gel chromatography, the elution profiles of this fragment and the hCG# as-CTP(115-145) prepared by trypsin digestion of ashCG were essentially indistinguishable (apparent molecular weights 14,200 and 14,000, respectively). The immunological characteristics of the fragment in both hCG# CTP and hCG# as-CTP RIA were indistinguishable from those of the hCG,6 as-CTP(115-145) glycopeptide. Carboxyterminal fragments of hCG# were evident in urine specimens obtained from 10 of 11 patients with choriocarcinoma but not in those ob-

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“…species of hCGa in the placenta has been described (23,25,26). It is possible that the large hCGa-like material produced by the transformed placental cells was the precursor form of hCGa, as speculated by Weintraub et al (27).…”

Section: Discussionmentioning

confidence: 95%

Establishment of clonal human placental cells synthesizing human choriogonadotropin.

Chou¹

1978

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

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Seven clonal human placental cell lines were established by transformation of human first-trimester placental cells with simian virus 40. These transformed cells synthesized native human choriogonadotropin (chorionic gonadotropin) (hCG) as well as the free a and P subunits of hCG. The amount of native hCG synthesized by these cells was, however, lower than the amount of free P subunit. (Both hCG and the P subunit are detected by the radioimmiunoassay for 0 subunit, but only hCG is detected by the radioreceptor assay.) The a and ft subunits produced by these transformed placental cells were heterogeneous in size; the sizes of the predominant a and P species, however, corresponded to those of urinary a and P

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POLYMORPHISM OF PROTEIN AND POLYPEPTIDE HORMONES¹

Cited by 130 publications

References 25 publications

Differences between purified ectopic and normal alpha subnits of human glycoprotein hormones.

Differences between purified ectopic and normal alpha subnits of human glycoprotein hormones.

Characterization of a carboxyterminal peptide fragment of the human choriogonadotropin beta-subunit excreted in the urine of a woman with choriocarcinoma.

Establishment of clonal human placental cells synthesizing human choriogonadotropin.

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POLYMORPHISM OF PROTEIN AND POLYPEPTIDE HORMONES1

Cited by 130 publications

References 25 publications

Differences between purified ectopic and normal alpha subnits of human glycoprotein hormones.

Differences between purified ectopic and normal alpha subnits of human glycoprotein hormones.

Characterization of a carboxyterminal peptide fragment of the human choriogonadotropin beta-subunit excreted in the urine of a woman with choriocarcinoma.

Establishment of clonal human placental cells synthesizing human choriogonadotropin.

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POLYMORPHISM OF PROTEIN AND POLYPEPTIDE HORMONES¹