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Laboratory Investigations in the Diagnosis and Follow-Up of GH

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Laboratory Investigations in the Diagnosis and Follow-Up of GH review Laboratory investigations in the diagnosis and follow-up of GH-related disorders 1 Medizinische Klinik und Poliklinik Katharina Schilbach1 IV, Klinikum der Universität http://orcid.org/0000-0002-8667-0296 München, Munich, Germany Martin Bidlingmaier1 http://orcid.org/0000-0002-4681-6668 ABSTRACT In addition to auxiological, clinical and metabolic features measurements of growth hormone (GH) and insulin-like growth factor I (IGF-I) complement our tools in diagnosis and follow-up of GH-related disorders. While comparably robust during the pre-analytical phase, measurement and interpretation of concentrations of both hormones can be challenging due to analytical issues and biological confounders. Assay methods differ in terms of antibody specificity, interference from binding proteins, reference preparations and sensitivity. GH assays have different specificity towards different GH- isoforms (e.g. 20 kDa GH, placental GH) and interference from the GH antagonist Pegvisomant. The efficacy to prevent binding protein interference is most important in IGF-I assays. Methodological differences between assays require that reference intervals and diagnostic cut-offs are assay-specific. Among biological variables, pubertal development and age are most relevant for IGF-I, making detailed Correspondence to: reference intervals mandatory for interpretation. GH has pulsatile secretion and short half-life. Its Martin Bidlingmaier concentration is modified by acute factors such as stress, exercise and sleep, but also by intake of oral Medizinische Klinik und Poliklinik IV Klinikum der Universität München estrogens and anthropometric factors (e.g. BMI). Other GH dependent biomarkers such as free IGF-I, Ziemssenstr. 1 IGF binding protein 3 (IGFBP 3) and acid labile subunit (ALS) have been proposed. Their concentrations 80336 München largely mirror the information obtained through measurement of IGF-I, but their measurement can Germany [email protected] be helpful in particular situations. In this review, we describe the evolution of analytical methods to muenchen.de measure biomarkers of GH action, the impact of the methodological changes on laboratory results and the need to include biological variables in their interpretation. Arch Endocrinol Metab. 2019;63(6):618-29 Received on Oct/9/2019 Accepted on Oct/12/2019 Keywords DOI: 10.20945/2359-3997000000192 Growth hormone; insulin-like growth factor I; binding proteins; growth hormone deficiency; acromegaly INTRODUCTION the results obtained from measurements by different laboratories or with assays from different manufacturers n all growth hormone (GH) related disorders – GH still are common (4). In addition to analytical issues, deficiency (GHD), GH insensitivity and GH excess I a wide spectrum of endogenous and pharmacological – GH and insulin-like growth factor-I (IGF-I) are the factors influence circulating concentrations of the most important biomarkers used for diagnosis and hormones and need to be taken into account. during follow-up. Other parameters, such as insulin- This review focusses on the analytical and like growth factor binding protein 3 (IGFBP 3) and interpretative aspects related to GH and IGF-I acid labile subunit (ALS), can be useful in particular concentrations. We also describe less frequently used situations, but overall their diagnostic relevance is limited GH-related biomarkers. Suitability of specific stimulation (1,2). Although GH and IGF-I are widely used, both and suppression tests and the respective diagnostic cut- biomarkers have shortcomings due to particularities of offs have been extensively discussed elsewhere, and are the analytical process itself, but also due to difficulties in not the primary focus of this article (5-8). the interpretation of the results. Discrepancies between the results from measurements of GH and IGF-I concentrations have been reported repeatedly (3) and GROWTH HORMONE can lead to problems in clinical management. Throughout the last decades, GH and IGF-I assays GH molecule AE&M all rights reserved. © evolved. Generally, assays have become more sensitive GH is a polypeptide hormone and a cytokine of the Copyright and specific. Nevertheless, significant differences in growth factor superfamily. GH is mainly expressed 618 Arch Endocrinol Metab. 