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PubMed1998

Characterization of the heat shock response in the gills of sea lampreys and a brook lamprey at different intervals of their life cycles.

The heat shock response (HSR) was characterized in the gills of two lamprey species that differ with respect to their adult life history. In vivo labelling with [35S]methionine revealed an enhanced synthesis of heat shock proteins (HSPs) having approximate molecular weights of 70 kDa (HSP70) and 90 kDa (HSP90) following heat treatment. Induction of the HSR occurred in larval lampreys (ammocoetes) following temperature elevations of 13-16 degrees C for the parasitic species, the sea lamprey (Petromyzon marinus) and 16-20 degrees C for the nonparasitic species, the brook lamprey (Lampetra appendix). The case in L. appendix represents the greatest increase in temperature required to induce the HSR in gill tissue among aquatic poikilotherms studied to data and induction occurs within a temperature range (25-29 degrees C) not normally experienced by these animals. Western blotting detected the presence of 70 and 90 kDa HSPs and HSP70 levels were greater in post-metamorphic L. appendix than in ammocoetes both before and after heat shock. The HSR of lampreys appears to be induced during times of emergency when large, rapid temperature increases are experienced. The high set-point temperature for induction of the response may be a consequence of both the environments they presently inhabit and their experiences during evolution.

Animals↗
PubMed1983

Concentration of triiodothyronine in the sera of the sea lamprey, Petromyzon marinus, and the brook lamprey, Lampetra lamottenii, at various phases of the life cycle.

Triiodothyronine (T3) was measured by double antibody radioimmunoassay in the sera of individuals of all stages of the life cycle in the sea lamprey, Petromyzon marinus, and in larval (ammocoetes) and metamorphosing individuals of the brook lamprey, Lampetra lamottenii. There was no significant difference in results from the two species. Although serum T3 concentration did not vary significantly in ammocoetes maintained at the same temperature throughout the year, concentrations in ammocoetes displayed an inverse response to fluctuations in water temperature. Ammocoetes maintained at temperatures of 7 to 10 degrees and 19 to 21 degrees exhibited significantly different circulating T3 levels of 2400 and 1550 ng dl-1, respectively. Therefore, it is expected that there may be some seasonal variation in the levels of the hormone in ammocoetes in their natural environment. A precipitous collapse of the serum levels of T3 was observed by an early stage of metamorphosis (100 ng dl-1) and no significant difference in levels was observed throughout the remaining period of this phase. Young parasitic adults and adult lampreys collected during their spawning migration (upstream migrants) exhibited circulating T3 concentrations of 40 and 30 ng dl-1, respectively. T3 levels in some upstream migrants were below the limit of detection (less than 5 ng dl-1). The metamorphic decline in serum T3 may simply mark the beginning of the lower T3 levels that characterizes the adult serum.

Animals↗
PubMed1995

Urotensin II from the river lamprey (Lampetra fluviatilis), the sea lamprey (Petromyzon marinus), and the paddlefish (Polyodon spathula).

Urotensin II was isolated from extracts of the whole brain of the river lamprey (Lampetra fluviatilis) and the sea lamprey (Petromyzon marinus). The primary structure of the peptide from both species is the same (Asn-Asn-Phe-Ser-Asp-Cys-Phe-Trp-Lys-Tyr-Cys-Val) and this amino acid sequence is identical to that of urotensin II from the dogfish and skate. Consistent with previous morphological studies indicating that the Agnatha lack a caudal neurosecretory system, urotensin II was not detected in an extract of P. marinus spinal cord. The data suggest that the urotensin II may have functioned in the earliest vertebrates as a neurotransmitter/neuromodulator in the central nervous system rather than as a neurohormone of the caudal neurosecretory system. Urotensin II was also isolated from an extract of the spinal cord of a chondrostean fish, the paddlefish (Polyodon spathula). The primary structure of the paddlefish urotensin II (Gly-Ser-Thr-Ser-Glu-Cys-Phe-Trp-Lys-Tyr-Cys-Val) is the same as that of another chondrostean, the sturgeon (Acipenser ruthenus). The study provides further evidence for a widespread distribution of urotensin II in vertebrate species and suggests that the primary structure of the peptide is better conserved in these phylogenetically ancient fish than in teleosts.

Amino Acid Sequence↗
PubMed2004

In situ characterization of gonadotropin- releasing hormone-I, -III, and glutamic acid decarboxylase expression in the brain of the sea lamprey, Petromyzon marinus.

