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PubMed1990

B-lymphocyte populations in Xenopus laevis.

Two-color immunofluorescence technique was used to show the development and distribution of surface mu- cytoplasmic mu+ (s mu- c mu+) pre-B, s mu+ B- and s mu+ cIg+ plasma cells in metamorphic, postmetamorphic, and adult Xenopus. Generation of pre-B cells was evident in hematopoietic liver and spleen, but not in bone marrow, thymus, and duodenal mucosa. Surface immunoglobulin positive small lymphocytes were the most abundant in the spleen while plasma cells were detected in the thymus, duodenal mucosa, spleen, and liver. We had shown previously the appearance of s mu- c mu+ pre-B cells in the liver of Xenopus larvae at developmental stage 46 and later at stage 49 in the spleen. The frequency of pre-B cells dropped to zero at stage 58, the climax of metamorphosis. Pre-B cells start to reappear slowly as a second wave, at stage 60 through early postmetamorphic life in the liver and spleen. The percentage of surface Ig+ (sIg+) cells in the spleen of developing animals from stage 60 onward is comparable to that observed in adult life. In adult animals, the periphery of the liver continues to be active in hematopoiesis and contains some IgM producing plasma cells and rare sIg+ small lymphocytes while the pre-B cells are almost nonexistent in this region. The spleen, which is also active in some hematopoiesis, constitutes the main site of B-cell differentiation. Three ontogenic stages of pre-B, B-, and plasma cells are present in this organ. Pre-B and plasma cells are of low density and heterogeneous in size while small sIg+ B lymphocytes are of high density and much more homogeneous in size. The bone marrow in these lower anuran amphibia is rudimentary and is not a lymphopoietic tissue; in adult animals it is active only in differentiation of neutrophilic granulocytes.

Animals↗
PubMed1993

Antibody dependent haemolysin, complement and opsonin in sera of a major carp, Cirrhina mrigala and catfish, Clarias batrachus and Heteropneustes fossilis.

The present communication is a continuation of our earlier study on the natural serum haemagglutinin/lectins of Cirrhina mrigala, Clarias batrachus and Heteropneustes fossilis. Sera of Cirrhina mrigala, belonging to the major carp family, could not only agglutinate heterologous rabbit erythrocytes, but also lyse them spontaneously. This lysis of rabbit RBC by Cirrhina mrigala sera was calcium ion dependent and heat sensitive, indicating thereby that the haemolysis was mediated by the fish serum complement system via the classical pathway. Quantification of CH50 and APCH50 levels in the sera of Clarias batrachus and Heteropneustes fossilis as well as in the sera of amphibia, aves and mammals showed that lower vertebrates predominantly possessed an alternative pathway of the complement system, while on the other hand, in the higher vertebrates the major pathway of complement activation was classical. Furthermore sera of Clarias batrachus and Heteropneustes fossilis had opsonins, which could stimulate heterologous rat peritoneal macrophages to engulf Staphylococcus aureus with the production of superoxide anion. From this study we concluded that fishes have been armed with various powerful natural humoral defense systems for their protection against environmental pathogens.

Animals↗
PubMed1988

Characterization of an IgY-like low molecular weight immunoglobulin class in the Mexican axolotl.

The general thinking about the phylogenic distribution of vertebrate Ig classes is that fish and urodele amphibians are only able to synthesize polymeric IgM-like molecules and that the emergence of a new class of LMW Ig occurs for the first time in anouran species. Following immunization of the Mexican axolotl (Ambystoma mexicanum, Amphibia, Urodela) with TNP-SRBC, HMW anti-TNP antibody molecules are only detected. We have previously shown that these polymeric Ig are constituted of 76 kDa H-chains associated to 27-30 kDa L-chains, respectively recognized by MAbs 33.45.1 and 33.101.2. However, the euglobulin fraction purified from normal axolotl serum contains, beside HMW Ig, abundant 172 kDa molecules which are recognized by MAb 33.101.2 in Western blotting in non-reducing conditions but are not labelled with MAb 33.45.1. In the present work, we characterize this 172 kDa molecule as a LMW Ig which differs from the HMW Ig both at the level of the physicochemical and antigenic properties of their H-chain components. This new 11.9 S axolotl Ig presents some similarities with anouran IgY. The detection of IgY-like molecules in urodele amphibian extends the occurrence of at least two antigenically different H-chain isotypes to all the representative modern classes of the Tetrapoda superclass.

