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Results for “Ictaluridae”

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3 recordsLinked to original sources

PubMed1978

Cerebellar afferents in teleost catfish (Ictaluridae).

The cerebellar afferents in the bullhead catfish (Teleostei) were labeled by relying on the retrograde transport of horseradish peroxidase (HRP). Retrogradely labeled neurons were seen in: spinal cord, lateral cuneate nucleus, inferior olive, reticular nuclei, vestibular nuclei, nucleus subeminentialis, n. lateralis valvulae, locus coeruleus, n. mesencephalicus dorsalis, the basal optic nuclei, and a nucleus at the isthmic level which may be equivalent to the pontine nuclei of birds and mammals. Inputs to the molecular layer arise from the inferior olive, locus coeruleus and n. lateralis valvulae in addition to subjacent granule cells. No projections to cerebellum were seen to arise from either the optic tectum or from the inferior lobe. The so-called "lobo-cerebellar" tract in teleosts was reported by Goldstein, amongst many others, who mistook the superior secondary gustatory nucleus for a deep cerebellar nucleus.

Afferent Pathways↗

PubMed1979

Biochemical studies of taste sensation--VIII. Partial characterization of alanine-binding taste receptor sites of catfish Ictalurus punctatus using mercurials, sulfhydryl reagents, trypsin and phospholipase C.

1. Taste receptors for L-alanine in the channel catfish Ictalurus punctatus have been partially characterized. The binding activity, which is localized to a sedimentable fraction (Fraction P2), was assayed with L-[3H]alanine as the ligand. 2. Addition of HgCl2 or p-mercuribenzoate to the assay at 0.1-1 mM markedly inhibited binding. The effect was not reversible and was unaffected by increased L-alanine in the binding assay. 3. The sulfhydryl reagents iodoacetate, 5,5'-dithiobis(2-nitrobenzoic acid), arsenite, and N-ethylmaleimide did not show appreciable inhibition of binding. The results suggest that the inhibitory effect of mercurials is not on specific sulfhydryl groups at alanine-binding sites. 4. Treatment of Fraction P2 with phospholipase C decreased binding activity and treatment with trypsin led to increased binding activity.

Alanine↗

PubMed2025

Use of shotgun immunoproteomics for the development of protein vaccines against Edwardsiella piscicida.

Edwardsiella piscicida is an important emerging pathogen in various cultured fish species. This study aimed to identify immunogenic E. piscicida proteins and evaluate these antigens as protein vaccines for use in aquaculture. Shotgun immunoproteomics using anti-E. piscicida serum from rainbow trout (Oncorhynchus mykiss) and channel catfish (Ictalurus punctatus) (♀) × blue catfish (Ictalurus furcatus) (♂) hybrids inoculated with formalin-killed whole-bacteria preparations identified 36 candidate immunogenic E. piscicida proteins. The chaparonin GroEL, the glycine 2TM zipper domain-containing protein (GlyZip), and coproporphyrinogen-III oxidase (COPIII) were used to orally (PO) and intra-coelomically (IC) immunize Chinook salmon (Oncorhynchus tshawytscha). Fish IC vaccinated with either GlyZip or COPIII demonstrated a slight, but non-significant, improvement in survival post-challenge with E. piscicida S11-285. Surprisingly, fish IC or PO vaccinated with GroEL displayed an anti-protective effect (RPS = -184 % and RPS = -76 %, respectively) against subsequent challenge. All IC vaccinated fish generated a strong specific antibody response against the immunizing protein, and sham vaccinated fish challenged with E. piscicida S11-285 generated a significantly higher specific antibody response to the GroEL and GlyZip proteins than negative control fish, suggesting that shotgun immunoproteomics was effective for detection of immunogenic bacterial proteins that can stimulate humoral immune responses in the host fish.

Animals↗