The distribution of lamprey gonadotropin-releasing hormone (GnRH)-I and -III has been extensively characterized by immunocytochemistry in the forebrain of the sea lamprey, Petromyzon marinus. However, the cellular location of lamprey GnRH-III mRNA expression by in situ hybridization in the lamprey brain has not been determined. We show for the first time the location of expression of lamprey GnRH-III, as well as provide a more comprehensive in situ study of lamprey GnRH-I and glutamic acid decarboxylase (GAD; GABA-synthesizing enzyme) mRNA expression in the brain of the lamprey in different reproductive life stages. Colorimetric and dual-label fluorescent amplification methods of in situ hybridization were used on brain tissue sections of adult, juvenile, and larval sea lamprey. In each life stage of the lamprey, expression of lamprey GnRH-I was shown in the preoptic area (POA) and the hypothalamus forming the characteristic arc-like cell population extending from the preoptic nucleus (NPO) to the neurohypophysis. Lamprey GnRH-III expression was also seen in the POA of each life stage in close proximity to lamprey GnRH-I mRNA containing neurons. GAD expression was shown in distinct cell clusters in and around the POA, in the olfactory bulb, in the dorsal thalamus beneath the habenular region, and also in the ventral-medial hypothalamus stretching from the periventricular region to the anterior portion of the rhombencephalon. Using dual-label in situ hybridization, we have shown that lamprey GnRH-I and -III mRNA are colocalized in the same cells in the POA in adult lampreys. Dual-label in situ hybridization also showed close proximity of GAD mRNA containing neurons and GnRH containing neurons in the POA. These data suggest that gamma-aminobutyric acid (GABA) may directly affect GnRH release in the brain of the sea lamprey.

Animals↗
PubMed2002

Angiotensin converting enzyme-like activity in tissues from the river lamprey or lampern, Lampetra fluviatilis, acclimated to freshwater and seawater.

Angiotensin converting enzyme (ACE) or kininase II is a dipeptidyl-carboxypeptidase that converts angiotensin I (Ang I) to angiotensin II (Ang II) in the renin-angiotensin system (RAS) and inactivates bradykinin in the kallikrein-kinin system (KKS). Angiotensin converting enzyme-like activity (ACELA) has been demonstrated in a wide range of vertebrates, and only in lampreys is a lack of ACELA still suggested. Though long controversial, a lamprey RAS has recently been identified by isolation and sequencing of lamprey Ang I and the measurement of circulating plasma angiotensins. We therefore re-investigated the presence of ACE in tissues from the river lamprey or lampern, Lampetra fluviatilis, using a highly sensitive fluorimetric assay. Significant detection of ACELA was found in a wide range of lamprey tissues (brain, gill, gonad, gut, heart, liver, skeletal muscle, skin, kidney, and plasma). The mammalian ACE inhibitor captopril at 10(-5)M was an effective, but variable inhibitor of the ACELA found in most lamprey tissues. The brain contained the highest ACELA, while kidney (including urinary duct), skin, gonads, and heart only contained very low ACELA. In most tissues, ACELA was similar in lampreys acclimated to freshwater (FW) and seawater (SW). However, gut ACELA was significantly higher in lampreys acclimated to SW than in FW-acclimated lampreys. Liver, skin, and gonad ACELA was significantly lower in lampreys acclimated to SW than in FW lampreys. Male and female lampreys acclimated to FW showed similar ACELA in all tissues except the kidney (including the urinary duct), where ACELA was significantly higher in male than in female lampreys. These results indicate that ACELA, a component of the RAS and KKS, is present in tissues from one of the earliest evolved groups of vertebrates.

Adaptation, Physiological↗
PubMed2005

Comparison of synthesis of 15 alpha-hydroxylated steroids in males of four North American lamprey species.

Recent studies have provided evidence that 15 alpha-hydroxytestosterone (15 alpha-T) and 15 alpha-hydroxyprogesterone (15 alpha-P) are produced in vitro and in vivo in adult male sea lampreys (Petromyzon marinus), and that circulatory levels increase in response to injections with gonadotropin-releasing hormone (GnRH). We examined four species from the Petromyzontidae family including silver lampreys (Ichthyomyzon unicuspis), chestnut lampreys (I. castaneus), American brook lampreys (Lethenteron appendix), and Pacific lampreys (Entosphenus tridentatus) to determine if these unusual steroids were unique to sea lampreys or a common feature in lamprey species. In vitro production was examined through incubations of testis with tritiated precursors, and 15 alpha-T and 15 alpha-P production was confirmed in all species through co-elution with standards on both high performance liquid chromatography (HPLC) and thin layer chromatography. In vivo production was proven by demonstrating that HPLC-fractionated plasma had peaks of immunoreactive 15 alpha-T and 15 alpha-P that co-eluted with standards through using previously developed radioimmunoassays for 15 alpha-T and 15 alpha-P. The possible functionality of 15 alpha-T and 15 alpha-P was further examined in silver and Pacific lampreys by investigating the effect of injection of either type of lamprey GnRH on plasma concentrations of 15 alpha-T and 15 alpha-P. Injections with exogenous GnRH did not affect circulatory levels of either steroid in silver lampreys, and only GnRH III elicited higher levels of both steroids in Pacific lampreys. The 15 alpha-hydroxylase enzyme(s) for steroids appeared to present in adult males of all species examined, but the question of whether 15 alpha-hydroxylated steroids are functional in these lamprey species, and the significance of the 15-hydroxyl group, requires further research.

