An in vitro model for evaluating peripheral regulation of growth in fish: effects of 17β-estradiol and testosterone on the expression of growth hormone receptors, insulin-like growth factors, and insulin-like growth factor type 1 receptors in rainbow trout (Oncorhynchus mykiss).

A central component of growth coordination in vertebrates is the growth hormone (GH)-insulin-like growth factor-1 (IGF-1) system. To date, most studies on the control of vertebrate growth have focused on regulation of pituitary GH production and release. In this study, we used liver, muscle, and gill tissue from sexually immature rainbow trout incubated in vitro to evaluate the extrapituitary effects of 17β-estradiol (E2) and testosterone (T) on mRNA and functional expression of growth hormone receptors (GHR), insulin-like growth factors 1 and 2 (IGF-1, IGF-2), and type 1 IGF receptors (IGFR1).

Resolving the growth-promoting and metabolic effects of growth hormone: Differential regulation of GH-IGF-I system components.

Growth hormone regulates numerous processes in vertebrates including growth promotion and lipid mobilization. During periods of food deprivation, growth is arrested yet lipid depletion is promoted. In this study, we used rainbow trout on different nutritional regimens to examine the regulation of growth hormone (GH)-insulin-like growth factor-I (IGF-I) system elements in order to resolve the growth-promoting and lipid catabolic actions of GH.

Isolation, characterization, and distribution of two cDNAs encoding for growth hormone receptor in rainbow trout (Oncorhynchus mykiss).

Growth hormone (GH) plays important roles in a vast array of physiological processes, including growth, metabolism, and reproduction. In this study, cDNAs for two unique growth hormone receptor variants were cloned and sequenced from rainbow trout. The two cDNAs, one consisting of 2920 bp and the other of 2820 bp, share 87.

Localization of cytoplasmic and extracellular domains of Na,K-ATPase by epitope tag insertion.

We have used epitope tag addition to analyze the transmembrane topology of the Na,K-ATPase catalytic (alpha) subunit. An antigenic peptide derived from the hemagglutinin (HA) of influenza virus was inserted at 15 different positions within the rat Na,K-ATPase alpha 1 subunit isoform. The functional integrity of the tagged proteins was tested by their capacity to confer ouabain resistance upon human HEK 293 cells.

An inhibitor of nuclear scaffold protease blocks chemical transformation of fibroblasts.

A nuclear scaffold (NS) protease has previously been implicated in production of the M(r) 46,000 ATP-binding protein in NS (which may acquire nucleoside triphosphatase activity and participate in nucleocytoplasmic transport) by cleavage of a subset of lamins A/C. In a preceding paper (G. Clawson, L.