Ambystoma↗
PubMed1982

Extract from brain stimulates neurite outgrowth from fetal rat retinal explants.

Explants from rat fetal retina were placed in culture and assayed for fiber outgrowth. In contrast to results obtained with lower vertebrates, nerve growth factor (NGF) does not seem to play a role in this system: NGF is not able to stimulate fiber outgrowth and antibodies to NGF do not block the spontaneously occurring fiber outgrowth. However, an extract prepared from pig brain is able to stimulate fiber outgrowth in a dose-dependent manner. It is suggested that such an extract can be used as a source of putative neurotrophic factors exhibiting in the mammalian central nervous system (CNS) an action similar to that of NGF in the peripheral nervous system (PNS) of mammals and in the CNS of lower vertebrates like fishes and amphibia.

Animals↗
PubMedDate not supplied

On the presence of nucleus ruber in the urodele Salamandra salamandra and the caecilian Ichthyophis kohtaoensis.

The presence of nucleus ruber in urodeles and caecilians (amphibia) was investigated. For that purpose, horseradish peroxidase was applied to the rostral spinal cord, the medulla oblongata at various levels and the dorsolateral funiculus. Whereas Salamandra salamandra possesses a rubrospinal tract, it is absent in the limbless caecilian Ichthyophis kohtaoensis.

Amphibians↗
PubMed1992

Isolation and primary structure of an amphibian neurotensin.

Using a radioimmunoassay system employing an antiserum which recognises the common C-terminal tripeptide (YIL) of neurotensin (NT) and neuromedin N (NN), immunoreactivity was identified in extracts of brain (65.8 pmol/g), small intestine (44.2 pmol/g) and rectum (13.2 pmol/g) of the European common frog (Rana temporaria). No immunoreactivity was detected in extracts of stomach and skin. Reverse-phase HPLC analysis of each tissue extract resolved a single immunoreactive peptide with identical retention time in each case. The immunoreactive peptide was isolated by reverse-phase HPLC from brain extracts and an N-terminal pyroglutamyl residue was successfully removed enzymatically. The molecular mass of des(pyroglutamyl) frog NT, determined by plasma desorption mass spectroscopy, was 1440 Da. The primary structure of this peptide was determined by gas-phase sequencing and the calculated molecular mass, 1440.7 Da, was in close agreement with that derived by mass spectroscopy. The full primary structure of frog NT was established as: QSHISKARRPYIL. When compared with bovine NT, frog NT exhibits five amino acid substitutions in the N-terminal region, whereas the C-terminal hexapeptide sequence (RRPYIL), which mediates the classical biological effects of NT, is completely conserved. Amphibia thus possess a tridecapeptide NT which is analogous to that of higher vertebrates and considerable constraints on the primary structure of the C-terminal biologically-active core have existed for a vast evolutionary time span.

Amino Acid Sequence↗
PubMed1983

Specific interaction of proteins with 5 S RNA and tRNA in the 42 S storage particle of Xenopus oocytes.

During early oogenesis in amphibia, most of the 5 S RNA and tRNA is stored in a ribonucleoprotein particle that sediments at 42 S. In Xenopus laevis the 42 S particle contains two major proteins: of Mr 48 000 (P48) and 43 000 (P43). It is shown that heterogeneity in composition of the 42 S particle reflects a changing situation whereby initially, both 5 S RNA and tRNA are complexed with P48 (1 molecule 5 S RNA: 1 molecule P48; 2 or 3 molecules tRNA: 1 molecule P48), but later, tRNA becomes increasingly associated with P43 (in a 1:1 ratio) although 5 S RNA remains complexed with a cleavage product of P48. These changes relate to the eventual utilization of the excess 5 S RNA and tRNA in ribosome assembly and protein synthesis.

