Macroprolactinemia: Diagnostic, Clinical, and Pathogenic Significance
Macroprolactinemia is characterized by a large molecular mass of PRL (macroprolactin) as the main molecular form of PRL in sera, the frequent elevation of serum PRL (hyperprolactinemia), and the lack of symptoms. Macroprolactin is largely a complex of PRL with immunoglobulin G (IgG), especially anti...
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Wiley
2012-01-01
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| Series: | Clinical and Developmental Immunology |
| Online Access: | http://dx.doi.org/10.1155/2012/167132 |
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| author | Akira Shimatsu Naoki Hattori |
| author_facet | Akira Shimatsu Naoki Hattori |
| author_sort | Akira Shimatsu |
| collection | DOAJ |
| description | Macroprolactinemia is characterized by a large molecular mass of PRL (macroprolactin) as the main molecular form of PRL in sera, the frequent elevation of serum PRL (hyperprolactinemia), and the lack of symptoms. Macroprolactin is largely a complex of PRL with immunoglobulin G (IgG), especially anti-PRL autoantibodies. The prevalence of macroprolactinemia is 10–25% in patients with hyperprolactinemia and 3.7% in general population. There is no gender difference and a long-term followup demonstrates that macroprolactinemia develops before middle age and is likely a chronic condition. Polyethylene-glycol- (PEG-) precipitation method is widely used for screening macroprolactinemia, and gel filtration chromatography, protein A/G column, and I125-PRL binding studies are performed to confirm and clarify its nature. The cross-reactivity of macroprolactin varies widely according to the immunoassay systems. The epitope on PRL molecule recognized by the autoantibodies is located close to the binding site for PRL receptors, which may explain that macroprolactin has a lower biological activity. Hyperprolactinemia frequently seen in macroprolactinemic patients is due to the delayed clearance of autoantibody-bound PRL. When rats are immunized with rat pituitary PRL, anti-PRL autoantibodies are produced and hyperprolactinemia develops, mimicking macroprolactinemia in humans. Screening of macroprolactinemia is important for the differential diagnosis of hyperprolactinemia to avoid unnecessary examinations and treatments. |
| format | Article |
| id | doaj-art-3426dd24c75f47b0a1cbcba59540de51 |
| institution | Kabale University |
| issn | 1740-2522 1740-2530 |
| language | English |
| publishDate | 2012-01-01 |
| publisher | Wiley |
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| series | Clinical and Developmental Immunology |
| spelling | doaj-art-3426dd24c75f47b0a1cbcba59540de512025-02-03T06:01:37ZengWileyClinical and Developmental Immunology1740-25221740-25302012-01-01201210.1155/2012/167132167132Macroprolactinemia: Diagnostic, Clinical, and Pathogenic SignificanceAkira Shimatsu0Naoki Hattori1Clinical Research Institute, National Hospital Organization Kyoto Medical Center, 1-1 Mukaihata-cho, Fukakusa, Fushimi-ku, Kyoto 612-8555, JapanDepartment of Pharmaceutical Sciences, Ritsumeikan University, Shiga 525-8577, JapanMacroprolactinemia is characterized by a large molecular mass of PRL (macroprolactin) as the main molecular form of PRL in sera, the frequent elevation of serum PRL (hyperprolactinemia), and the lack of symptoms. Macroprolactin is largely a complex of PRL with immunoglobulin G (IgG), especially anti-PRL autoantibodies. The prevalence of macroprolactinemia is 10–25% in patients with hyperprolactinemia and 3.7% in general population. There is no gender difference and a long-term followup demonstrates that macroprolactinemia develops before middle age and is likely a chronic condition. Polyethylene-glycol- (PEG-) precipitation method is widely used for screening macroprolactinemia, and gel filtration chromatography, protein A/G column, and I125-PRL binding studies are performed to confirm and clarify its nature. The cross-reactivity of macroprolactin varies widely according to the immunoassay systems. The epitope on PRL molecule recognized by the autoantibodies is located close to the binding site for PRL receptors, which may explain that macroprolactin has a lower biological activity. Hyperprolactinemia frequently seen in macroprolactinemic patients is due to the delayed clearance of autoantibody-bound PRL. When rats are immunized with rat pituitary PRL, anti-PRL autoantibodies are produced and hyperprolactinemia develops, mimicking macroprolactinemia in humans. Screening of macroprolactinemia is important for the differential diagnosis of hyperprolactinemia to avoid unnecessary examinations and treatments.http://dx.doi.org/10.1155/2012/167132 |
| spellingShingle | Akira Shimatsu Naoki Hattori Macroprolactinemia: Diagnostic, Clinical, and Pathogenic Significance Clinical and Developmental Immunology |
| title | Macroprolactinemia: Diagnostic, Clinical, and Pathogenic Significance |
| title_full | Macroprolactinemia: Diagnostic, Clinical, and Pathogenic Significance |
| title_fullStr | Macroprolactinemia: Diagnostic, Clinical, and Pathogenic Significance |
| title_full_unstemmed | Macroprolactinemia: Diagnostic, Clinical, and Pathogenic Significance |
| title_short | Macroprolactinemia: Diagnostic, Clinical, and Pathogenic Significance |
| title_sort | macroprolactinemia diagnostic clinical and pathogenic significance |
| url | http://dx.doi.org/10.1155/2012/167132 |
| work_keys_str_mv | AT akirashimatsu macroprolactinemiadiagnosticclinicalandpathogenicsignificance AT naokihattori macroprolactinemiadiagnosticclinicalandpathogenicsignificance |