Animals↗
PubMed2003

HPLC and ELISA analyses of larval bile acids from Pacific and western brook lampreys.

Comparative studies were performed on two native lamprey species, Pacific lamprey (Lampetra tridentata) and western brook lamprey (Lampetra richardsoni) from the Pacific coast along with sea lamprey (Petromyzon marinus) from the Great Lakes, to investigate their bile acid production and release. HPLC and ELISA analyses of the gall bladders and liver extract revealed that the major bile acid compound from Pacific and western brook larval lampreys was petromyzonol sulfate (PZS), previously identified as a migratory pheromone in larval sea lamprey. An ELISA for PZS has been developed in a working range of 20 pg-10 ng per well. The tissue concentrations of PZS in gall bladder were 127.40, 145.86, and 276.96 micro g/g body mass in sea lamprey, Pacific lamprey, and western brook lamprey, respectively. Releasing rates for PZS in the three species were measured using ELISA to find that western brook and sea lamprey released PZS 20 times higher than Pacific lamprey did. Further studies are required to determine whether PZS is a chemical cue in Pacific and western brook lampreys.

Animals↗
PubMed1984

Purification of a lamprey complement protein homologous to the third component of the mammalian complement system.

A lamprey protein homologous to the third component of mammalian complement was isolated from lamprey plasma and was tentatively designated lamprey C3. Lamprey C3 is a major protein in lamprey serum with electrophoretic mobility of beta-globulin and with m.w. of 190,000. It consists of three polypeptide chains (84,000-alpha, 74,000-beta, and 32,000-gamma chains) linked by disulfide bonds. The protein retains a unique internal thiolester bond on the alpha-chain that is cleaved on methylamine treatment or on limited proteolysis with trypsin. Lamprey C3 by itself could not bind to zymosan or rabbit red cells, but it could covalently bind to these substances when activated by other factors present in lamprey serum. The binding of lamprey C3 to activating surfaces is mediated by covalent bonds and is accompanied by limited proteolysis of the alpha-chain. A fragment with an m.w. of 35,000 containing the internal thiolester site was isolated from methylamine-treated lamprey C3 bound to activated thiol-Sepharose by extensive tryptic digestion followed by dithiothreitol treatment. Lamprey C3 functions as the essential factor in phagocytosis of rabbit red cells by lamprey phagocytes. However, it is not involved in naturally occurring hemolytic activity in lamprey serum.

Animals↗
PubMed2006

Shifting patterns of nitrogen excretion and amino acid catabolism capacity during the life cycle of the sea lamprey (Petromyzon marinus).

The jawless fish, the sea lamprey (Petromyzon marinus), spends part of its life as a burrow-dwelling, suspension-feeding larva (ammocoete) before undergoing a metamorphosis into a free swimming, parasitic juvenile that feeds on the blood of fishes. We predicted that animals in this juvenile, parasitic stage have a great capacity for catabolizing amino acids when large quantities of protein-rich blood are ingested. The sixfold to 20-fold greater ammonia excretion rates (J(Amm)) in postmetamorphic (nonfeeding) and parasitic lampreys compared with ammocoetes suggested that basal rates of amino acid catabolism increased following metamorphosis. This was likely due to a greater basal amino acid catabolizing capacity in which there was a sixfold higher hepatic glutamate dehydrogenase (GDH) activity in parasitic lampreys compared with ammocoetes. Immunoblotting also revealed that GDH quantity was 10-fold and threefold greater in parasitic lampreys than in ammocoetes and upstream migrant lampreys, respectively. Higher hepatic alanine and aspartate aminotransferase activities in the parasitic lampreys also suggested an enhanced amino acid catabolizing capacity in this life stage. In contrast to parasitic lampreys, the twofold larger free amino acid pool in the muscle of upstream migrant lampreys confirmed that this period of natural starvation is accompanied by a prominent proteolysis. Carbamoyl phosphate synthetase III was detected at low levels in the liver of parasitic and upstream migrant lampreys, but there was no evidence of extrahepatic (muscle, intestine) urea production via the ornithine urea cycle. However, detection of arginase activity and high concentrations of arginine in the liver at all life stages examined infers that arginine hydrolysis is an important source of urea. We conclude that metamorphosis is accompanied by a metabolic reorganization that increases the capacity of parasitic sea lampreys to catabolize intermittently large amino acid loads arising from the ingestion of protein rich blood from their prey/hosts. The subsequent generation of energy-rich carbon skeletons can then be oxidized or retained for glycogen and fatty acid synthesis, which are essential fuels for the upstream migratory and spawning phases of the sea lamprey's life cycle.

