Growth Hormone Binding Proteins

Baumann, Gerhard

doi:10.1007/978-1-4615-5163-8_3

Cited by 2 publications

(1 citation statement)

References 159 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In reference to soluble growth hormone receptor, some soluble forms of PRLR were assumed to have the following functions: 1) increase prolactin half-life by stabilizing prolactin structure (Baumann, 1993); and 2) serve as a storage reservoir for prolactin and growth hormone (GH) so that they can be released upon requirements (Kopchick and Andry, 2000). Human GH also binds to the extracellular domain of the hPRLR via 1:1 complex (Somers et al, 1994); 3) Serve as a transporter for circulating PRLR and growth hormone (Horseman, 2002).…”

Section: Introductionmentioning

confidence: 99%

Multiple human prolactin receptors and signaling

Ding¹,

Wu²

2010

Afr. J. Biotechnol.

View full text Add to dashboard Cite

Human prolactin receptor (PRLR) transcripts and their protein products exhibit heterogenic structures and functions. This multiplicity constitutes a gene regulatory system. Short PRLR might modulate longer PRLR structures and signaling. Here we overviewed 10 forms (including two putative forms) of PRLR structures, signaling and functions and analyzed the possible regulatory system regarding multiple PRLRs. Particularly, we discovered that a mimic of phosphorylated prolactin induced p21 waf1 expression via a short form of PRLR S1b in prostate cancer cells. In addition, an intron retention was discovered in PRLR mRNA transcript via sequence analysis, showing that an intron encodes PRLR once needed. PRLR splicing and intron retention might be a critical modulating system to regulate PRLR structures and functions. Furthermore, PRLR genomic size was extended to 182 kb, versus the former report, 70 kb. Interestingly, dozens of PRLR-linked genes on chromosome 5 might interplay one another. This review fully uncovered the associations in PRLR multiplicity and functions, suggesting that shorter PRLR might modulate long PRLR function via multiple PRLR system in both mRNA and protein levels.

show abstract

Section: Introductionmentioning

confidence: 99%

Multiple human prolactin receptors and signaling

Ding¹,

Wu²

2010

Afr. J. Biotechnol.

View full text Add to dashboard Cite

show abstract

Tumor Necrosis Factor-α Converting Enzyme (TACE) Is a Growth Hormone Binding Protein (GHBP) Sheddase: The Metalloprotease TACE/ADAM-17 Is Critical for (PMA-Induced) GH Receptor Proteolysis and GHBP Generation*

et al. 2000

View full text Add to dashboard Cite

The GH binding protein (GHBP), which exists in many vertebrates, is a circulating high affinity binding protein corresponding to the extracellular domain of the GH receptor (GHR). In humans, rabbits, and several other species, the GHBP is generated by proteolysis of the GHR and shedding of its extracellular domain. We previously showed that GHBP shedding is inducible by the phorbol ester phorbol 12-myristate,13-acetate (PMA) and inhibited by the metalloprotease inhibitor, Immunex Corp. Compound 3 (IC3). The metzincin metalloprotease, tumor necrosis factor-alpha (TNF-alpha)-converting enzyme (TACE), catalyzes the shedding of TNF-alpha from its transmembrane precursor, a process that is also inhibitable by IC3. TACE may hence be a candidate for GHBP sheddase. In this study, we reconstitute fibroblasts derived from a TACE knockout mouse (Null cells) with either the rabbit (rb) GHR alone (Null/R) or rbGHR plus murine TACE (Null/R+T). Although GHR in both cells was expressed at similar abundance, dimerized normally and caused JAK2 activation in response to GH independent of TACE expression, PMA was unable to generate GHBP from Null/R cells. In contrast, PMA caused ample GHBP generation from TACE reconstituted (Null/R + T) cells, and this GHBP shedding was substantially inhibited by IC3 pretreatment. Corresponding to the induced shedding of GHBP from Null/R + T cells, PMA treatment caused a significant loss of immunoblottable GHR in Null/R+T, but not in Null/R cells. We conclude that TACE is an enzyme required for PMA-induced GHBP shedding and that PMA-induced down-regulation of GHR abundance may in significant measure be attributable to TACE-mediated GHR proteolysis.

show abstract

Growth Hormone Binding Proteins

Cited by 2 publications

References 159 publications

Multiple human prolactin receptors and signaling

Multiple human prolactin receptors and signaling

Tumor Necrosis Factor-α Converting Enzyme (TACE) Is a Growth Hormone Binding Protein (GHBP) Sheddase: The Metalloprotease TACE/ADAM-17 Is Critical for (PMA-Induced) GH Receptor Proteolysis and GHBP Generation*

Contact Info

Product

Resources

About