Animals↗
PubMed1995

IgY: clues to the origins of modern antibodies.

IgY is the functional equivalent of IgG in birds, reptiles and amphibia, but many aspects of its biology are poorly understood. Recent studies have increased awareness of the genetics and functions of this molecule, and have revealed its position as the ancestor of the uniquely mammalian antibodies IgG and IgE. Here, Greg Warr, Kathy Magor and David Higgins review current knowledge of IgY structure, function and expression in the context of the evolutionary role of this primitive immunoglobulin.

Amphibians↗
PubMed1992

Isolation and structural characterization of peptides related to alpha- and gamma-melanocyte-stimulating hormone (MSH) from the frog brain.

Peptides that are derived from the processing of proopiomelanocortin were isolated in pure form from the brain of the frog Rana ridibunda. The primary structure of the most abundant of those peptides was established as: Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val. This amino acid sequence is identical to that of mammalian and frog pituitary alpha-melanocyte-stimulating hormone (MSH) and the peptide co-eluted with synthetic desacetyl alpha-MSH, indicating that it is COOH-terminally alpha-amidated. A second component, which exhibited a shorter retention time, co-eluted with the glycine-extended form of desacetyl alpha-MSH [ACTH(1-14)]. The primary structure of the third peptide isolated in pure form from the brain extract was established as: Lys-Tyr-Val-Met-Ser-His-Phe-Arg-Trp-Asn-Lys-Phe-NH2. This sequence corresponds to Lys-gamma 1-MSH as predicted from the nucleotide sequence of frog proopiomelanocortin. The presence of substantial amounts of desacetyl alpha-MSH and Lys-gamma 1-MSH in the frog brain supports the concept that, in amphibia, melanotropins may act as neurotransmitters and/or neuromodulators as well as hormonal peptides.

Amino Acid Sequence↗
PubMed1985

Peptides of the APUD system in amphibian skins.

Methanol extracted skins from 84 species of amphibia were screened, measuring by RIAs: gastrin-CCK, VIP, calcitonin, GIP, PP and motilin. G-CCK-like immunoreactivity was found in 97.6%; VIP-like immunoreactivity in 41%; CT-like immunoreactivity in 34%; GIP-like immunoreactivity in 10%; PP-like immunoreactivity in 40% and MT-like immunoreactivity in 60% of the samples. The use of a sequence-specific radioimmunoassay and of gel-chromatography confirmed the caerulein-CCK-8-like nature of the immunoreactive material. Detected amounts of the other peptides (VIP, CT, GIP, PP, MT) were too low for bioassay or chromatographic studies, thus leaving the question open if they are due to some kind of unspecific interferences or, most likely, to species-specificity differences of the used antisera.

APUD Cells↗
PubMed1985

Cholecystokinin and its receptors in vertebrates and invertebrates.

Recent studies have indicated that cholecystokinin (CCK) peptides have a long evolutionary history. However, whereas all vertebrates examined have been shown to contain CCK-like peptides, this has not been possible to demonstrate for all invertebrate groups. Immunostaining studies indicate that CCK peptides originate only in neurons in groups below the level of the protochordates. It seems likely that CCK gastrointestinal endocrine cells evolved first at the level of the protochordates, possibly from sensory gut neurons similar to those seen in the invertebrates. Immunochemical and biological studies of a few invertebrate CCK-like peptides suggest that those molecules are substantially different in structure from vertebrate CCKs. Gastrin appears to have evolved from CCK at the level of the appearance of amniotes in vertebrate phylogeny. In mammals, central and peripheral CCK receptors differ in specificity for CCK- and gastrin-like peptides. Comparative studies reveal that this is true for birds as well, but reptiles, amphibia, and fish brain and pancreas CCK receptors exhibit nearly identical specificity patterns. This suggests that the lower vertebrate CCK receptor is ancestral to the distinct brain and pancreas CCK receptors seen in birds and mammals.

