Androgen binding proteins of testis, epididymis, and plasma in man and monkey.

Vigersky, Robert A.; Loriaux, D. Lynn; Ss, Howards; Hodgen, G B; Lipsett, Mortimer B.; Chrambach, A.

doi:10.1172/jci108557

Cited by 49 publications

(12 citation statements)

References 20 publications

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“…It would seem unlikely that an unrelated serum carrier protein for GH would acquire exactly the same specificity as the membrane receptor. It should be recalled that the hormonal specificities of the corticosteroid-binding globulin (13), the sex steroid-binding globulin (14), the thyroid-binding globulin (15), and the somatomedin-binding proteins (16) differ substantially from those of the receptors for their respective hormones. We doubt that the GH-BP is an important transport protein because only about 20-25% of plasma GH is complexed.…”

Section: Resultsmentioning

confidence: 99%

Absence of serum growth hormone binding protein in patients with growth hormone receptor deficiency (Laron dwarfism).

Daughaday¹,

Trivedi²

1987

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

196

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It has recently been recognized that human serum contains a protein that specifically binds human growth hormone (hGH). This protein has the same restricted specificity for hGH as the membrane-bound GH receptor. To determine whether the GH-binding protein is a derivative of, or otherwise related to, the GH receptor, we have examined the serum of three patients with Laron-type dwarfism, a condition in which GH refractoriness has been attributed to a defect in the GH receptor. The binding of 1251-labeled hGH incubated with serum has been measured after gel filtration of the serum through an Ultrogel AcA 44 minicolumn. Nonspecific binding was determined when '25I-hGH was incubated with serum in tho presence of an excess of GH. Results are expressed as percent of specifically bound 251-hGH and as specific binding relative to that of a reference serum after correction is made for endogenous GH. The mean ± SEM of specific binding of sera from eight normal adults (26-46 years of age) was 21.6 ± 0.45%, and the relative specific binding was 101.1 ± 8.6%. Sera from 11 normal children had lower specific binding of 12.5 ± 1.95% and relative specific binding of 56.6 ± 9.1%. Sera from three children with Laron-type dwarfism lacked any demonstrable GH binding, whereas sera from 10 other children with other types of nonpituitary short stature had normal relative specific binding. We suggest that the serum GHbinding protein is a soluble derivative of the GH receptor. Measurement of the serum GH-binding protein may permit recognition of other abnormalities of the GH receptor.When normal human serum is subjected to gel filtration in neutral buffers, higher-molecular-weight forms of growth hormone (GH) have been frequently reported (1, 2). While these big forms of GH have been attributed to incompletely processed precursor forms of the hormone or aggregated GH molecules, there is now evidence that complexes of GH with a specific serum binding protein exist in human serum and the serum of a number of mammals.The presence of a specific GH-binding protein (GH-BP) was first convincingly established in rabbit serum by Ymer and Herington (3). They added "25I-labeled human GH (hGH) or 125mlabeled bovine GH to normal rabbit serum, and after 2 hr of incubation, the reaction mixture was filtered through Ultrogel. As much as 45% of the added 125I-labeled hGH (125I-hGH) was bound to a component with a Mr of >100,000. Rabbit OH-BP had little affinity for either prolactin or human placental lactogen. The serum GH-BP, like a cytosolic GH-BP found in liver, exhibited 100% cross-reactivity with a monoclonal antireceptor antibody raised by Simpson et al. (4,5) against GH receptors isolated from rabbit liver membranes. These observations led Ymer and Herington to suggest that the serum GH-BP arises from the liver and might be structurally related to the membrane-bound GH receptor. Herington et al. (6) then demonstrated a similar GH-BP in human serum by gel filtration. The techniques of charcoal adsorption and PEG precipitation, which are oft...

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Section: Resultsmentioning

confidence: 99%

Absence of serum growth hormone binding protein in patients with growth hormone receptor deficiency (Laron dwarfism).