Amino Acids↗
PubMed1995

Glial cells of the lamprey nervous system contain keratin-like proteins.

Lamprey axons regenerate following spinal cord transection despite the formation of a glial scar. As we were unable to detect a lamprey homologue of glial fibrillary acidic protein (GFAP), a major constituent of astrocytes, we studied the composition of intermediate filament (IF) proteins of lamprey glia. Monoclonal antibodies (mAbs) were raised to lamprey spinal cord cytoskeletal extracts and these mAbs were characterized by using Western blotting and immunocytochemistry. On two-dimensional (2-D) Western blots, five of the mAbs detected three major IF polypeptides in the molecular weight (MW) range of 45-56 kD. Further studies were conducted to determine the relationship between the lamprey glial-specific antigen and other mammalian IF proteins. Antikeratin 8 antibody recognized two of the three polypeptides. Several of the glial-specific mAbs reacted with human keratins 8 and 18 on Western blots. Keratin-like immunoreactivity was found in all parts of the central and peripheral nervous systems in both larval and adult lampreys. The immunocytochemical staining patterns of glial-specific mAbs were indistinguishable on lamprey spinal cord sections. However, on brain sections, two distinct patterns were observed. A subset of mAbs stained only a few glial fibers in the brain, whereas others stained many more brain glia, particularly the ependymal cells. The former group of mAbs recognized only the two lower MW polypeptides on 2-D Western blots, but the latter group of mAbs recognized all three major IF polypeptides. This correlation is supported by the observation that the highest MW IF polypeptide has an increased level of expression in the brain relative to the spinal cord. Thus, in the lamprey, the glial cells of both spinal cord and brain express molecules similar to simple epithelial cytokeratins, but their IFs may contain these keratins in different stoichiometric proportions. The widespread presence in the lamprey of primitive glial cells containing keratin-like intermediate filaments may have significance for the extraordinary ability of lamprey spinal axons to regenerate.

Animals↗
PubMed2004

Evidence that petromyzontid lampreys employ a common migratory pheromone that is partially comprised of bile acids.

This study examined whether the larval pheromone employed by adult sea lamprey (Petromyzon marinus) to locate spawning streams and known to be at least partially comprised of bile acids is also employed by other lamprey species. Both production and release of lamprey-specific bile acids, and sensitivity to them were examined in a wide variety of species. High pressure liquid chromatography and electrospray ionization/mass spectrometry (ESI-MS) found gallbladders from 10 species of European and North American lamprey to contain large quantities of petromyzonol sulfate (PS) together with much smaller quantities of allocholic acid (ACA) and petromyzonol (P). Evaluation of holding waters from three of these species using ESI-MS found all to contain large quantities of PS and lesser quantities of ACA in similar ratios. Electro-olfactogram recording from the olfactory systems of three parasitic lamprey species found all to detect PS and ACA with high sensitivity. Behavioral studies using migratory adult sea lamprey found them to be attracted to the odors of heterospecific larvae as well as conspecific larvae, both of which contained similar amounts of PS and ACA. Finally, adult silver lampreys (Ichthyomyzon unicuspis) were also found to be attracted to the odor of larval sea lamprey. Together, these results demonstrate that PS and ACA are commonly produced and released by larval petromyzontid lampreys and likely used as part of a common evolutionarily conserved pheromone. This scenario is reasonable because lampreys share similar larval and spawning habitat requirements, and their larvae derive no apparent benefit from producing compounds that serve as an attractant for adults.

Animals↗
PubMed1998

Regulation of iron metabolism in the sanguivore lamprey Lampetra fluviatilis--molecular cloning of two ferritin subunits and two iron-regulatory proteins (IRP) reveals evolutionary conservation of the iron-regulatory element (IRE)/IRP regulatory system.

