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Protein Sci. 2002 Jul;11(7):1834-44.
The neuropeptide Y monomer in solution is not folded in the pancreatic-polypeptide fold.

Bettio A, Dinger MC, Beck-Sickinger AG.

Institute of Biochemistry, University of Leipzig, Talstrasse 33, D-04103 Leipzig, Germany.

Fluorescence-labelled analogs of NPY, a 36-amino acid peptide amide, were synthesized by solid-phase peptide synthesis and used for fluorescence-resonance energy transfer studies to investigate the conformation. Energy-transfer efficiency measurements in different media at the concentration of 10 microM are in agreement with a model of the NPY structure proposed by NMR studies (performed at millimolar concentration) in which the C-terminal part of the molecule adopts an alpha-helical conformation while the N-terminal part is flexible. According to this model, the alpha-helix is stabilized by intermolecular hydrophobic interactions because of the formation of dimers. The decrease of the peptide concentration causes a shift of the dimerization equilibrium toward the monomeric form. Energy-transfer efficiency measurements performed at lower concentrations do not support the hypothesis of the folding back of the N-terminal tail onto the C-terminal alpha-helix to yield the so-called "PP-fold" conformation. This structure is observed in the crystal structure of avian pancreatic polypeptide, a member of the NPY peptide hormone family, and it has been considered to be the bioactive one. Our results complete the structural characterization of NPY in solution at concentration ranges in which NMR experiments are not feasible. Furthermore, these results open the way to study the conformation of the receptor-bound ligand.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12070335&dopt=Abstract

Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8898-902. Epub 2002 Jun 17.
In vivo properties of an anti-GnRH Spiegelmer: an example of an oligonucleotide-based therapeutic substance class.

Wlotzka B, Leva S, Eschgfaller B, Burmeister J, Kleinjung F, Kaduk C, Muhn P, Hess-Stumpp H, Klussmann S.

NOXXON Pharma AG, Gustav-Meyer-Allee 25, 13355 Berlin, Germany.

Spiegelmers are high-affinity l-enantiomeric oligonucleotide ligands that display high resistance to enzymatic degradation compared with d-oligonucleotides. The target binding properties of Spiegelmers can be designed by an in vitro-selection process starting from a random pool of oligonucleotides. Applying this method, a Spiegelmer with high affinity (K(D) = 20 nM) for the peptide hormone, gonadotropin-releasing hormone (GnRH) was isolated. The Spiegelmer acts as an antagonist to GnRH in Chinese hamster ovary cells stably expressing the human GnRH receptor, and its activity is unchanged by linking to 40-kDa polyethylene glycol. In a castrated rat model the Spiegelmer further demonstrated strong GnRH antagonist activity, which is more pronounced and persists longer with the polyethylene glycol-linked derivative. Furthermore, in rabbits the anti-GnRH Spiegelmer was shown to have a very low, possibly negligible immunogenic potential. These studies suggest that Spiegelmers could be of substantial interest in the development of new pharmaceutical approaches against GnRH and other targets.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12070349&dopt=Abstract

Saudi Med J. 2002 Jun;23(6):651-7.
Are women at an increased risk of gestational thyrotoxicosis?

Ardawi MS, Nasrat HA, Rouzi AA, Mustafa BE.

Department of Clinical Biochemistry and Laboratory of Medicine, New Jeddah Clinic Hospital, Kingdom of Saudi Arabia. ardawimahoo.com

OBJECTIVE: To evaluate the relative importance of thyroid hormones and human chorionic gonadotropin in relation to the risk of gestational thyrotoxicosis in Saudi women living in Jeddah, Kingdom of Saudi Arabia. METHODS: A prospective study was conducted on Saudi healthy pregnant women (N=406) at 12-15 weeks of gestation and compared with healthy non-pregnant controls (N=200). Maternal serum levels of free thyroxine free triiodothyronine, thyrotropin, human chorionic gonadotropin and free b-human chorionic gonadotropin together with urinary iodine excretion were determined. Analysis of variance was used to examine differences among the groups for different variables and the Bonferroni criterion was used when significance tests were made. RESULTS: Pregnant women were classified into 2 groups according to the lower limit of serum thyrotropin levels in non-pregnant euthyroid controls at >= 0.3 mIU/L (Group one) or < 0.30 mIU/L (Group 2). Suppressed levels of serum thyrotropin (< 0.30 mIU/L) were found in 11.1% of pregnant women which was accompanied by significant increases in free thyroxine (P<0.001), free triiodothyronine (P < 0.05), human chorionic gonadotropin (P<0.001) and b-human chorionic gonadotropin (P<0.001). A significant negative correlation between serum levels of thyrotropin and that of human chorionic gonadotropin (r=-0.381, P<0.001) was observed. The relative risk of having a serum thyrotropin level of < 0.30 mIU/L was 4.89 (P<0.001) for the pregnant women examined as compared with non-pregnant controls. Approximately 5.6% of the women examined exhibited biochemical evidence of thyrotoxicosis. CONCLUSION: The results of the present study show that Saudi pregnant women are at risk of developing biochemical evidence of thyrotoxicosis during early gestation, and thus, are likely to be at greater risk of clinically evident gestational thyrotoxicosis and hyperemesis gravidarum. Genetically determined differences in the synthesis or metabolism of human chorionic gonadotropin isoforms, or both may contribute to this increased risk.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12070541&dopt=Abstract

Saudi Med J. 2002 May;23(5):529-35.
Screening for congenital hypothyroidism.

