Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:Q9UIJ5 (Rec)
 58,342 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have recently identified a region, N-terminus residues 9-30, in the extracellular domain of the follicle-stimulating hormone (FSH) receptor capable of binding FSH, but not luteinizing hormone (LH) or thyroid-stimulating hormone (FSH) (Dattatreyamurty and Reichert (1992) Mol. Cell. Endocrinol. 87, 9-17). The objectives of the present study were to examine the interaction between a synthetic peptide corresponding to this receptor sequence and the beta-subunit of FSH, and to identify which FSH-beta regions are involved in the interaction. FSH-beta subunit and synthetic FSH-beta peptides 1-15, 71-85 and 101-111 effectively bound 125I-labeled FSH rec-(9-30) peptide, and binding was inhibited by excess unlabeled FSH receptors. Scatchard analysis indicated that the synthetic FSH-beta peptides had affinities for FSH rec-(9-30) peptide in the order of 10(6) M-1 (Ka), with the sum of individual peptide affinities (Ka = 1.21 x 10(7) M-1) closely approximating that of the intact beta-subunit (1.02 x 10(7) M-1). Polyclonal antibodies raised against FSH rec-(9-30) peptide completely inhibited the binding of 125I-labeled receptor peptide to hFSH, hFSH-beta, and hFSH-beta peptides 1-15, 71-85 and 101-111. Our results indicate that recognition of FSH-beta by N-terminus region (9-30) of the FSH receptor involves contact with residues in three discontinuous binding regions on FSH-beta.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Identification of regions of the follitropin (FSH) beta-subunit that interact with the N-terminus region (residues 9-30) of the FSH receptor. 831 32

Recombinant human TSH (rec-hTSH; Thyrogen, lot M-17073) obtained from transformed Chinese hamster ovary cells was tested for both radioiodination and preparation of a secondary standard used in RIA and immunoradiometric assay (IRMA) for routine clinical investigation. Results were compared to those obtained with high quality pituitary TSH (pit-hTSH; Dr. P. Torjesen, Oslo, Norway; and NIDDK, Rockville, MD), traditionally used in these assays. After extensive characterization and testing, it was found that [125I]rec-hTSH matched all binding and chromatographic criteria usually obtained with [125I]pit-hTSH, including Stokes' radius, labeling, and storage stability, and did not introduce any significant bias when used in the measurement of unknown serum samples. A preparation of rec-hTSH was calibrated against a local secondary standard as well as against two well known international reference preparations (NIDDK hTSH RP-1 and WHO International Reference Preparation 80/558) by IRMA and RIA. In the RIA, NIDDK anti-hTSH-3 polyclonal antibody was used, whereas in the IRMA, two commercial preparations were used: a monoclonal antibody as the detecting antibody, and a polyclonal antibody as the capture antibody. In both assays, the recombinant standard preparation yielded good fit displacement curves, showing significant parallelism compared to pit-hTSH and therefore allowing an unbiased measurement of unknown serum samples. The specific activity of the rec-hTSH preparation calibrated against the WHO International Reference Preparation was 7.7 IU/mg protein when measured by IRMA and 7.1 IU/mg when measured by RIA. In conclusion, these results indicate for the first time that rec-hTSH can fully replace pit-hTSH as both standard and tracer in diagnostic in vitro systems such as RIA and IRMA, suggesting that other recombinant glycosylated hormones might also serve for immunoassay reagent preparation.
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PMID:The use of recombinant human thyrotropin produced by Chinese hamster ovary cells for the preparation of immunoassay reagents. 855 Jul 60

The hypophyseal pars tuberalis (PT) has been the focus of numerous studies attempting to understand its physiological role in the reproductive regulation and modulation by the neuroendocrine system. Ultrastructural studies of the PT in a number of species have shown that it consists of a well-developed hypophyseal area with important secretory activity, demonstrated by the abundance of secretory granules in the cytoplasm and the marked blood irrigation. This article describes ultrastructural and immunocytochemical aspects of the PT in viscachas captured in their habitat. The cell types identified were PT-specific cells, agranulated cells, and Folliculostellate cells. PT-specific cells are divided into type I and II. Type I cells have cytoplasms with secretory granules of 150-500 nm diameter. The secretory granules of type II PT-specific cells are 65-200 nm in diameter. Both cellular types exhibit numerous nerve endings on the plasmatic membranes. Agranulated cells exhibit nuclei with lax chromatin, mitochondria, phagosomes, scarce Golgi complex, and rough endoplasmic reticulum. Folliculostellate cells exhibit an irregularly shaped and moderately condensed nucleus. All the described cellular types exhibit deposits of cytoplasmic glycogen. The immunocytochemical study revealed the presence of cells immunostained for LH-beta and FSH-beta in the PT caudal zone. ACTH was only detected in the zona tuberalis. No staining was observed with antiprolactin, anti-TSH-beta, and anti-GH sera. Folliculostellate cells exhibited staining with anti-S-100. The results demonstrate that the viscacha PT is a hypophyseal zone with specific cellular types, which exhibits evident secretory activity. The presence of nerve endings suggests neural control of the function of PT cells.
Anat Rec A Discov Mol Cell Evol Biol 2005 May
PMID:Ultrastructural and immunocytochemical studies of the viscacha (Lagostomus maximus maximus) pituitary pars tuberalis. 1579 82