Four unlabeled antibody bridge techniques: a comparison.

Ordronneau, Paul; Lindstrom, P. B.M.; Petrusz, Peter

doi:10.1177/29.12.7033366

Cited by 180 publications

(40 citation statements)

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“…The sections were washed in buffer and incubated for 1 h r each in species-specific goat anti-mouse IgG antibodies (1:120; American Qualex, La Mirada, CA) and, after another wash, mouse peroxidase-antiperoxidase complex (1:125; Sternberger Meyer Immunocytochemicals, Jarrettsville, MD). After a buffer wash and a 20 min incubation in 10% serum, the goat anti-mouse and peroxidase-antiperoxidase steps were repeated for 1 hr each in order to amplify the staining (Houser et al, 1983;Ordronneau et al, 1981). Sections were treated with 3,3'-diaminobenzidine .…”

Section: Methodsmentioning

confidence: 99%

Transient and continuous expression of NADPH diaphorase in different neuronal populations of developing rat spinal cord

Wetts

Phelps

Vaughn

1995

Developmental Dynamics

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Nitric oxide is a novel intercellular messenger whose role in neuronal development is not yet known. As a first step toward elucidating its developmental function, we examined the pattern of NADPH diaphorase histochemical staining, an indicator of the presence of nitric oxide synthase, in the rat spinal cord at pre and postnatal ages. Some types of neurons expressed diaphorase activity transiently during development. For example, a subset of somatic motor neurons, located in the ventrolateral corner of a few caudal segments of the cervical spinal cord, were diaphorase-positive beginning on E15, but gradually became diaphorase-negative by birth. In contrast, other spinal neurons expressed diaphorase activity continuously from development into adulthood. Preganglionic autonomic motor neurons became diaphorase-positive early in their development, as they were migrating toward their adult positions. Other spinal neurons, such as those in superficial dorsal horn, first expressed diaphorase relatively late in their development, after reaching their final location. The transient expression in some cell types, as well as the early expression in others, suggest that nitric oxide may have an important role(s) during development, which may differ from its functions in the adult nervous System. 0 1995 Wiley-Liss, Inc.

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Section: Methodsmentioning

confidence: 99%

Transient and continuous expression of NADPH diaphorase in different neuronal populations of developing rat spinal cord

Wetts

Phelps

Vaughn

1995

Developmental Dynamics

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“…Slides were deparaffinized and stained by using the peroxidase-antiperoxidase complex (StembergerMeyer Immunocytochemicals, Jarrettsville, MD) according to the "double PAP" method (23). The distribution of CRF was compared to that of other pancreatic hormones by localizing two antigens in the same section with contrasting chromogens (24).…”

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confidence: 99%

Corticotropin-releasing factor (CRF)-like immunoreactivity in the vertebrate endocrine pancreas.

Petrusz¹,

Merchenthaler²,

Maderdrut³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

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The light microscopic immunocytochemical localization of corticotropin-releasing factor (CRF) is described in the endocrine pancreas of several species representing the major classes of vertebrates: fishes (channel catfish, Ictalurus punctatus), amphibians (African clawed toad, Xenopu8 laevis), reptiles (chameleon, Anolis carolinensis), birds (chicken, Gallus domesticus), and several mammals (rat, mouse, cat, rhesus monkey, and man). The CRF-containing cells are scattered over the entire islet tissue in primates and cat, whereas in rat and mouse they are located at the periphery of the islets. In the chicken and catfish, the CRF-containing cells are found in a central location within islets and form larger clusters or cords. Single cells with CRF-like immunoreactivity are interspersed between acinar cells of the exocrine pancreas in all species studied. The CRF cells show a substantial topographical overlap with glucagon cells, but their precise identity and function remain to be determined.Corticotropin-releasing factor (CRF), a 41-amino acid peptide, has been isolated and characterized from extracts of ovine hypothalamus as a potent stimulator of the secretion of corticotropin (ACTH) and 3-endorphin (1-3). Immunocytochemical studies have established that most of the CRF in the hypothalamus is located both in neurons of the paraventricular nucleus and in terminals around portal capillaries of the median eminence (4-7). CRF-like immunoreactivity has been identified in hypophysial portal blood (8). The neural pathways through which CRF reaches the median eminence also have been described (9). Like other neuropeptides, CRF is widely distributed in extrahypothalamic areas of the brain, determined by both radioimmunoassay (10) and immunocytochemistry (11)(12)(13). In addition to stimulating the release of ACTH and /8-endorphin, CRF has a broad range of pharmacological effects, which include changes in behavior, heart rate, blood pressure, and in blood concentrations of epinephrine, norepinephrine, glucagon, and glucose (14-18). Thus, CRF appears to be an important regulatory peptide mediating stress-related physiological responses and predictably possessing other, hitherto unsuspected, hormone-or neurotransmitter-like activities. On the basis of current hypotheses concerning the common evolutionary origin of hormones and neurotransmitters (19)(20)(21) (Altamont, NY). One African clawed toad (Xenopus laevis) and pancreatic tissue from two channel catfish (Ictalurus punctatus) were gifts from L. J. Haverkamp (Neurobiology Program, University of North Carolina) and J. E. Brinn (Department of Anatomy, East Carolina University), respectively. Three lizards (Anolis carolinensis) were purchased from Carolina Biological Supply (Burlington, NC). Pancreatic tissue from two adult cats and two adult rhesus monkeys (Macaca mulatta) also was studied. Human pancreas (courtesy of E. K. MacRae and F. D. Dalldorf) was from a 1-year-old infant who died in an accident.Preparation of Tissues. Rat, mouse, cat, monkey, chicken, ...

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“…Moreover, it is well known that the peroxidase-DAB marker has a diameter of more than 20 nm (24) and that it penetrates some distance into the section (21). These findings suggest that the immunoperoxidase method is not adequate for the exact immunolocation of basement membrane components.…”

Section: Discussionmentioning

confidence: 99%