Two ferritin cDNAs were cloned from the liver and spinal cord of the sanguivore lamprey Lampetra fluviatilis, an extant representative of the ancient agnathan (jawless) stage in vertebrate evolution. The deduced proteins of 20.2 kDa (H-subunit) and 20.1 kDa (M-subunit) display 73% sequence identity, and both contain the ferroxidase center characteristic of animal H-ferritin. A highly conserved iron-responsive element (IRE) was identified in the 5' untranslated region of lamprey H-ferritin. Lamprey ferritin IRE forms a specific complex with crude lamprey and rat liver extracts, and with recombinant human iron-regulatory protein (IRP-1) in an electrophoretic mobility shift assay. Furthermore, lamprey ferritin IRE competes with labeled human ferritin IRE for binding to IRP in lamprey and mammalian extracts. Two liver cDNA sequences encoding 323 residues and 101 residues of two genetically distinct lamprey IRP were amplified by PCR. Lamprey IRP-1 and IRP-2, which are 72% identical, display about 74% sequence identity to their presumed homologues in mammals. Northern blot analysis shows that two IRP transcripts of 3.6 kb and 5.8 kb are expressed in lamprey liver. Given the ancient lineage of lampreys, the results indicate that the IRE/IRP regulatory system has remained highly conserved during the evolution of vertebrates.

Amino Acid Sequence↗
PubMed2000

Multiple transcripts encoding lamprey gonadotropin-releasing hormone-I precursors.

The cDNA encoding lamprey prepro-gonadotropin releasing hormone-I (lamprey GnRH-I) has been isolated and sequenced in an agnathan, the sea lamprey, Petromyzon marinus. The lamprey GnRH-I precursor is the first identified in an ancient lineage of vertebrates and has the same overall tripartite structure as other vertebrate GnRH precursors. The amino acid sequence of lamprey GnRH-I and the processing site (Gly-Lys-Arg) are highly conserved during 500 million years of evolution with 60-70% identity compared with those of tetrapod and teleost GnRH precursors. In contrast, the GnRH associated peptide regions are markedly divergent, with less than 20% identity compared with all identified vertebrate precursors. Unlike all other known vertebrate GnRH precursors, which typically have one and in a single case two transcripts, three distinct transcripts were isolated and sequenced in lampreys. These lamprey GnRH-I transcripts, termed GAP49, GAP50 and GAP58, differed in the length of the GAP coding sequence and were demonstrated to be the products of a single gene. Analysis of the lamprey GnRH-I gene intron-2 splice junction demonstrated that alternate splicing produces the different lamprey GnRH-I transcripts. Lamprey GnRH-I is the first GnRH gene demonstrated to utilize splice sequence variants to produce multiple transcripts, which may reflect an ancestral gene regulatory mechanism.

Amino Acid Sequence↗
PubMed2006

Identification of sea lamprey GTHbeta-like cDNA and its evolutionary implications.

We have identified the first and perhaps only gonadotropin beta-like protein by cDNA cloning in sea lamprey, a member of the oldest lineage of vertebrates, the agnathans. Two pituitary gonadotropins (GTHs: follicle-stimulating hormone (FSH) and luteinizing hormone (LH)) have been identified in representative species of all classes of vertebrates except the agnathans. The present study was undertaken to identify GTH in sea lamprey, Petromyzon marinus, to gain a further understanding of the origin and evolution of reproductive pituitary hormones and their respective genes in vertebrates. Sea lamprey preGTHbeta-like cDNA was cloned from a plasmid cDNA library using an expressed sequence tag analysis. The preGTHbeta-like cDNA encoded 150 amino acids, in which the GTHbeta-like protein consisted of 134 amino acid residues. Sea lamprey GTHbeta-like protein contained 12 Cys residues and two N-glycosylation sites at homologous positions to those of FSHbeta and LHbeta. The region of the molecule that has been proposed to control receptor binding specificity (i.e., the region between the 10th and 12th Cys residues) suggests that the proposed heterodimer would be more like a FSH than a LH. Sea lamprey GTHbeta-like protein-producing cells were identified immunocytochemically in the ventral part of the proximal pars distalis of pituitary using antiserum prepared against a synthetic peptide of preGTHbeta-like protein (52-68). Intraperitoneal administration of sea lamprey GnRH-I and -III at 100 microg/g body weight (twice at a 24h interval) increased expression of GTHbeta-like protein in the pituitary of adult female sea lamprey during the final maturational period. Thus, these results are the first to demonstrate the presence of a single GTH-like system in lampreys. Because the sea lamprey GTHbeta-like protein is a clear out-group compared to those of the LH and FSH family based on phylogenic analysis, we propose that an ancestral glycoprotein hormone gave rise to only one GTH in lampreys and to the glycoprotein hormone family that gave rise to LH, FSH, and TSH during the early evolution of gnathostomes.

Amino Acid Sequence↗