Henry G, Sobki SH, Othman JM.

Pathology Department, Security Forces Hospital, PO Box 3643, Riyadh 11481, Kingdom of Saudi Arabia. waynfh.med.sa

OBJECTIVE: To review the screening program for congenital hypothyroidism in the Riyadh Al-Kharj Hospital Programme, Riyadh, Kingdom of Saudi Arabia, and to investigate the clinical and biochemical characteristics of affected infants. METHODS: The study was carried out from 1985 to 2000 in the Clinical Chemistry Division, Department of Pathology, Riyadh Armed Forces Hospital, Kingdom of Saudi Arabia. Laboratory data and case notes of infants diagnosed with congenital hypothyroidism were used to supply the relevant data and information. RESULTS: One hundred and twenty-one thousand, four hundred and four infants were screened over a period of nearly 15 years. The overall incidence of congenital hypothyroidism was 1:2759 live births with a female: male ratio of 1.8:1. The incidence in a rural satellite hospital was 1:1538. No seasonal variation was observed. Apart from jaundice, signs and symptoms of congenital hypothyroidism were rarely present in the neonatal period. The neonatal and maternal parameters of affected infants did not differ significantly from those of other infants. The predominant cause of congenital hypothyroidism was athyreosis (45%), followed by thyroid ectopia (24%) and dyshormonogenesis (17%). The mean age at the start of treatment of infants diagnosed in the screening program was 10.3 days. CONCLUSION: The screening program based on initial measurement of thyroid stimulating hormone in cord blood captures 97% of infants born in the Riyadh Al-Kharj Hospital Programme. The incidence of congenital hypothyroidism was 1:2759 live births with a female:male ratio of nearly 2:1. Congenital hypothyroidism infants had similar neonatal parameters as other infants. No seasonality in the incidence of congenital hypothyroidism was observed. In general, affected infants were started on thyroxine very soon after birth.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12070574&dopt=Abstract

Cancer Immunol Immunother. 2002 Jul;51(5):263-70. Epub 2002 Apr 24.
Induction of Tc2 cells with specificity for prostate-specific antigen from patients with hormone-refractory prostate cancer.

Perambakam S, Xue BH, Sosman JA, Peace DJ.

Section of Hematology/Oncology (M/C 734), Room 3150, Molecular Biology Research Building, 900 S. Ashland Avenue, The University of Illinois at Chicago, Chicago, IL 60607, USA.

Prostate-specific antigen (PSA) is a potentially useful antigen for targeted T-cell immunotherapy of prostate cancer (CaP). Our laboratory has identified a synthetic nonamer peptide (PSA 146-154) homologue of PSA, which binds to the prevalent human leukocyte antigen, HLA-A2, and elicits specific cytotoxic T-lymphocyte (CTL) responses from normal individuals of the HLA-A2 phenotype. In the present study, we report on the induction of CTL from peripheral blood mononuclear cells (PBMC) of patients with hormone-refractory CaP, which exhibit the same specificity. T-cell lines were established from two patients by stimulation of PBMC with PSA 146-154 peptide in vitro. The T-cell lines exhibited specific cytolytic activity against T2 cells pulsed with PSA 146-154 peptide, but not a control HLA-A2 binding peptide (HIV-RT 476-484) via chromium release assay (CRA). The T-cell lines also showed PSA 146-154 peptide-specific IL-4 responses, but no detectable interferon-gamma (IFN-gamma) responses via enzyme-linked immuno-spot assays. Magnetic immuno-selection studies of one of the T-cell lines demonstrated that both cytolytic and interleukin-4 (IL-4) responses were mediated by CD8(+), but not by CD4(+) T cells. This Tc2 line was further characterized for the ability to recognize endogenously processed PSA epitopes. The line specifically secreted IL-4 in response to HLA-A2(+) target cells transfected to express PSA and specifically lysed the PSA(+) target cells, but not control transfected cells. The results indicate that the PSA 146-154 peptide emulates a naturally processed and presented peptide epitope of PSA that is within the T-cell repertoire of HLA-A2(+)patients with CaP.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12070713&dopt=Abstract

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