Animals↗
PubMedDate not supplied

Chromatographic and immunological evidence for mammalian GnRH and chicken GnRH II in eel (Anguilla anguilla) brain and pituitary.

Gonadotropin-releasing hormone (GnRH) peptides in the brain and pituitary of the European eel (Anguilla anguilla) were investigated by reverse phase high performance liquid chromatography (HPLC) and radioimmunoassay with region-specific antisera. Two GnRH molecular forms were demonstrated in brain and pituitary extracts. One form eluted in the same position as synthetic mammalian GnRH on HPLC and was recognized by antibodies directed against the NH2 and COOH termini of mammalian GnRH as well as by antibodies to the middle region. The second form eluted in the same position as synthetic chicken GnRH II and was recognized by specific antibodies to this molecule. Salmon GnRH and chicken GnRH I were not detected. The occurrence of mammalian GnRH in teleost fish suggests that this molecular form is more ancient than was previously suspected and arose earlier than in primitive tetrapods, or that it has arisen in the eel through random mutation of salmon GnRH. The lack of salmon GnRH in the eel brain indicates that this molecular form is not common to all teleost species. The finding in eel brain of chicken GnRH II, which has previously been described in species of Mammalia, Aves, Reptilia, Amphibia, Osteichthyes, and Chondrichthyes, supports our hypothesis that this widespread structural variant may represent an early evolved and conserved form of GnRH.

Anguilla↗
PubMedDate not supplied

Chicken GnRH II occurs together with mammalian GnRH in a South American species of marsupial (Monodelphis domestica).

Two molecular forms of gonadotropin-releasing hormone (GnRH) were demonstrated in hypothalamic extracts of M. domestica using high performance liquid chromatography and radioimmunoassay with specific GnRH antisera. One form eluted in the same position as synthetic mammalian GnRH and was quantified equally by two mammalian GnRH antisera, while the second form coeluted with synthetic chicken GnRH II and was quantified equally with two chicken GnRH II antisera. The finding of chicken GnRH II in a South American species of marsupial, which has previously been reported in some Australian species of marsupial and in species of Aves, Reptilia, Amphibia, Osteichthyes and Chondrichthyes, supports our hypothesis that this widespread structural variant may represent an early evolved and conserved form of GnRH.

Amino Acid Sequence↗
PubMedDate not supplied

Primary structure of frog PYY: implications for the molecular evolution of the pancreatic polypeptide family.

A peptide belonging to the pancreatic polypeptide (PP) family was isolated in pure form from the intestine of the European green frog (Rana ridibunda). The primary structure of the peptide was established as: Tyr-Pro-Pro-Lys-Pro-Glu-Asn-Pro-Gly-Glu10-Asp-Ala- Ser-Pro-Glu-Glu-Met-Thr-Lys-Tyr20-Leu-Thr-Ala-Leu-Arg-His-Tyr-Ile- Asn-Leu30-Val - Thr-Arg-Gln-Arg-Tyr-NH2. This amino acid sequence shows moderate structural similarity to human PYY (75% identity) but stronger similarity to the PP family peptides isolated from the pancreas of the salmon (86%) and dogfish (83%). The data suggest that the two putative duplications of an ancestral PP family gene that have given rise to PP, PYY and NPY in mammals had already taken place by the time of the appearance of the amphibia. In fish, however, only a single duplication has occurred, giving rise to NPY in nervous tissue and a PYY-related peptide in both pancreas and gut.

Amino Acid Sequence↗
PubMed1983

Comparative and scaling aspects of heart and body weights with reference to blood supply of cardiac fibers.

