Abstract
The measurement of the protein hormone prolactin (PRL) in biological samples has developed over the years into a routine clinical assay aiding the diagnosis of multiple medical conditions. PRL is known to exist in multiple isoforms circulating throughout the body. Current methodologies for measuring the PRL levels typically involve a variety of immunoassays. However, most of these tests are not capable of distinguishing between the different isoforms. To address this need, we have developed a highly specialized method employing multiple reaction monitoring mass spectrometry (MRM-MS) capable of monitoring seven distinct peptides from two of the most common prolactin isoforms (the 23 kDa PRL and its 16 kDa N-terminal cleavage product). Since serum is the main source of clinical specimen for the measurement of prolactin isoforms, the method described in this chapter is focused on the approach to processing whole serum samples for prolactin analysis via reversed-phase liquid chromatography (RPLC) and MRM-MS.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Bole-Feysot C, Goffin V, Edery M, Binart N, Kelly PA (1998) Prolactin (PRL) and its receptor: actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice. Endocr Rev 19:225–268
Freeman ME, Kanyicska B, Lerant A, Nagy G (2000) Prolactin: structure, function, and regulation of secretion. Physiol Rev 80:1523–1631
Corbacho AM, Macotela Y, Nava G et al (2000) Human umbilical vein endothelial cells express multiple prolactin isoforms. J Endocrinol 166:53–62
Wennbo H, Törnell J (2000) The role of prolactin and growth hormone in breast cancer. Oncogene 19:1072–1076
Chen DK, So YT, Fisher RS (2005) Use of serum prolactin in diagnosing epileptic seizures. Neurology 65:668–675
Clevenger CV, Furth PA, Hankinson SE, Schuler LA (2003) The role of prolactin in mammary carcinoma. Endocr Rev 24:1–27
Tworoger SS, Eliassen AH, Sluss P, Hankinson SE (2007) A prospective study of plasma prolactin concentrations and risk of premenopausal and postmenopausal breast cancer. J Clin Oncol 25:1482–1488
Tworoger SS, Hankinson SE (2006) Prolactin and breast cancer risk. Cancer Lett 243:160–169
Tworoger SS, Hankinson SE (2008) Prolactin and breast cancer etiology: an epidemiologic perspective. J Mammary Gland Biol Neoplasia 13:41–53
Vonderhaar BK (1998) Prolactin: the forgotten hormone of human breast cancer. Pharmacol Ther 79:169–178
Vonderhaar BK (1999) Prolactin involvement in breast cancer. Endocr Relat Cancer 6:389–404
Faupel-Badger JM, Sherman ME, Garcia-Closas M et al (2010) Prolactin serum levels and breast cancer: relationships with risk factors and tumor characteristics among pre- and postmenopausal women in a population-based case–control study from Poland. Br J Cancer 103:1097–1102
Linher-Melville K, Zantinge S, Sanli T et al (2011) Establishing a relationship between prolactin and altered fatty acid β-Oxidation via carnitine palmitoyl transferase 1 in breast cancer cells. BMC Cancer 11:56–70
Rouet V, Bogorad RL, Kayser C et al (2010) Local prolactin is a target to prevent expansion of basal/stem cells in prostate tumors. Proc Natl Acad Sci USA 107:15199–15204
Baranowska B, Radzikowska M, Wasilewska-Dziubinska E, Roguski K, Morowiec M (2006) The role of VIP and somatostatin in the control of GH and prolactin release in anorexia nervosa and in obesity. Ann NY Acad Sci 921:443–455
Paick JS, Yan JH, Kim SW, Ku JH (2006) The role of prolactin levels in the sexual activity of married men with erectile dysfunction. BJU Int 98:1269–1273
Hattori N (1996) The frequency of macroprolactinemia in pregnant women and the heterogeneity of its etiologies. J Clin Endocrinol Metab 81:586–590
Smith CR, Norman MR (1990) Prolactin and growth hormone: molecular heterogeneity and measurement in serum. Ann Clin Biochem 27:542–550
Clapp C, González C, Macotela Y (2006) Vasoinhibins: a family of N-terminal prolactin fragments that inhibit angiogenesis and vascular function. Front Horm Res 35:64–73
Clapp C, Martial JA, Guzman RC, Rentier-Delure F, Weiner RI (1993) The 16-kilodalton N-terminal fragment of human prolactin is a potent inhibitor of angiogenesis. Endocrinology 133:1292–1299
Piwnica D, Touraine P, Struman I et al (2004) Cathepsin D processes human prolactin into multiple 16 K-like N-terminal fragments: study of their antiangiogenic properties and physiological relevance. Mol Endocrinol 18:2522–2542
Faupel-Badger JM, Ginsburg E, Fleming JM et al (2010) 16-kDa prolactin reduces angiogenesis, but not growth of human breast cancer tumors in vivo. Horm Cancer 1:71–79
Hilfiker-Kleiner D, Kaminski K, Podewski E et al (2007) A cathepsin D-cleaved 16-kDa form of prolactin mediates postpartum cardiomyopathy. Cell 128:589–600
Acknowledgments
This project has been funded in whole or in part with federal funds from the National Cancer Institute, National Institutes of Health, under Contract HHSN261200800001E. The content of this publication does not necessarily reflect the views or policies of the Department of Health and Human Services, nor does mention of trade names, commercial products, or organizations imply endorsement by the United States Government.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2013 Springer Science+Business Media, LLC
About this protocol
Cite this protocol
Waybright, T.J., Xu, X., Faupel-Badger, J.M., Xiao, Z. (2013). Preparation of Human Serum for Prolactin Measurement by Multiple Reaction Monitoring Mass Spectrometry. In: Zhou, M., Veenstra, T. (eds) Proteomics for Biomarker Discovery. Methods in Molecular Biology, vol 1002. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-360-2_16
Download citation
DOI: https://doi.org/10.1007/978-1-62703-360-2_16
Published:
Publisher Name: Humana Press, Totowa, NJ
Print ISBN: 978-1-62703-359-6
Online ISBN: 978-1-62703-360-2
eBook Packages: Springer Protocols