2019;63/6 Laboratory assessment of GH-related diseases in somatotropic cells of the pituitary gland. It is immunoassays. Specificity increased by the use of secreted into the blood stream and mediates its effects monoclonal antibodies rather than polyclonal antisera via dimerized GH receptors in many tissues. GH in (11). Most older assays had recognized a spectrum circulation consists of a variety of different isoforms, of different GH isoforms together with their homo- fragments and molecular complexes (homo- and hetero- and heterodimers and – multimers, while monoclonal dimers and oligomers) (9). With over 90%, the 22kDa antibodies recognize a defined epitope on the surface isoform (22,129 Da) is the most abundant isoform, of the GH molecule and therefore tend to only and best reflects total pituitary GH secretion (10). pick a narrow spectrum of all the GH molecules in Therefore, current guidelines request that modern GH circulation. This is part of the explanation why GH assays should be designed to specifically measure this concentrations as measured by newer assays tend to isoform (4,11). The second most abundant isoform be lower than those measured by assays which were is the 20kDa isoform (20,274 Da), although the available 20 years ago. It is also important to keep biological significance of this isoform has not yet been in mind that other GH isoforms such as the GH fully understood (9). In addition, other isoforms with antagonist pegvisomant or GH-V can significantly minor chemical modifications exist (10). In circulation, cross-react with GH assays. Less specific assays might the different isoforms aggregate to some extent, thereby also cross-react with closely related molecules such forming dimers and multimers. One particular GH as prolactin or placental lactogen. Currently, there isoform occurs only in females during pregnancy. It is is only one automated GH immunoassay that does synthesized and secreted by the placenta and therefore not have cross-reactivity with all of those molecules termed “placental growth hormone” (GH-V). (13). Another factor potentially affecting reported Recently, the spectrum of GH isoforms was further GH concentrations is interference from growth increased by the invention of a mutated GH molecule hormone binding protein (GHBP). In circulation, with antagonistic properties. This artificial isoform approximately 50% of GH is bound to GHBP, and today is known as the GH antagonist pegvisomant and reliable GH immunoassays should ensure that relevant used in the treatment of acromegaly. It binds to the epitopes are not hidden through GHBP binding (11). GH receptor but inhibits signal transduction and hence Alongside changes in assay specificity, there was IGF-I release (12,13). also an evolution of the standard preparations used to calibrate the assays: Originally, only cadaveric Technical aspects of GH measurements GH extracted from pituitaries was available. These To measure GH concentrations for clinical routine preparations, including international standards 66/217 purposes, assays from different commercially sources as and 80/505, were purified to some degree, but still well as some in-house methods are being used. Most consisted of a mixture of isoforms. When recombinant of the assays still recognize a broader spectrum of GH GH became available, the international reference isoforms or have unknown isoform specificity. However, preparation IRP 88/624 was introduced (4,17). Since some of today’s routine assays have already incorporated this preparation consisted solely of pure 22kD GH, the recent recommendations and specifically detect the signal generated from this calibrator compared to the 22kDa isoform only (4,11). As indicated above, pituitary extracts was stronger in assays preferentially current evidence suggests that this isoform represents detecting this isoform, while it was weaker in total pituitary GH secretion. Although of scientific assays preferentially recognizing other isoforms. interest, available studies on specific measurement of Consequently, depending on the isoform specificity of isoforms other than 22kD GH did not reveal additional the assay used, reported GH concentrations for clinical diagnostic value in clinical routine situations. samples changed. Because reference preparations of Detection of GH activity in humans was first recombinant origin can be much better standardized described in 1955, while the first GH immunoassay than pituitary extracts, and because they allow was reported in 1961 (14,15). However, the molecular traceability to mass concentrations rather than arbitrary structure of human GH wasn’t discovered until units, guidelines strongly recommend the use of such the 1970th (16). Over the past decades, GH assays recombinant preparations (4). Today the most common AE&M all rights reserved. evolved from relatively unspecific radioimmunoassays preparation used to calibrate GH assays is the latest © to modern, highly sensitive chemiluminescence recombinant IRP 98/574 (Table 1). The uniform use Copyright Arch Endocrinol Metab. 2019;63/6 619 Laboratory assessment of GH-related diseases of this preparation has removed some, though not all, sample handling as well as storage conditions rather of the differences
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