Daughaday¹,

Trivedi²

1987

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

196

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“…Electro phoresis in acrylamide gels of different composition could not separate any androgen-binding protein from SHBG in the human testis (13). Affinity chroma tography on Con A-Sepharose may prove to be the method of choice in solving this problem.…”

Section: Discussionmentioning

confidence: 98%

Interaction of Steroid-Binding Serum Proteins with Concanavalin A-Sepharose 4B

Lea¹

1979

Horm Res

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The interaction between steroid-binding serum proteins and concanavalin A was studied using affinity chromatography on concanavalin A-Sepharose 4B. The sex hormone-binding globulins of man and rabbit together with the corticosteroid-binding globulins of man, rabbit and guinea pig were all bound quantitatively by the affinity medium. Only two thirds of rat corticosteroid-binding globulin showed an affinity for concanavalin A indicating this protein to be heterogeneous with respect to terminal mannose or glucose residues. The progesterone-binding globulin in pregnant guinea pig serum, possessing the highest carbohydrate content of the proteins investigated, did not bind to concanavalin A-Sepharose 4B. Affinity chromatography on concanavalin A-Sepharose 4B is documented to be a valuable supplement to existing methods for analysing steroid-protein interactions.

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“…In humans and nonhuman primates, however, there is controversy with regards to its existence. It has been suggested that the steroid-binding protein detected in primate testicular and epididymal cytosol is actually SBP arising from blood contamination when the tissues are homogenized (20). However, others have indicated that ABP and SBP can be distinguished electrophoretically due to differences in sialic acid content of their carbohydrate moiety (21).…”

Section: Methodsmentioning

confidence: 99%

Immunocytochemical localization of the sex steroid-binding protein of plasma in tissues of the adult monkey Macaca nemestrina.

Bordin¹,

Pétra²

1980

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

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The sex steroid-binding protein (SBP) present in the serum of the monkey Macaca nemestrina is shown to exist in cells of tissue involved in reproduction. The localization was demonstrated by immunofluorescence with monospecific antibodies raised against homogeneous human SBP. These antibodies were previously shown to crossreact with monkey SBP. The protein appears to be located in the cytoplasm of epithelial cells lining the prostate alveoli, the ducti of the epididymis, and the seminiferous tubula of the testes of the monkey. The plasma of humans and that of most species tested contain a protein, SBP, which specifically binds 5a-dihydrotestosterone (DHT) and testosterone with high affinity and estradiol-17f with lower affinity depending upon the species. This protein has been purified to homogeneity from the plasma of humans (1-4), rabbits (5), cows (6), and dogs (7). The physicochemical characteristics of the protein isolated from each of these species have been described (3-9).Various reports have appeared suggesting that, in humans, SBP may enter interstitial fluid and tissues and, therefore, may not be exclusively localized in the plasma (10-13). Others, however, have suggested that this observed presence of SBP in cell extracts is due to plasma contamination when the tissues are homogenized. Although the nature of the experimental evidence gathered from those studies does not allow us to distinguish between these two possibilities, it becomes imperative to establish whether or not SBP exists inside cells of target tissues. The consequence of tissue localization of this protein will undoubtedly affect our thoughts and future experimentation with regards to the physiological role of SBP in relation to sex steroid hormone action.We have been able to prepare monospecific antibodies against homogeneous human SBP (14). These antibodies also crossreact with nonhuman primate SBP, such as that present in the plasma of the monkey (Macaca nemestrina) and the The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact. 5678 baboon (Papio cynocephalus) (14). The antibodies, however, do not crossreact with the plasma of any other animals tested, including rabbits, dogs, cats, sheep, goats, cows, and calves (14). Using the monkey model, we have presented preliminary evidence for the existence of SBP within tissue cells.t In this report, we formally describe our results in detail and discuss the possible implication of these findings in relation to already existing information. METHODSSBP was purified from human serum essentially as described (1) except for a modified affinity chromatographic procedure (2). In some cases, the purified protein was passed through an antitransferrin-agarose column to remove traces of transferrin. This immunoadsorbent was synthesized as follows: 12 ml of Affigel-10 (Bio-Rad) was washed rapidly with cold distilled water on a small fritte...

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Androgen binding proteins of testis, epididymis, and plasma in man and monkey.

Cited by 49 publications

References 20 publications

Absence of serum growth hormone binding protein in patients with growth hormone receptor deficiency (Laron dwarfism).

Absence of serum growth hormone binding protein in patients with growth hormone receptor deficiency (Laron dwarfism).

Interaction of Steroid-Binding Serum Proteins with Concanavalin A-Sepharose 4B

Immunocytochemical localization of the sex steroid-binding protein of plasma in tissues of the adult monkey Macaca nemestrina.

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