mProX™ Human GHRH Stable Cell Line

Halmos G, et al. "Signaling mechanism of growth hormone-releasing hormone receptor.." Vitamins and hormones, 2023.
The hypothalamic peptide growth hormone-releasing hormone (GHRH) plays an important role in stimulating the secretion of growth hormone (GH) through binding and activation of the GHRH-R receptor, which belongs to the G protein-coupled receptor family. Recently, splice variants (SV) of GHRH-Rs have been identified in human tumors and other tissues, with splice variant 1 (SV1) being the most closely related to the full-length GHRH-R and retaining functionality in response to GHRH stimulation. The potential clinical applications of GHRH agonists and antagonists have been extensively studied in diverse fields, such as endocrinology, oncology, cardiology, diabetes, obesity, metabolic disorders, Alzheimer's disease, ophthalmology, and wound healing. This chapter provides an overview of the expression and potential function of GHRH-Rs and their splice variants in different tissues, as well as the molecular mechanisms and signaling pathways involved in their activation. Additionally, the therapeutic applications of GHRH analogs are discussed. In summary, GHRH and its receptors have potential therapeutic implications in various diseases and further research on their functions and molecular mechanisms is warranted.
Pubmed: 37717982   DOI: 10.1016/bs.vh.2023.06.004

Gonzalez-Lopez NM, et al. "In-house standards derived from doping peptides: Enzymatic and serum stability ." Biomedical chromatography : BMC, 2023.
The impact of matrix effect and sample pretreatment on the accuracy of peptide recovery in biological matrices is significant. To address this issue, the use of an internal standard (IS) is common; however, it is not always available, limiting the effectiveness of the analytical method. Therefore, this study aimed to identify short peptides that can serve as ISs in the quantification of peptides in biological matrices. Through solid-phase peptide synthesis, doping peptides GHRP-4, GHRP-5, GHRP-6, Sermorelin (1-11), Sermorelin (13-20), and Sermorelin (22-29) were synthesized and subjected to treatment with human blood, trypsin, and chymotrypsin to evaluate their stability. The peptides were then analyzed using the high-performance liquid chromatography-diode array detector (HPLC-DAD) method. The results showed that GHRP-4, GHRP-6, and Sermorelin (22-29) displayed both stability to enzymatic and blood treatment, making them viable options as in-house ISs for peptide quantification in biological samples. To further assess these peptides' suitability, GHRP-6 and Sermorelin (22-29) were used to analyze a dimeric peptide ((26) [F] LfcinB (20-30)(2) ) in four different matrices. The study established a distinct profile for each peptide in terms of protein binding and enzymatic stability, highlighting their potential as effective ISs for peptide quantification in biological samples.
Pubmed: 37688464   DOI: 10.1002/bmc.5741