Eduardo A. Nillni

Research Summary

 

Specialty:     Neuroscience:          Neuroendocrinology

 

Cell Biology and

Biochemistry:          Protein processing and trafficking

 

The main focus in my laboratory is to study the biology of different neuropeptides involved in the regulation of energy balance, thyroid function and growth hormone axis. The proneuropeptide and peptide hormones currently investigated in my laboratory are, proThyrotropin releasing hormone (proTRH), progrowth hormone-releasing hormone (proGHRH), prooipimelanocortin (POMC) and leptin.  We also study the effect that leptin and the norepinephrine system has on the gene transcription and biosynthesis of neuropeptides and on the prohormone convertases (PCs) involved in the post-translational processing of proneuropeptides.

 

Overview of research programs

 

Our laboratory has contributed in great part the current knowledge on the neurobiology of proThyrotropin Releasing Hormone (proTRH).  We have contributed to a better understanding of how several neuro-endocrine inputs (norepinephrine, NE, a-melanocyte stimulating hormone, a-MSH, neuropeptide Y, NPY) and other hormones (leptin and glucocorticoids) affect proTRH gene regulation, its biosynthesis and processing. We also promoted the discovery of novel proTRH-derived peptides with potential biologic function(s). In physiological models, we have shown the effect that lactation has on hypothalamic proTRH processing, and discovered a proTRH-derived peptide that is derived from proTRH processing and is capable of inducing prolactin (PRL) secretion in pituitary cells.  We also studied the impact of cold stress on thermoregulation in the fat/fat mouse, which has a deficient level of hypophysiotropic TRH, and demonstrated recently that other proTRH-derived peptide increases in the periaquaductal gray matter during morphine withdrawal. We have developed a post-translational processing model for proTRH, and demonstrated that PC1 and PC2 are responsible for the processing of proTRH at specific sites.  We also showed that carboxypeptidase E is the primary enzyme involved in the removal of basic residues after the PC cleavage.  In the rat brain tissues with high levels of proTRH expression, we showed tissue-specific processing for different proTRH peptides.

 

Energy balance

 

As an adaptive response to starvation, the hypothalamic-pituitary-thyroid axis is down-regulated in rodents. This is caused, at least in part, by suppression of proTRH mRNA expression in the hypothalamus, which can be reversed by leptin. The action of leptin on TRH neurons in the paraventricular nucleus (PVN) of the hypothalamus occurs through an indirect pathway, involving the release of neuropeptides such as NPY, a-MSH and AgRP from arcuate nucleus, and a direct pathway of leptin action on TRH neurons expressing the leptin receptor. In our studies we investigate the molecular and cellular events involved in the action of leptin and a-MSH on the proTRH life cycle. We also study the effect that leptin, a-MSH and NE has on the gene expression and biosynthesis of PC1 and PC2. 

 

Pro-neuropeptide processing and trafficking

 

In recent years considerable research has focused on the expression of neuropeptide genes and their tissue-specific regulation.  However, it has become clear that the peptides derived from these genes play significant neuromodulatory roles in the control of the central nervous system neurotransmitters.  Even more astounding is the discovery that multiple neuropeptides with distinct physiological functions arise from the processing of single polypeptide precursors.  The post-translational processing and the intracellular sorting of these precursors are key elements to understand these processes.  Our laboratory studies the processing and trafficking of proTRH and proGHRH and the role that PC1 and PC2 play in this process.  We also try to identify the intracellular sorting signals and receptors involved in the correct trafficking of secretory proteins to the regulated secretory pathway.

 

Cold stress and energy consumption

 

TRH is essential for the survival of most animals in cold environments and TRH secretion by the hypothalamus is increased during cold. Moreover the NE system plays a crucial role in cold-induced augmentation of TRH secretion and in increased thermogenesis during leptin rise as a response to consume more calories.  TRH neurons in the PVN receive dense NE innervations. We study the mechanisms whereby cold and NE enhance mature TRH production through processing of its precursor.

 

Prolactin

 

Suckling increases preproTRH mRNA in hypothalamic paraventricular neurons (PVN) and also markedly increases TRH release during the first period of lactation.  Our laboratory has recently shown that lactation alters preproTRH processing resulting in the generation of novel proTRH-derived peptides with prolactin secretion activity. We are studying the receptor and signal transduction pathway for these molecules.

 

Tissue-specific processing of proTRH in the brain

 

ProTRH is differentially processed in the brain suggesting distinct roles for TRH and other non-TRH proTRH-derived peptides as neurotransmitters and neuromodulators. We investigate the potential biologic role of these peptides under different physiological conditions.

 

Projects available:  Prothyrotropin releasing hormone processing and sorting

                                  Progrowth hormone releasing hormone processing and sorting

                                  Leptin and other regulatory peptides regulation of the hypothalamic pituitary thyroid axis

                                  Stimulation of prolactin biosynthesis by novel peptides

                                

 

 

 

 

 

 

Selected Publications:

 

Nillni EA, Lee A, Legradi G, Lechan RM, Effect of precipitated morphine withdrawal on post-translational processing of prothyrotropin releasing hormone (ProTRH) in the ventrolateral column of the midbrain periaqueductal gray. J Neurochem 2002 Mar;80(5):874-84

 

Nillni EA, Aird F, Seidah NG, Todd RB, Koenig J,  PreproTRH178-199 and two novel peptides (pFQ7 and pSE14) derived from its processing, which are produced in the paraventricular nucleus of the rat hypothalamus, are regulated during suckling, Endocrinology 2001, 142, 896-906.

 

Harris M, Aschkenasi C, Elias CF, Chandrankunnel A, Nillni EA, Bjorbaek C,

Elmquist JK, Flier JS, Hollenberg AN. Transcriptional regulation of the thyrotropin-releasing hormone gene by leptin and melanocortin signaling., J Clin Invest 2001, 107(1):111-120.

 

Nillni EA, Vaslet C, Harris M, Hollenberg A, Bjorbak C, Flier JS. 

Leptin Regulates Prothyrotropin-releasing Hormone Biosynthesis.Evidence for direct and indirect pathways. J Biol Chem. 2000, 275(46):36124-36133.

 

Nillni EA, Steinmetz R, Pescovitz OH. Posttranslational processing of progrowth hormone-releasing hormone.  Endocrinology. 1999 Dec;140(12):5817-27.

                     

Nillni EA, Sevarino KA.  The biology of pro-thyrotropin-releasing hormone-derived peptides.

Endocr Rev. 1999 Oct;20(5):599-648. Review.

 

Nillni EA. Neuroregulation of ProTRH biosynthesis and processing.

Endocrine. 1999 Jun;10(3):185-99. Review.

 

Schaner P, Todd RB, Seidah NG, Nillni EA. Processing of prothyrotropin-releasing hormone by the family of prohormone convertases.  J Biol Chem. 1997 Aug 8;272(32):19958-68.

 

Nillni EA, Luo LG, Jackson IM, McMillan P.  Identification of the thyrotropin-releasing hormone precursor, its processing products, and its coexpression with

convertase 1 in primary cultures of hypothalamic neurons: anatomic distribution of PC1 and PC2. Endocrinology. 1996 Dec;137(12):5651-61.