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The anatomy of sharks, rays, and chimaeras (chondrichthyans) is crucial to understanding the evolution of the cranial system in vertebrates due to their position as the sister group to bony fishes (osteichthyans). Strikingly different arrangements of the head in the two constituent chondrichthyan groups—holocephalans and elasmobranchs—have played a pivotal role in the formation of evolutionary hypotheses targeting major cranial structures such as the jaws and pharynx. However, despite the advent of digital dissections as a means of easily visualizing and sharing the results of anatomical studies in three dimensions, information on the musculoskeletal systems of the chondrichthyan head remains largely limited to traditional accounts, many of which are at least a century old. Here, we use synchrotron tomographic data to carry out a digital dissection of a holocephalan and an elasmobranch widely used as model species: the elephantfish, Callorhinchus milii, and the small‐spotted catshark, Scyliorhinus canicula. We describe and figure the skeletal anatomy of the head, labial, mandibular, hyoid, and branchial cartilages in both taxa as well as the muscles of the head and pharynx. In Callorhinchus, we make several new observations regarding the branchial musculature, revealing several previously unreported or ambiguously characterized muscles, likely homologous to their counterparts in the elasmobranch pharynx. We also identify a previously unreported structure linking the pharyngohyal of Callorhinchus to the neurocranium. Finally, we review what is known about the evolution of chondrichthyan cranial muscles from their fossil record and discuss the implications for muscle homology and evolution, broadly concluding that the holocephalan pharynx is likely derived from a more elasmobranch‐like form which is plesiomorphic for the chondrichthyan crown group. This dataset has great potential as a resource, particularly for researchers using these model species for zoological research, functional morphologists requiring models of musculature and skeletons, as well as for palaeontologists seeking comparative models for extinct taxa. [ABSTRACT FROM AUTHOR]

Abstract: The renin–angiotensin system is an enzyme-linked hormonal cascade that plays an important role in body fluid and cardiovascular regulation. The system is initiated by the action of renin on the precursor protein, angiotensinogen (AGT), whose sequence information is scarce because of its high variability among species. In the present study, we cloned AGT in chondrichthyans (elasmobranchs: Triakis scyllium, Dasyatis akajei, Leucoraja erinacea and a holocephalan: Callorhinchus milii). Homology was low among AGTs thus far identified; 25–28% between elasmobranchs and tetrapods and 33–61% even within chondrichthyans. All chondrichthyan angiotensin (ANG) II’s have a unique Pro3 instead of Val3 as seen in all other species. In addition, holocephalan ANG II has an unusual His4 instead of Tyr4. In addition, and the N-terminal amino acid, which is usually Asp1 in tetrapods and Asn1 in fishes, was highly variable (Asp, Asn or Tyr) in chondrichthyans. Molecular phylogenetic analysis showed that chondrichthyan AGT precursors are clustered into a group separated from those of tetrapods and teleosts. The AGT gene was most abundantly expressed in the liver, followed by the kidney, interrenal tissue and rectal gland of Triakis where biological actions of ANG II have been demonstrated. Collectively, we identified diversified AGT genes for the first time in chondrichthyes and showed that their ANG II’s have unique amino acid residues at positions 1, 3 and 4. High variability of ANG II sequences in chondrichthyans is discussed in relation to their unique regulatory mechanisms such as urea-based osmoregulation. [Copyright &y& Elsevier]

This study investigated vasodilator mechanisms in the dorsal aorta of the elephant fish, Callorhinchus milii, using anatomical and physiological approaches. Nitric oxide synthase could only be located in the perivascular nerve fibres and not the endothelium of the dorsal aorta, using NADPH histochemistry and immunohistochemistry. In vitro organ bath experiments demonstrated that a NO/soluble guanylyl cyclase (GC) system appeared to be absent in the vascular smooth muscle, since the NO donors SNP (10−4 mol l−1) and SIN-1 (10−5 mol l−1) were without effect. Nicotine (3 × 10−4 mol l−1) mediated a vasodilation that was not affected by ODQ (10−5 mol l−1), l-NNA (10−4 mol l−1), indomethacin (10−5 mol l−1), or removal of the endothelium. In contrast, the voltage-gated sodium channel inhibitor, tetrodotoxin (10−5 mol l−1), significantly decreased the dilation induced by nicotine, suggesting that it contained a neural component. Pre-incubation of the dorsal aorta with the calcitonin gene-related peptide (CGRP) receptor antagonist, CGRP8–37 (10−6 mol l−1) also caused a significant decrease in the nicotine-induced dilation. We propose that nicotine is mediating a neurally-derived vasodilation in the dorsal aorta that is independent of NO, prostaglandins and the endothelium, and partly mediated by CGRP. [ABSTRACT FROM AUTHOR]

Abstract: Receptor neurons in the olfactory and vomeronasal epithelia of vertebrates have dendritic specialization that is correlated to the receptor gene family they express and the G protein coupled with that receptor (in particular the G protein alpha subunit). There are not very many data in the literature about the morphological and molecular features of the olfactory epithelium of Chondrichthyes. In this work, the presence and distribution of different types of G protein alpha subunits (Gαo, Gαq and Gαolf) were investigated in the olfactory epithelium of the holocephalan Chimaera monstrosa using immunohistochemistry. Only Gαo-like immunoreactivity was detected in the microvillous receptor neurons and in numerous axon bundles of the fila olfactoria. These preliminary data are in agreement with studies showing G protein alpha subunits in elasmobranchs and support the data present in the literature about putative odorant receptor families in the sequenced genome of the holocephalan Callorhinchus milii. [Copyright &y& Elsevier]