Relative heart weight (RHW) differs in vertebrates with the ratio 1:20 between extremes (bottom bound fishes--Pleuronectidae--and birds). When plotting heart weight (HW) against body weight (BW) one obtains channels which contain not only vertebrates of the same classes (poikilotherms, small and big mammals and birds) but also animals belonging to different classes: tuna fish data are located in the "small mammalian channel" together with data of large tropical snakes while large mammals (upwards 4000 g) belong to the "bird channel". Reasons for such groupings are not clear and physical activity seems not to be the only reason. When comparing active and non active vertebrates one finds that the RHW is as a rule greater in physically more active poikilotherms and homoiotherms. The RHW is also higher in wild than in domesticated forms the differences appearing after weaning (wild vs laboratory rat). In spongy type of myocardium the growth of cardiac fibers results in restriction of the blood flow through lacunae and the contact between endothelial cells lining growing strands of musculature probably provokes formation of capillaries. The appearance of mixed type of myocardium (outer compact and inner spongy compartments) is not bound to the water to land transition since it occurs also in some fishes; it does not occur or is rare in amphibia and is frequent in reptiles. The compact outer layer comprises a different proportion of the cardiac wall volume (5-73%). Metabolic differences were described between cardiac cells in compact and spongy compartments.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1985

Calcium paradox from cyclostome to man: a comparative study.

In seven poikilotherm species, i.e. cyclostome, Myxine glutinosa; teleosts, Gadus morrhua; Platichtys flesus; amphibia, R. pipiens; R. temporaria; Xenopus laevis; reptiles, Vipera berus. Ca paradox could not be obtained in ventricular strips at 8-12 degrees C. In similar preparations from human atria at 30 degrees C and 37 degrees, Ca paradox was obtained similarly as in other homoiotherms. In homoiotherms, lowered temperature (below 30 degrees C) has a protective effect. Viper myocardium did not display Ca paradox at 12, 22 or 32 degrees C, whereas human myocardium displayed Ca paradox even at 30 C. It is postulated that the absence of Ca paradox in poikilotherms is not due to the low temperature. In hagfish (Myxine glutinosa) the absence of Ca paradox seems to be due to the specific conditions concerning Ca exchange in the myocardial cell (large glycocalyx).

Animals↗
PubMed1986

Cobalt-dependent stimulation of sodium transport in the amphibian skin and nephron.

One to ten millimolar CoCl2, when applied to the outer surface of the apical membrane of the frog skin (Rana temporaria), reversibly increased the potential differences and short-circuit current. These observations suggest that Co2+ may control the gating system of the sodium channel. In the kidney of the newt (Triturus vulgaris), proximal reabsorption is increased under the influence of 0.5 mM CoCl2 injected into the lumen. When CoCl2 (0.5 mM) was injected into the lumen of the distal tubule of the newt kidney, Na+ and Cl- reabsorption was stimulated simultaneously Ca2+ transport was inhibited. The data obtained suggested that Co2+ may affect the state of the sodium and calcium channels of nonexcitable membranes of amphibia, and thus may be involved in the regulation of the function of the renal tubules.

Animals↗
PubMed1989

Hyperoxia decreases lung size of amphibian tadpoles without changing GSH-peroxidases or tissue peroxidation.

1. During the development of D. pictus larvae (Amphibia) in normoxia, selenium (Se) GSH-Px increased whereas non-Se GSH-Px did not change. 2. Acclimation to 60 or 100% O2 did not change Se GSH-Px or non-Se GSH-Px. 3. Hyperoxia did not change tissue peroxidation (TBA-RS) confirming the good capacity of D. pictus tadpoles for O2-adaptation. 4. Since hyperoxic induction of catalase (CAT) has been previously described in D. pictus tadpoles, it is concluded that CAT is more important than both GSH-Px for the establishment of O2-adaptation. 5. Increases of Se GSH-Px, SOD and CAT, are probably important for adaptation to the change from aquatic to aerial environment during metamorphosis in normoxia. 6. Chronic exposure to 100% O2 enormously reduced the lung size of D. pictus larvae.

Adaptation, Physiological↗